angiotensin ii angii  (Millipore)


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    Structured Review

    Millipore angiotensin ii angii
    Lack of ClC-2 reduced <t>AngII-induced</t> HBVSMC proliferation. a and b Cells were transfected with ClC-2 siRNA (siClC-2; 20 nM) or negative siRNA (negative; 20 nM) for 48 h in prior to angiotensin II (AngII) treatment (10 − 7 M) for another 48 h. Cell proliferation was determined using the CCK-8 assay ( a ) and <t>BrdU</t> incorporation ( b ). c and d The protein expressions of PCNA ( c ) and Ki67 ( d ) were detected using western blotting. ** p
    Angiotensin Ii Angii, supplied by Millipore, used in various techniques. Bioz Stars score: 89/100, based on 4029 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "ClC-2 knockdown prevents cerebrovascular remodeling via inhibition of the Wnt/β-catenin signaling pathway"

    Article Title: ClC-2 knockdown prevents cerebrovascular remodeling via inhibition of the Wnt/β-catenin signaling pathway

    Journal: Cellular & Molecular Biology Letters

    doi: 10.1186/s11658-018-0095-z

    Lack of ClC-2 reduced AngII-induced HBVSMC proliferation. a and b Cells were transfected with ClC-2 siRNA (siClC-2; 20 nM) or negative siRNA (negative; 20 nM) for 48 h in prior to angiotensin II (AngII) treatment (10 − 7 M) for another 48 h. Cell proliferation was determined using the CCK-8 assay ( a ) and BrdU incorporation ( b ). c and d The protein expressions of PCNA ( c ) and Ki67 ( d ) were detected using western blotting. ** p
    Figure Legend Snippet: Lack of ClC-2 reduced AngII-induced HBVSMC proliferation. a and b Cells were transfected with ClC-2 siRNA (siClC-2; 20 nM) or negative siRNA (negative; 20 nM) for 48 h in prior to angiotensin II (AngII) treatment (10 − 7 M) for another 48 h. Cell proliferation was determined using the CCK-8 assay ( a ) and BrdU incorporation ( b ). c and d The protein expressions of PCNA ( c ) and Ki67 ( d ) were detected using western blotting. ** p

    Techniques Used: Transfection, CCK-8 Assay, BrdU Incorporation Assay, Western Blot

    2) Product Images from "Autocrine laminin-5 ligates ?6?4 integrin and activates RAC and NF?B to mediate anchorage-independent survival of mammary tumors"

    Article Title: Autocrine laminin-5 ligates ?6?4 integrin and activates RAC and NF?B to mediate anchorage-independent survival of mammary tumors

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200302023

    NF κ B activation is necessary and sufficient for anchorage-independent survival of MECs. (A and B) Cell viability was calculated using the Live/Dead assay for T4-2s (A) and T4 β4Δ cyto/V12RAC (B) MECs treated with either vehicle (Control), a peptide that inhibits nuclear translocation of NFκB SN50 (SN50), or a nonfunction-blocking peptide SN50M (SN50M) grown in rBM for 96 h with or without a function-blocking mAb to β1 integrin. (C) Cell viability calculated using the Live/Dead assay for T4-2 controls (T4-2) or T4-2s expressing a mutant IκBα (IκBαM) grown and treated as in A. (D) Confocal immunofluorescence microscopy images of Cytokeratin 18 (Texas red) and NFκB p65 (FITC) in S-1 controls (S-1) and S-1s overexpressing an exogenous NFκB p65 (S-1 p65) showing constitutive nuclear NFκB p65 in the S-1 p65 structures (arrows, nuclei as indicated by “n”). Bar, 20 μm. (E) Quantification of 100–200 representative cells assayed from images similar to D demonstrating a significant increase in nuclear NFκB p65 in S-1s overexpressing NFκB p65 (S-1 p65). (F) Cell viability was calculated using the Live/Dead assay for S-1 and S-1 cells overexpressing NFκB p65 (S-1 p65) grown and treated as described for A. (G) Soft agar assay results demonstrating overexpressing exogenous NFkB p65 (S-1 p65) permits S-1s (S-1) to form colonies in soft agar. Results for A–C and E–G are the mean ± SEM of three to five experiments. *, P ≤ 0.05; ***, P ≤ 0.001.
    Figure Legend Snippet: NF κ B activation is necessary and sufficient for anchorage-independent survival of MECs. (A and B) Cell viability was calculated using the Live/Dead assay for T4-2s (A) and T4 β4Δ cyto/V12RAC (B) MECs treated with either vehicle (Control), a peptide that inhibits nuclear translocation of NFκB SN50 (SN50), or a nonfunction-blocking peptide SN50M (SN50M) grown in rBM for 96 h with or without a function-blocking mAb to β1 integrin. (C) Cell viability calculated using the Live/Dead assay for T4-2 controls (T4-2) or T4-2s expressing a mutant IκBα (IκBαM) grown and treated as in A. (D) Confocal immunofluorescence microscopy images of Cytokeratin 18 (Texas red) and NFκB p65 (FITC) in S-1 controls (S-1) and S-1s overexpressing an exogenous NFκB p65 (S-1 p65) showing constitutive nuclear NFκB p65 in the S-1 p65 structures (arrows, nuclei as indicated by “n”). Bar, 20 μm. (E) Quantification of 100–200 representative cells assayed from images similar to D demonstrating a significant increase in nuclear NFκB p65 in S-1s overexpressing NFκB p65 (S-1 p65). (F) Cell viability was calculated using the Live/Dead assay for S-1 and S-1 cells overexpressing NFκB p65 (S-1 p65) grown and treated as described for A. (G) Soft agar assay results demonstrating overexpressing exogenous NFkB p65 (S-1 p65) permits S-1s (S-1) to form colonies in soft agar. Results for A–C and E–G are the mean ± SEM of three to five experiments. *, P ≤ 0.05; ***, P ≤ 0.001.

    Techniques Used: Activation Assay, Live Dead Assay, Translocation Assay, Blocking Assay, Expressing, Mutagenesis, Immunofluorescence, Microscopy, Soft Agar Assay

    3) Product Images from "Effect of wild bitter gourd treatment on inflammatory responses in BALB/c mice with sepsis"

    Article Title: Effect of wild bitter gourd treatment on inflammatory responses in BALB/c mice with sepsis

    Journal: Biomedicine

    doi: 10.7603/s40681-014-0017-y

    COX-2, NF-κB, and iNOS inflammatory protein expression in six groups of mice after four-week test diet, values mean ± SD of each group. Values not sharing a superscript (a-e) differ significantly by one-way ANOVA and Duncan’s Multiple Range Test ( p
    Figure Legend Snippet: COX-2, NF-κB, and iNOS inflammatory protein expression in six groups of mice after four-week test diet, values mean ± SD of each group. Values not sharing a superscript (a-e) differ significantly by one-way ANOVA and Duncan’s Multiple Range Test ( p

    Techniques Used: Expressing, Mouse Assay

    4) Product Images from "Genetically modified human placenta-derived mesenchymal stem cells with FGF-2 and PDGF-BB enhance neovascularization in a model of hindlimb ischemia"

    Article Title: Genetically modified human placenta-derived mesenchymal stem cells with FGF-2 and PDGF-BB enhance neovascularization in a model of hindlimb ischemia

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2015.4089

    hPDMSC survival in the ischemic tissue. Immunohistochemical staining with an antibody against human-specific surface of intact mitochondria protein indicated that xenografted hPDMSCs survived in the ischemic tissue for at least four weeks. Scale bar, 50 µ m; magnification ×3. hPDMSC, human placenta-derived mesenchymal stem cell. AD-F-P, adenoviral bicistronic vector containing FGF2 and PDGF-BB; ctrl, control without PDMSCs.
    Figure Legend Snippet: hPDMSC survival in the ischemic tissue. Immunohistochemical staining with an antibody against human-specific surface of intact mitochondria protein indicated that xenografted hPDMSCs survived in the ischemic tissue for at least four weeks. Scale bar, 50 µ m; magnification ×3. hPDMSC, human placenta-derived mesenchymal stem cell. AD-F-P, adenoviral bicistronic vector containing FGF2 and PDGF-BB; ctrl, control without PDMSCs.

    Techniques Used: Immunohistochemistry, Staining, Derivative Assay, Plasmid Preparation

    5) Product Images from "Limited role of regulatory T cells during acute Theiler virus-induced encephalitis in resistant C57BL/6 mice"

    Article Title: Limited role of regulatory T cells during acute Theiler virus-induced encephalitis in resistant C57BL/6 mice

    Journal: Journal of Neuroinflammation

    doi: 10.1186/s12974-014-0180-9

    Early recruitment of T cells into Theiler’s murine encephalomyelitis virus (TMEV)-infected brain in the absence of Tregs. Following intraperitoneal administration of PBS or diphtheria toxin (DT), DEREG mice were intracerebrally infected with TMEV. (A) Immunohistochemistry of TMEV infected brains at 3 days post inoculation (dpi) (left panel) and 7 dpi (right panel) reveals higher numbers of CD3 + T cells only at 3 dpi in DT-treated mice (lower panel) compared to PBS-treated mice (upper panel). (B) Quantification of CD3 + T cells in the cerebral neuroparenchyma of 6 to 8 infected mice reveals a significantly increased number on T cells in DT-treated mice at 3 dpi. Box and whisker plots display median and quartiles with maximum and minimum values. * P -value
    Figure Legend Snippet: Early recruitment of T cells into Theiler’s murine encephalomyelitis virus (TMEV)-infected brain in the absence of Tregs. Following intraperitoneal administration of PBS or diphtheria toxin (DT), DEREG mice were intracerebrally infected with TMEV. (A) Immunohistochemistry of TMEV infected brains at 3 days post inoculation (dpi) (left panel) and 7 dpi (right panel) reveals higher numbers of CD3 + T cells only at 3 dpi in DT-treated mice (lower panel) compared to PBS-treated mice (upper panel). (B) Quantification of CD3 + T cells in the cerebral neuroparenchyma of 6 to 8 infected mice reveals a significantly increased number on T cells in DT-treated mice at 3 dpi. Box and whisker plots display median and quartiles with maximum and minimum values. * P -value

    Techniques Used: Infection, Mouse Assay, Immunohistochemistry, Whisker Assay

    6) Product Images from "Critical Role for Glial Cells in the Propagation and Spread of Lymphocytic Choriomeningitis Virus in the Developing Rat Brain"

    Article Title: Critical Role for Glial Cells in the Propagation and Spread of Lymphocytic Choriomeningitis Virus in the Developing Rat Brain

    Journal: Journal of Virology

    doi: 10.1128/JVI.76.13.6618-6635.2002

    Fifty-micrometer-thick sections through the hippocampal formation immunohistochemically stained for LCMV (panels A, B, D, E, F, and G) or GFAP (panel C). LCMV infection in the hippocampus initially involves astrocytes. The granule cells of the dentate gyrus become chronically infected. (A) Low-power image of hippocampal region at PD8 shows infection within the ependyma, parenchymal cells adjacent to the ependyma (double arrowheads), and fornix (arrowhead). The dentate gyrus (arrow) is not labeled. (B) Area beneath the ependyma, represented by the box in panel A, shows that the infected cells have the morphology of astrocytes (arrowheads). (C) A section adjacent to panel B immunohistochemically labeled for GFAP, a marker for astrocytes. The GFAP-positive cells in panel C have the same morphology as the LCMV-infected cells in panel B, indicating that the infected parenchymal cells on PD8 are astrocytes. (D) By PD18, infection in the hippocampal region is less intense but still present beneath the ependyma (double arrowheads) and in the fornix (arrowhead). The dentate gyrus stratum granulosum (arrow) now shows evidence of infection. (E) Higher magnification of box in panel D shows that granule cells of the dentate gyrus (arrows), and nearby astrocytes (arrowheads) are both infected with LCMV on PD18. (F) By PD49, infection has been cleared from the hippocampal region, including the fornix (arrowhead), except for granule cells of the dentate gyrus (arrow), where viral antigen persists. (G) Higher magnification of the box in panel F demonstrates that cell bodies and dendrites of dentate granule cells (arrows) and a few hilar neurons (double arrowheads) are still infected. The virus has been cleared from glial cells. Bars, 1 mm (A, D, and F); 20 μm (B and C); 100 μm (E and G).
    Figure Legend Snippet: Fifty-micrometer-thick sections through the hippocampal formation immunohistochemically stained for LCMV (panels A, B, D, E, F, and G) or GFAP (panel C). LCMV infection in the hippocampus initially involves astrocytes. The granule cells of the dentate gyrus become chronically infected. (A) Low-power image of hippocampal region at PD8 shows infection within the ependyma, parenchymal cells adjacent to the ependyma (double arrowheads), and fornix (arrowhead). The dentate gyrus (arrow) is not labeled. (B) Area beneath the ependyma, represented by the box in panel A, shows that the infected cells have the morphology of astrocytes (arrowheads). (C) A section adjacent to panel B immunohistochemically labeled for GFAP, a marker for astrocytes. The GFAP-positive cells in panel C have the same morphology as the LCMV-infected cells in panel B, indicating that the infected parenchymal cells on PD8 are astrocytes. (D) By PD18, infection in the hippocampal region is less intense but still present beneath the ependyma (double arrowheads) and in the fornix (arrowhead). The dentate gyrus stratum granulosum (arrow) now shows evidence of infection. (E) Higher magnification of box in panel D shows that granule cells of the dentate gyrus (arrows), and nearby astrocytes (arrowheads) are both infected with LCMV on PD18. (F) By PD49, infection has been cleared from the hippocampal region, including the fornix (arrowhead), except for granule cells of the dentate gyrus (arrow), where viral antigen persists. (G) Higher magnification of the box in panel F demonstrates that cell bodies and dendrites of dentate granule cells (arrows) and a few hilar neurons (double arrowheads) are still infected. The virus has been cleared from glial cells. Bars, 1 mm (A, D, and F); 20 μm (B and C); 100 μm (E and G).

    Techniques Used: Staining, Infection, Labeling, Marker

    7) Product Images from "Input-Specific Immunolocalization of Differentially Phosphorylated Kv4.2 in the Mouse Brain"

    Article Title: Input-Specific Immunolocalization of Differentially Phosphorylated Kv4.2 in the Mouse Brain

    Journal: Learning & Memory

    doi:

    Mouse brain coronal sections. Staining for ERK triply phosphorylated Kv4.2 ( A ), carboxy-terminal PKA-phosphorylated Kv4.2 ( B ) and amino-terminal PKA-phosphorylated Kv4.2 ( C ). The right half in each brain displays immunoreactivity to the appropriate antibody, whereas the left half is representative of the immunoreactivity seen when the antibody is preincubated with its appropriate antigen. In general, staining across antibodies is strong in areas consistent with those described by the pattern of total Kv4.2 staining. Strong immunoreactivity is seen in the hippocampus, thalamus, medial habenular nucleus, striatum, amygdala, cortex, and cerebellum.
    Figure Legend Snippet: Mouse brain coronal sections. Staining for ERK triply phosphorylated Kv4.2 ( A ), carboxy-terminal PKA-phosphorylated Kv4.2 ( B ) and amino-terminal PKA-phosphorylated Kv4.2 ( C ). The right half in each brain displays immunoreactivity to the appropriate antibody, whereas the left half is representative of the immunoreactivity seen when the antibody is preincubated with its appropriate antigen. In general, staining across antibodies is strong in areas consistent with those described by the pattern of total Kv4.2 staining. Strong immunoreactivity is seen in the hippocampus, thalamus, medial habenular nucleus, striatum, amygdala, cortex, and cerebellum.

    Techniques Used: Staining

    Cortex and Cerebellum. Staining of ERK triply phosphorylated Kv4.2 ( A,D ), carboxy-terminal PKA-phosphorylated Kv4.2 ( B,E ), and amino-terminal PKA-phosphorylated Kv4.2 ( C,F ) in the cortex ( A,B,C ) and cerebellum ( D,E,F ) at 100×. In the cortex, ERK triply phosphorylated Kv4.2 antibodies show predominant staining in layer IV of the cortex with possible evidence of barrels ( A ). Carboxy-terminal PKA-phosphorylated Kv4.2 staining shows weak immunoreactivity in layers V and VI ( B ). Amino-terminal PKA-phosphorylated Kv4.2 staining displays immunoreactivity in layers IV, V, and VI with the strongest signal in layers V and VI ( C ). In the cerebellum, staining with the ERK triply phosphorylated and carboxy-terminal PKA-phosphorylated Kv4.2 is nearly identical. Strong staining can be visualized in the granular layer, however, staining is absent from the Purkinje cell bodies and is only minor in the molecular layer ( D,E ). In contrast to the other two antibodies, amino-terminal PKA-phosphorylated Kv4.2 antibodies recognize the molecular layer, and staining is highly reduced in the granular layer. Purkinje cell bodies are void of immunoreactivity.
    Figure Legend Snippet: Cortex and Cerebellum. Staining of ERK triply phosphorylated Kv4.2 ( A,D ), carboxy-terminal PKA-phosphorylated Kv4.2 ( B,E ), and amino-terminal PKA-phosphorylated Kv4.2 ( C,F ) in the cortex ( A,B,C ) and cerebellum ( D,E,F ) at 100×. In the cortex, ERK triply phosphorylated Kv4.2 antibodies show predominant staining in layer IV of the cortex with possible evidence of barrels ( A ). Carboxy-terminal PKA-phosphorylated Kv4.2 staining shows weak immunoreactivity in layers V and VI ( B ). Amino-terminal PKA-phosphorylated Kv4.2 staining displays immunoreactivity in layers IV, V, and VI with the strongest signal in layers V and VI ( C ). In the cerebellum, staining with the ERK triply phosphorylated and carboxy-terminal PKA-phosphorylated Kv4.2 is nearly identical. Strong staining can be visualized in the granular layer, however, staining is absent from the Purkinje cell bodies and is only minor in the molecular layer ( D,E ). In contrast to the other two antibodies, amino-terminal PKA-phosphorylated Kv4.2 antibodies recognize the molecular layer, and staining is highly reduced in the granular layer. Purkinje cell bodies are void of immunoreactivity.

    Techniques Used: Staining

    Antibody specificity. Western blotting was performed on hippocampal homogenate membrane preps by use of antibodies against ERK triply phosphorylated Kv4.2 ( A ), carboxy-terminal PKA-phosphorylated Kv4.2 ( B ), and amino-terminanl PKA-phosphorylated Kv4.2 ( C ). Preincubation with the corresponding antigen blocked 90%–100% of immunoreactivity. In C , the hippocampus was first treated with forskolin to improve the immunoreactivity.
    Figure Legend Snippet: Antibody specificity. Western blotting was performed on hippocampal homogenate membrane preps by use of antibodies against ERK triply phosphorylated Kv4.2 ( A ), carboxy-terminal PKA-phosphorylated Kv4.2 ( B ), and amino-terminanl PKA-phosphorylated Kv4.2 ( C ). Preincubation with the corresponding antigen blocked 90%–100% of immunoreactivity. In C , the hippocampus was first treated with forskolin to improve the immunoreactivity.

    Techniques Used: Western Blot

    Higher magnification of area CA3. Staining of ERK triply phosphorylated Kv4.2 at 200× ( A ) and 100× ( D ), carboxy-terminal PKA-phosphorylated Kv4.2 at 200× ( B ) and 100× ( E ), and amino-terminal PKA-phosphorylated Kv4.2 at 200× ( C ). Heavy staining of CA3 neuronal soma can be seen in A , with a dearth of immunoreactivity in this same area in B and C. D and E show the contrast in immunoreactivity in the stratum lucidum between the ERK triply phosphorylated Kv4.2 antibody ( D ) and the carboxy-terminal PKA-phosphorylated Kv4.2 antibody ( E ).
    Figure Legend Snippet: Higher magnification of area CA3. Staining of ERK triply phosphorylated Kv4.2 at 200× ( A ) and 100× ( D ), carboxy-terminal PKA-phosphorylated Kv4.2 at 200× ( B ) and 100× ( E ), and amino-terminal PKA-phosphorylated Kv4.2 at 200× ( C ). Heavy staining of CA3 neuronal soma can be seen in A , with a dearth of immunoreactivity in this same area in B and C. D and E show the contrast in immunoreactivity in the stratum lucidum between the ERK triply phosphorylated Kv4.2 antibody ( D ) and the carboxy-terminal PKA-phosphorylated Kv4.2 antibody ( E ).

    Techniques Used: Staining

    Higher magnification of area CA1. Staining of ERK triply phosphorylated Kv4.2 at 100× ( A ), carboxy-terminal PKA-phosphorylated Kv4.2 at 100× ( B ), and amino-terminal PKA-phosphorylated Kv4.2 at 100× ( C ). Strong immunoreactivity in the CA1 stratum oriens (so) and stratum radiatum (sr) can be seen in A and B with a dearth of immunoreactivity in these same layers in C . However, there is a relative dearth of immunoreactivity in the stratum lacunosum moleculare (slm) in A and B , whereas immunoreactivity is strong in the slm in C . The immunoreactivity in the molecular layer of the dentate gyrus (ml-dg) is increased in B as compared with A and C . (sp) Stratum pyramidali.
    Figure Legend Snippet: Higher magnification of area CA1. Staining of ERK triply phosphorylated Kv4.2 at 100× ( A ), carboxy-terminal PKA-phosphorylated Kv4.2 at 100× ( B ), and amino-terminal PKA-phosphorylated Kv4.2 at 100× ( C ). Strong immunoreactivity in the CA1 stratum oriens (so) and stratum radiatum (sr) can be seen in A and B with a dearth of immunoreactivity in these same layers in C . However, there is a relative dearth of immunoreactivity in the stratum lacunosum moleculare (slm) in A and B , whereas immunoreactivity is strong in the slm in C . The immunoreactivity in the molecular layer of the dentate gyrus (ml-dg) is increased in B as compared with A and C . (sp) Stratum pyramidali.

    Techniques Used: Staining

    Kv4.2 structure and peptide antigens. Schematic structure of Kv4.2 with highlighted ERK and PKA phosphorylation sites. The ERK triply phosphorylated antibody was made against a peptide running from AA586 to AA618, which includes the ERK phosphorylation sites Thr 602 , Thr 607 , and Ser 616 . The carboxy-terminal PKA-phosphorylated Kv4.2 antibody was made against a peptide running from AA546 to AA548, which includes a PKA phosphorylation site at Ser 552 . The amino-terminal PKA-phosphorylated Kv4.2 antibody was made against a peptide running from AA32 to AA44, which includes a PKA phosphorylation site at Thr 38 .
    Figure Legend Snippet: Kv4.2 structure and peptide antigens. Schematic structure of Kv4.2 with highlighted ERK and PKA phosphorylation sites. The ERK triply phosphorylated antibody was made against a peptide running from AA586 to AA618, which includes the ERK phosphorylation sites Thr 602 , Thr 607 , and Ser 616 . The carboxy-terminal PKA-phosphorylated Kv4.2 antibody was made against a peptide running from AA546 to AA548, which includes a PKA phosphorylation site at Ser 552 . The amino-terminal PKA-phosphorylated Kv4.2 antibody was made against a peptide running from AA32 to AA44, which includes a PKA phosphorylation site at Thr 38 .

    Techniques Used:

    8) Product Images from "Morbillivirus Infection of the Mouse Central Nervous System Induces Region-Specific Upregulation of MMPs and TIMPs Correlated to Inflammatory Cytokine Expression"

    Article Title: Morbillivirus Infection of the Mouse Central Nervous System Induces Region-Specific Upregulation of MMPs and TIMPs Correlated to Inflammatory Cytokine Expression

    Journal: Journal of Virology

    doi: 10.1128/JVI.75.17.8268-8282.2001

    Expression of gelatinases MMP-2 and MMP-9 in microdissected brain structures. (a) Gelatin zymography. To increase their concentration, the gelatinases were purified from brain structure lysates on gelatin-Sepharose beads, using the method of Zhang and Gottschall (67), and loaded on a 9% polyacrylamide gel containing gelatin (0.07%) and activated (20 h at 37°C), and then the gels were stained. Constitutive expression of active MMP-2 (65 kDa) was detected in all sham-inoculated structures, while faint MMP-9 proteolytic activity (92 kDa) was seen only in the mesencephalon, brain stem, cerebellum, and spinal cord. MMP-2 and pro-MMP-9 were markedly upregulated in infected brain structures, in particular in the rostral part of the brain. (b) Densitometric analysis. Data expressed as the ratio of infected/sham-inoculated normalized values (relative units) showed upregulation of MMP-2 and MMP-9 mainly in the hippocampus and, to a lesser extent, in the cortex and hypothalamus of infected mice. cx, cortex; mes, mesencephalon; hip, hippocampus; hyp, hypothalamus; bs, brain stem; cb, cerebellum; sc, spinal cord. (c) APMA treatment of hippocampal lysates. To determine if gelatinases are expressed as prozymogens or active enzymes, hippocampal lysates from sham-inoculated and infected mice at 14 dpi were treated with APMA and then electrophoresed as above. The zymograms for the untreated samples (lanes 1 and 2) showed two clear bands of respective apparent molecular masses of 65 and 92 kDa, presumably corresponding to active MMP-2 and pro-MMP-9, which were strongly upregulated in infected hippocampus (lane 2). In the APMA-treated samples (lanes 3 and 4), the 92-kDa product disappeared while a 75-kDa apparent molecular mass product became visible; the 65-kDa product corresponds to active MMP-2 that remained unchanged. Culture supernatant from PMA-treated BHK21 cells (containing the MMP-2 active forms) and TNF-α-treated DEV cells (containing the MMP-9 active form) were used as positive controls. Lanes 1 and 3, hippocampus from a sham-inoculated mouse; lanes 2 and 4, hippocampus from an infected mouse
    Figure Legend Snippet: Expression of gelatinases MMP-2 and MMP-9 in microdissected brain structures. (a) Gelatin zymography. To increase their concentration, the gelatinases were purified from brain structure lysates on gelatin-Sepharose beads, using the method of Zhang and Gottschall (67), and loaded on a 9% polyacrylamide gel containing gelatin (0.07%) and activated (20 h at 37°C), and then the gels were stained. Constitutive expression of active MMP-2 (65 kDa) was detected in all sham-inoculated structures, while faint MMP-9 proteolytic activity (92 kDa) was seen only in the mesencephalon, brain stem, cerebellum, and spinal cord. MMP-2 and pro-MMP-9 were markedly upregulated in infected brain structures, in particular in the rostral part of the brain. (b) Densitometric analysis. Data expressed as the ratio of infected/sham-inoculated normalized values (relative units) showed upregulation of MMP-2 and MMP-9 mainly in the hippocampus and, to a lesser extent, in the cortex and hypothalamus of infected mice. cx, cortex; mes, mesencephalon; hip, hippocampus; hyp, hypothalamus; bs, brain stem; cb, cerebellum; sc, spinal cord. (c) APMA treatment of hippocampal lysates. To determine if gelatinases are expressed as prozymogens or active enzymes, hippocampal lysates from sham-inoculated and infected mice at 14 dpi were treated with APMA and then electrophoresed as above. The zymograms for the untreated samples (lanes 1 and 2) showed two clear bands of respective apparent molecular masses of 65 and 92 kDa, presumably corresponding to active MMP-2 and pro-MMP-9, which were strongly upregulated in infected hippocampus (lane 2). In the APMA-treated samples (lanes 3 and 4), the 92-kDa product disappeared while a 75-kDa apparent molecular mass product became visible; the 65-kDa product corresponds to active MMP-2 that remained unchanged. Culture supernatant from PMA-treated BHK21 cells (containing the MMP-2 active forms) and TNF-α-treated DEV cells (containing the MMP-9 active form) were used as positive controls. Lanes 1 and 3, hippocampus from a sham-inoculated mouse; lanes 2 and 4, hippocampus from an infected mouse

    Techniques Used: Expressing, Zymography, Concentration Assay, Purification, Staining, Activity Assay, Infection, Mouse Assay

    Immunodetection of gelatinases MMP-2 and MMP-9 and localization of gelatinolytic activity by ISZ. Immunodetection (IHC) of MMP-9 and MMP-2 using antibodies against the whole protein (reactive with both the proenzyme and enzyme forms) showed MMP-9 to be present in the hippocampus (a) at the level of the CA3 pyramidal layer. At the cellular level, MMP-9 was mainly found in neurons, identified by their size and localization (panel a and insert), as confirmed using double labeling. (c) MMP-9 (green), indicated by white arrows; (d) neuronal marker MAP-2 (red), indicated by white arrows. It is noteworthy that all the MAP-2-positive cells are not always MMP-9 positive. MMP-2 was mainly located in astrocyte-type cells (panel b and insert). For ISZ, the quenched fluorescent substrate (gelatin) was added directly to tissue sections, and enzymatic activity was detected by the unmasked fluorescence. Cellular gelatinolytic activity was faint and diffuse in brain sections from sham-inoculated mice (e) and was markedly enhanced in the cells of the pyramidal layers of the hippocampus from CDV-infected mice (f), which is also shown at a higher magnification (insert in panel f versus that in panel e). Magnifications, ×28 (a, b, e, f); ×40 (c, d, and inserts in panels a, b, e, and f).
    Figure Legend Snippet: Immunodetection of gelatinases MMP-2 and MMP-9 and localization of gelatinolytic activity by ISZ. Immunodetection (IHC) of MMP-9 and MMP-2 using antibodies against the whole protein (reactive with both the proenzyme and enzyme forms) showed MMP-9 to be present in the hippocampus (a) at the level of the CA3 pyramidal layer. At the cellular level, MMP-9 was mainly found in neurons, identified by their size and localization (panel a and insert), as confirmed using double labeling. (c) MMP-9 (green), indicated by white arrows; (d) neuronal marker MAP-2 (red), indicated by white arrows. It is noteworthy that all the MAP-2-positive cells are not always MMP-9 positive. MMP-2 was mainly located in astrocyte-type cells (panel b and insert). For ISZ, the quenched fluorescent substrate (gelatin) was added directly to tissue sections, and enzymatic activity was detected by the unmasked fluorescence. Cellular gelatinolytic activity was faint and diffuse in brain sections from sham-inoculated mice (e) and was markedly enhanced in the cells of the pyramidal layers of the hippocampus from CDV-infected mice (f), which is also shown at a higher magnification (insert in panel f versus that in panel e). Magnifications, ×28 (a, b, e, f); ×40 (c, d, and inserts in panels a, b, e, and f).

    Techniques Used: Immunodetection, Activity Assay, Immunohistochemistry, Labeling, Marker, Fluorescence, Mouse Assay, Infection

    MMP-2, MMP-9, and MT1-MMP mRNA expression analyzed by RT-PCR and densitometry. Total RNAs (0.5 μg) extracted from microdissected brain structures from infected and sham-inoculated mice were subjected to RT-PCR. After electrophoresis on an agarose gel and electrotransfer, Southern blotting of the amplicons was performed. Hybridization of specific internal radiolabeled probes allowed the semiquantification of each PCR product. MMP expression was then analyzed by phosphorimaging densitometry. (a) The relative mRNA content for each amplicon was calculated as a fraction of the levels of the housekeeping gene G3PDH mRNA (normalized values), and the results were expressed as a ratio of levels in infected mice relative to those in sham-inoculated mice (relative units). Only slight MMP-2 and MMP-9 upregulation was seen in brain structures of CDV-infected mice, the difference not being significant in the Mann-Whitney test (b). In contrast, marked upregulation of MT1-MMP was seen in infected mice, mainly in the rostral brain (cortex, hippocampus, and hypothalamus), the difference being statistically significant in the cortex and hypothalamus ( P
    Figure Legend Snippet: MMP-2, MMP-9, and MT1-MMP mRNA expression analyzed by RT-PCR and densitometry. Total RNAs (0.5 μg) extracted from microdissected brain structures from infected and sham-inoculated mice were subjected to RT-PCR. After electrophoresis on an agarose gel and electrotransfer, Southern blotting of the amplicons was performed. Hybridization of specific internal radiolabeled probes allowed the semiquantification of each PCR product. MMP expression was then analyzed by phosphorimaging densitometry. (a) The relative mRNA content for each amplicon was calculated as a fraction of the levels of the housekeeping gene G3PDH mRNA (normalized values), and the results were expressed as a ratio of levels in infected mice relative to those in sham-inoculated mice (relative units). Only slight MMP-2 and MMP-9 upregulation was seen in brain structures of CDV-infected mice, the difference not being significant in the Mann-Whitney test (b). In contrast, marked upregulation of MT1-MMP was seen in infected mice, mainly in the rostral brain (cortex, hippocampus, and hypothalamus), the difference being statistically significant in the cortex and hypothalamus ( P

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Infection, Mouse Assay, Electrophoresis, Agarose Gel Electrophoresis, Electrotransfer, Southern Blot, Hybridization, Polymerase Chain Reaction, Amplification, MANN-WHITNEY

    9) Product Images from "DEDD regulates degradation of intermediate filaments during apoptosis"

    Article Title: DEDD regulates degradation of intermediate filaments during apoptosis

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200112124

    Caspase-3 is recruited to IFs and associates with DEDD. (A) MCF7 cells were transiently transfected with procaspase-3–GFP, treated with STS (0, 2 and 4 h) and stained for K8. Cells were analyzed by confocal microscopy. Shown are two-dimensional pictures of three- dimensional images, which were created using 20 overlaying 0.5 μm z-sections. Merge, overlay of GFP fluorescence and K8 staining. Arrowheads denote caspase-3–GFP positivity on IFs. A three-dimensional image of this panel is depicted in Video 1 (available online at http://www.jcb.org/cgi/content/full/jcb.200112124/DC1 ). Bar, 10 μm. (B) Immunoprecipitation of caspase-3 from MCF7-C3 (with a rabbit polyclonal caspase-3 antibody) coimmunoprecipitated DEDD 2Ub as detected by biotinylated PRO29 and anti-ubiquitin mAb (left two panels). Control blot (right) with a different caspase-3 (CASP-3) mAb detected efficient caspase-3 immunoprecipitation. Note, the same blot was probed sequentially in the order PRO29, anti-CASP-3, anti-ubiquitin. All M r notations on left side of blots in kD.
    Figure Legend Snippet: Caspase-3 is recruited to IFs and associates with DEDD. (A) MCF7 cells were transiently transfected with procaspase-3–GFP, treated with STS (0, 2 and 4 h) and stained for K8. Cells were analyzed by confocal microscopy. Shown are two-dimensional pictures of three- dimensional images, which were created using 20 overlaying 0.5 μm z-sections. Merge, overlay of GFP fluorescence and K8 staining. Arrowheads denote caspase-3–GFP positivity on IFs. A three-dimensional image of this panel is depicted in Video 1 (available online at http://www.jcb.org/cgi/content/full/jcb.200112124/DC1 ). Bar, 10 μm. (B) Immunoprecipitation of caspase-3 from MCF7-C3 (with a rabbit polyclonal caspase-3 antibody) coimmunoprecipitated DEDD 2Ub as detected by biotinylated PRO29 and anti-ubiquitin mAb (left two panels). Control blot (right) with a different caspase-3 (CASP-3) mAb detected efficient caspase-3 immunoprecipitation. Note, the same blot was probed sequentially in the order PRO29, anti-CASP-3, anti-ubiquitin. All M r notations on left side of blots in kD.

    Techniques Used: Transfection, Staining, Confocal Microscopy, Fluorescence, Immunoprecipitation

    10) Product Images from "ClC-2 knockdown prevents cerebrovascular remodeling via inhibition of the Wnt/β-catenin signaling pathway"

    Article Title: ClC-2 knockdown prevents cerebrovascular remodeling via inhibition of the Wnt/β-catenin signaling pathway

    Journal: Cellular & Molecular Biology Letters

    doi: 10.1186/s11658-018-0095-z

    ClC-2 inhibition attenuated the AngII-induced activation of Wnt/β-catenin signaling. a through f HBVSMCs were transfected with ClC-2 siRNA (siClC-2; 20 nM) or negative siRNA (negative; 20 nM) and then stimulated with angiotensin II (AngII; 10 − 7 M) for 48 h. Shown are the western blotting results for β-catenin phosphorylation ( a ), β-catenin cytosol ( b ) and nuclear protein ( c ) levels, GSK-3β phosphorylation ( d ), and survivin ( e ) and cyclin D1 ( f ) protein expression. g Quantitative real-time PCR analysis of Wnt3a and Wnt5a mRNA expression. h The cells were treated with recombinant Wnt3a (100 ng/ml) for 48 h. Wnt3a expression was examined using quantitative real-time. i Viability of HBVSMCs transfected with ClC-2 siRNA followed by co-incubation with recombinant Wnt3a and AngII. ** p
    Figure Legend Snippet: ClC-2 inhibition attenuated the AngII-induced activation of Wnt/β-catenin signaling. a through f HBVSMCs were transfected with ClC-2 siRNA (siClC-2; 20 nM) or negative siRNA (negative; 20 nM) and then stimulated with angiotensin II (AngII; 10 − 7 M) for 48 h. Shown are the western blotting results for β-catenin phosphorylation ( a ), β-catenin cytosol ( b ) and nuclear protein ( c ) levels, GSK-3β phosphorylation ( d ), and survivin ( e ) and cyclin D1 ( f ) protein expression. g Quantitative real-time PCR analysis of Wnt3a and Wnt5a mRNA expression. h The cells were treated with recombinant Wnt3a (100 ng/ml) for 48 h. Wnt3a expression was examined using quantitative real-time. i Viability of HBVSMCs transfected with ClC-2 siRNA followed by co-incubation with recombinant Wnt3a and AngII. ** p

    Techniques Used: Inhibition, Activation Assay, Transfection, Western Blot, Expressing, Real-time Polymerase Chain Reaction, Recombinant, Incubation

    11) Product Images from "Dissociated expression of mitochondrial and cytosolic creatine kinases in the human brain: a new perspective on the role of creatine in brain energy metabolism"

    Article Title: Dissociated expression of mitochondrial and cytosolic creatine kinases in the human brain: a new perspective on the role of creatine in brain energy metabolism

    Journal: Journal of Cerebral Blood Flow & Metabolism

    doi: 10.1038/jcbfm.2013.84

    Expression of brain-type creatine kinase (BCK) and ubiquitous mitochondrial creatine kinase (uMtCK) in the cerebellum. ( A , B ) The 3,3′-diaminobenzidine tetrahydrochloride (DAB)–peroxidase staining of ( A ) uMtCK and ( B ) BCK in the cerebellar
    Figure Legend Snippet: Expression of brain-type creatine kinase (BCK) and ubiquitous mitochondrial creatine kinase (uMtCK) in the cerebellum. ( A , B ) The 3,3′-diaminobenzidine tetrahydrochloride (DAB)–peroxidase staining of ( A ) uMtCK and ( B ) BCK in the cerebellar

    Techniques Used: Expressing, Staining

    12) Product Images from "DUX4c Is Up-Regulated in FSHD. It Induces the MYF5 Protein and Human Myoblast Proliferation"

    Article Title: DUX4c Is Up-Regulated in FSHD. It Induces the MYF5 Protein and Human Myoblast Proliferation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0007482

    DUX4c over-expression induces cell proliferation. (A) PCNA was detected by immunofluorescence (red) 24 h post transfection with the pCIneo vectors indicated. The picture of DUX4c expressing cells was exposed 1.4 sec versus 2.7 sec for the other panels to visualize the cells. (B) The cells were switched 24 h post transfection to a differentiation medium, and observed 4 days later by phase contrast microscopy (left panels). Early differentiation was evaluated by desmin detection (green, right panels). (C) Cyclin A (green) and DUX4/4c (red) were detected by immunofluorescence 24 h post transfection of human immortalized myoblasts with the indicated pCIneo -vectors. (D) Human immortalized myoblasts were transfected with the indicated pCIneo -vectors and switched to differentiation medium 48 h later. Troponin T was detected by immunofluorescence 8 days later. Bars correspond to 20 µm.
    Figure Legend Snippet: DUX4c over-expression induces cell proliferation. (A) PCNA was detected by immunofluorescence (red) 24 h post transfection with the pCIneo vectors indicated. The picture of DUX4c expressing cells was exposed 1.4 sec versus 2.7 sec for the other panels to visualize the cells. (B) The cells were switched 24 h post transfection to a differentiation medium, and observed 4 days later by phase contrast microscopy (left panels). Early differentiation was evaluated by desmin detection (green, right panels). (C) Cyclin A (green) and DUX4/4c (red) were detected by immunofluorescence 24 h post transfection of human immortalized myoblasts with the indicated pCIneo -vectors. (D) Human immortalized myoblasts were transfected with the indicated pCIneo -vectors and switched to differentiation medium 48 h later. Troponin T was detected by immunofluorescence 8 days later. Bars correspond to 20 µm.

    Techniques Used: Over Expression, Immunofluorescence, Transfection, Expressing, Size-exclusion Chromatography, Microscopy

    DUX4c protein expression in myoblasts. (A) Transcription/translation in vitro in a rabbit reticulocyte lysate in the presence T7 RNA polymerase and [ 35 S]-cysteine with genomic fragments encoding DUX4 (lane 1) or DUX4c (lane 2) cloned in pCIneo . 52 kDa-DUX4 (white arrow) and 47 kDa-DUX4c (black arrow) are detected by autoradiography after 10% PAGE-SDS. (B–C) 30 µg total proteins extracted from primary myoblast were analysed by 4–12% PAGE-SDS and Western blot with the indicated primary antibodies, appropriate secondary antibodies coupled to HRP and the ECL kit. α-Tubulin was the loading control. (B) Competition: a 5-fold excess of DUX4c antigenic peptide was pre-incubated (+) or not (−) with the serum raised against DUX4c or cadherin as indicated. (C) Extracts were prepared either from proliferating myoblasts or 2 (d2) or 6 (d6) days after induction of differentiation. (D) DUX4c (red) was detected by immunofluorescence in nuclei of myoblasts and myotubes 2 (d2) and 6 (d6) days after inducing differentiation. a' and b' correspond respectively to two enlarged nuclei from d2 and d6 (white boxes in a and b). The labeling is weakened after competition with the immunogenic peptide (c). Troponin T (green) is a myotube differentiation marker. Myoblasts not fused to myotubes express DUX4c (red nuclei) but not troponin T. Bar corresponds to 20 µm. (E) 30 µg protein extracted from primary myotubes were analyzed by Western blot as in (C). (F) Densitometric scanning of the film shown in (E): DUX4c expression levels were normalized to α-Tubulin (relative absorbance units). C: control, F: FSHD, D: DMD.
    Figure Legend Snippet: DUX4c protein expression in myoblasts. (A) Transcription/translation in vitro in a rabbit reticulocyte lysate in the presence T7 RNA polymerase and [ 35 S]-cysteine with genomic fragments encoding DUX4 (lane 1) or DUX4c (lane 2) cloned in pCIneo . 52 kDa-DUX4 (white arrow) and 47 kDa-DUX4c (black arrow) are detected by autoradiography after 10% PAGE-SDS. (B–C) 30 µg total proteins extracted from primary myoblast were analysed by 4–12% PAGE-SDS and Western blot with the indicated primary antibodies, appropriate secondary antibodies coupled to HRP and the ECL kit. α-Tubulin was the loading control. (B) Competition: a 5-fold excess of DUX4c antigenic peptide was pre-incubated (+) or not (−) with the serum raised against DUX4c or cadherin as indicated. (C) Extracts were prepared either from proliferating myoblasts or 2 (d2) or 6 (d6) days after induction of differentiation. (D) DUX4c (red) was detected by immunofluorescence in nuclei of myoblasts and myotubes 2 (d2) and 6 (d6) days after inducing differentiation. a' and b' correspond respectively to two enlarged nuclei from d2 and d6 (white boxes in a and b). The labeling is weakened after competition with the immunogenic peptide (c). Troponin T (green) is a myotube differentiation marker. Myoblasts not fused to myotubes express DUX4c (red nuclei) but not troponin T. Bar corresponds to 20 µm. (E) 30 µg protein extracted from primary myotubes were analyzed by Western blot as in (C). (F) Densitometric scanning of the film shown in (E): DUX4c expression levels were normalized to α-Tubulin (relative absorbance units). C: control, F: FSHD, D: DMD.

    Techniques Used: Expressing, In Vitro, Clone Assay, Autoradiography, Polyacrylamide Gel Electrophoresis, Western Blot, Incubation, Immunofluorescence, Labeling, Marker

    DUX4c over-expression induces MYF5. (A–C) TE671 cells were transfected with the indicated pCIneo vectors. Nuclear extracts were deposited in triplicate on a plate where the MYOD1, MEF2 or MYF5 specific DNA target was immobilized. The DNA-bound protein was detected by ELISA (TransAm assay). Relative absorbances are given relative to the insertless pCIneo sample arbitrarily set to 1. Three independent experiments (1 to 3) made in triplicate are presented. (D) TE671 nuclear extracts were prepared 48 h after transfection as above and 30 or 15 (*) µg were analyzed by 10% PAGE-SDS and Western blotting with a serum raised against MYF5 or actin (internal control). NT: non transfected cells. (E) same as in D but transfection was with pAC1M2-DUX4c and DUX4c expression induced by doxycycline (o to1000 ng). (F) Mouse C2C12 cells were transfected with the indicated pCIneo vectors. Total protein extracts were prepared 24 or 48 h later and 40 µg were analysed by Western blot with a serum raised against MYF5 or DUX4c as in D. (G) 40 µg nuclear extracts of TE cells transfected with the indicated vectors were subjected to immunoprecipitation with the anti-DUX4c or the anti-MYF5 serum. The immunoprecipitate was analysed by Western blot with the anti-DUX4c or anti-MYF5 serum as in D.
    Figure Legend Snippet: DUX4c over-expression induces MYF5. (A–C) TE671 cells were transfected with the indicated pCIneo vectors. Nuclear extracts were deposited in triplicate on a plate where the MYOD1, MEF2 or MYF5 specific DNA target was immobilized. The DNA-bound protein was detected by ELISA (TransAm assay). Relative absorbances are given relative to the insertless pCIneo sample arbitrarily set to 1. Three independent experiments (1 to 3) made in triplicate are presented. (D) TE671 nuclear extracts were prepared 48 h after transfection as above and 30 or 15 (*) µg were analyzed by 10% PAGE-SDS and Western blotting with a serum raised against MYF5 or actin (internal control). NT: non transfected cells. (E) same as in D but transfection was with pAC1M2-DUX4c and DUX4c expression induced by doxycycline (o to1000 ng). (F) Mouse C2C12 cells were transfected with the indicated pCIneo vectors. Total protein extracts were prepared 24 or 48 h later and 40 µg were analysed by Western blot with a serum raised against MYF5 or DUX4c as in D. (G) 40 µg nuclear extracts of TE cells transfected with the indicated vectors were subjected to immunoprecipitation with the anti-DUX4c or the anti-MYF5 serum. The immunoprecipitate was analysed by Western blot with the anti-DUX4c or anti-MYF5 serum as in D.

    Techniques Used: Over Expression, Transfection, Enzyme-linked Immunosorbent Assay, Polyacrylamide Gel Electrophoresis, Western Blot, Expressing, Immunoprecipitation

    Transcriptional activity of the DUX4c gene. Transcriptional activity of the DUX4c promoter. HeLa, C 2 C 12 and TE671 cells were transfected with pGL3 vectors containing the luciferase reporter gene either promoterless (black bars) or fused to the DUX4c (white bars) or DUX4 ( striped bars) promoter. Luciferase activity was measured 24 h post-transfection and expressed relative to the activity of the promoterless vector set to 1. The means and standard errors are indicated (n = 18).
    Figure Legend Snippet: Transcriptional activity of the DUX4c gene. Transcriptional activity of the DUX4c promoter. HeLa, C 2 C 12 and TE671 cells were transfected with pGL3 vectors containing the luciferase reporter gene either promoterless (black bars) or fused to the DUX4c (white bars) or DUX4 ( striped bars) promoter. Luciferase activity was measured 24 h post-transfection and expressed relative to the activity of the promoterless vector set to 1. The means and standard errors are indicated (n = 18).

    Techniques Used: Activity Assay, Transfection, Luciferase, Plasmid Preparation

    DUX4c protein expression in muscle biopsies. (A) 30 µg protein extracted of muscle biopsies were analyzed by Western blot as in Fig. 3 , except that cytochrome C was the internal loading control. (B) Densitometric scanning of the Western blot shown in (A) and of additional samples (not shown): DUX4c expression levels were normalized to cytochrome C (relative absorbance units). Samples are indicated C1 to C4 for controls, F1 to F10 for FSHD, and D1 to D4 for DMD as well as the D4Z4 copy numbers of the FSHD patients. The biopsied muscle is indicaded (D, Q: non-affected deltoid or quadriceps ; T*: affected trapezius ). F10 also has a D4Z4 array contraction on the second 4q35 allele (+7).
    Figure Legend Snippet: DUX4c protein expression in muscle biopsies. (A) 30 µg protein extracted of muscle biopsies were analyzed by Western blot as in Fig. 3 , except that cytochrome C was the internal loading control. (B) Densitometric scanning of the Western blot shown in (A) and of additional samples (not shown): DUX4c expression levels were normalized to cytochrome C (relative absorbance units). Samples are indicated C1 to C4 for controls, F1 to F10 for FSHD, and D1 to D4 for DMD as well as the D4Z4 copy numbers of the FSHD patients. The biopsied muscle is indicaded (D, Q: non-affected deltoid or quadriceps ; T*: affected trapezius ). F10 also has a D4Z4 array contraction on the second 4q35 allele (+7).

    Techniques Used: Expressing, Western Blot

    Characterization of the DUX4c mRNA. (A) Schematic representation of the DUX4c promoter with the transcription start sites (arrows and positions) identified by 5′ RACE (primer indicated) on RNA extracted from control and FSHD myoblasts. (B) Top: Schematic representation of the p7.5 kb-DUX4c insert (see Supporting Information S2 ) close to its 3′ cloning site, showing the stop codon, the putative poly-A addition signal, two purine-rich (86 and 83%) regions (black boxes) and the primers used in 3′RACE (arrows, #350 and 351). Bottom: Mapping of the multiple 3′ ends and alternative splicing detected in the 3′RACE products. These were derived from RNAs of either C2C12 cells transfected with p7.5 kb-DUX4c or FSHD primary myoblasts (*). (C) Schematic representation of the DUX4c ORF with the homeoboxes (black boxes) and the primers used for RT-PCR. (D) Amplification of the DUX4c mRNA was performed on total RNA extracted from FSHD (F24) or control primary myoblasts (C29) either in proliferation (lanes 4 and 7) or differentiated to myotubes (diff.). RNA samples were incubated (+) or not (−) with DNase I, and reverse transcriptase (RT) as indicated. The PCR products were analysed by electrophoresis on a 1%-agarose gel and stained with ethidium bromide. As a positive control (lane 3), RT-PCR was performed on RNA of C2C12 cells transfected with p3 kb-DUX4c .
    Figure Legend Snippet: Characterization of the DUX4c mRNA. (A) Schematic representation of the DUX4c promoter with the transcription start sites (arrows and positions) identified by 5′ RACE (primer indicated) on RNA extracted from control and FSHD myoblasts. (B) Top: Schematic representation of the p7.5 kb-DUX4c insert (see Supporting Information S2 ) close to its 3′ cloning site, showing the stop codon, the putative poly-A addition signal, two purine-rich (86 and 83%) regions (black boxes) and the primers used in 3′RACE (arrows, #350 and 351). Bottom: Mapping of the multiple 3′ ends and alternative splicing detected in the 3′RACE products. These were derived from RNAs of either C2C12 cells transfected with p7.5 kb-DUX4c or FSHD primary myoblasts (*). (C) Schematic representation of the DUX4c ORF with the homeoboxes (black boxes) and the primers used for RT-PCR. (D) Amplification of the DUX4c mRNA was performed on total RNA extracted from FSHD (F24) or control primary myoblasts (C29) either in proliferation (lanes 4 and 7) or differentiated to myotubes (diff.). RNA samples were incubated (+) or not (−) with DNase I, and reverse transcriptase (RT) as indicated. The PCR products were analysed by electrophoresis on a 1%-agarose gel and stained with ethidium bromide. As a positive control (lane 3), RT-PCR was performed on RNA of C2C12 cells transfected with p3 kb-DUX4c .

    Techniques Used: Clone Assay, Derivative Assay, Transfection, Reverse Transcription Polymerase Chain Reaction, Amplification, Incubation, Polymerase Chain Reaction, Electrophoresis, Agarose Gel Electrophoresis, Staining, Positive Control

    Localization of the DUX4 and DUX4c genes. (A) Schematic representation of the 4q35 subtelomeric region with the D4Z4 repeat array and the SLC25A4 (previously known as ANT1 ) [41] , ALP [60] , FRG1 [14] , TUBB4Q [15] and FRG2 [16] genes. DUX4 maps within each D4Z4 element [21] and DUX4c within an isolated inverted D4Z4 unit at the D4S2463 locus. S/MAR and FR-MAR: nuclear scaffold/matrix attachment regions, [13] . Upper line: 4q35/10q26 limit of homology [27] . (B) Enlargement (inverted orientation) of the 7.5-kb fragment that contains DUX4c with part of the FRG2 gene. The DUX4c ORF is boxed, with the homeoboxes in black. The promoter GC boxes, the putative variant TATA box (CATAA) and polyadenylation signal are indicated. Numbering from the Eco RI site (GenBank acc. no. AY500824).
    Figure Legend Snippet: Localization of the DUX4 and DUX4c genes. (A) Schematic representation of the 4q35 subtelomeric region with the D4Z4 repeat array and the SLC25A4 (previously known as ANT1 ) [41] , ALP [60] , FRG1 [14] , TUBB4Q [15] and FRG2 [16] genes. DUX4 maps within each D4Z4 element [21] and DUX4c within an isolated inverted D4Z4 unit at the D4S2463 locus. S/MAR and FR-MAR: nuclear scaffold/matrix attachment regions, [13] . Upper line: 4q35/10q26 limit of homology [27] . (B) Enlargement (inverted orientation) of the 7.5-kb fragment that contains DUX4c with part of the FRG2 gene. The DUX4c ORF is boxed, with the homeoboxes in black. The promoter GC boxes, the putative variant TATA box (CATAA) and polyadenylation signal are indicated. Numbering from the Eco RI site (GenBank acc. no. AY500824).

    Techniques Used: ALP Assay, Isolation, Variant Assay

    13) Product Images from "Mcl-1 protects prostate cancer cells from cell death mediated by chemotherapy-induced DNA damage"

    Article Title: Mcl-1 protects prostate cancer cells from cell death mediated by chemotherapy-induced DNA damage

    Journal: Oncoscience

    doi:

    1198 + BA decreases Mcl-1 and increases DNA damage-associated γH2AX in TRAMP PCa Top panel: Representative IHC for Mcl-1 (x200, brown color) showed less protein in the high dose 1198/75 + BA/10 combination compared to 1198, BA, and vehicle control. Bottom panel: Representative IHC for γH2AX (x200, brown color) showed increased levels in the high dose 1198/75 + BA/10 combination compared to 1198, BA, and vehicle control. Similar results for Mcl-1 and γH2AX IHC were obtained from 02 additional mice from each group.
    Figure Legend Snippet: 1198 + BA decreases Mcl-1 and increases DNA damage-associated γH2AX in TRAMP PCa Top panel: Representative IHC for Mcl-1 (x200, brown color) showed less protein in the high dose 1198/75 + BA/10 combination compared to 1198, BA, and vehicle control. Bottom panel: Representative IHC for γH2AX (x200, brown color) showed increased levels in the high dose 1198/75 + BA/10 combination compared to 1198, BA, and vehicle control. Similar results for Mcl-1 and γH2AX IHC were obtained from 02 additional mice from each group.

    Techniques Used: Immunohistochemistry, Mouse Assay

    Mcl-1 knockdown in PC3 increases DNA damage-associated γH2AX immunostain after 1198 + BA or Dox treatment (A) DIF (top panel) showed that the 1198 + BA combination (24 h) increased immunostaining for γH2AX (red) greater than in 1198, BA, or control treated PC3 cells whereas immunostain for Mcl-1 (green) was similar (x200). In PC3/shMcl-1 cells (bottom panel), DIF immunostaining for γH2AX was further increased in the 1198 + BA combination (24 h) but less in 1198 and BA and none in control. Mcl-1 immunostaining was weak. (B) DIF of PC3/shMcl-1 cells treated with 1 μM Dox for 4 h showed greater immunostaining of γH2AX compared to PC3/shGFP control cells (x100). Mcl-1 immunostain was greater in PC3/shGFP compared to PC3/shMcl-1 cells. DAPI staining of nucleus is shown below DIF. (C) Trypan blue exclusion assay showed that 1 μM Dox (48 h) significantly increased cell death in PC3/shMcl-1 (M3) compared to PC3/shGFP control cells (*, P
    Figure Legend Snippet: Mcl-1 knockdown in PC3 increases DNA damage-associated γH2AX immunostain after 1198 + BA or Dox treatment (A) DIF (top panel) showed that the 1198 + BA combination (24 h) increased immunostaining for γH2AX (red) greater than in 1198, BA, or control treated PC3 cells whereas immunostain for Mcl-1 (green) was similar (x200). In PC3/shMcl-1 cells (bottom panel), DIF immunostaining for γH2AX was further increased in the 1198 + BA combination (24 h) but less in 1198 and BA and none in control. Mcl-1 immunostaining was weak. (B) DIF of PC3/shMcl-1 cells treated with 1 μM Dox for 4 h showed greater immunostaining of γH2AX compared to PC3/shGFP control cells (x100). Mcl-1 immunostain was greater in PC3/shGFP compared to PC3/shMcl-1 cells. DAPI staining of nucleus is shown below DIF. (C) Trypan blue exclusion assay showed that 1 μM Dox (48 h) significantly increased cell death in PC3/shMcl-1 (M3) compared to PC3/shGFP control cells (*, P

    Techniques Used: Immunostaining, Staining, Trypan Blue Exclusion Assay

    14) Product Images from "Expression of aquaporin 5 in primary carcinoma and lymph node metastatic carcinoma of non-small cell lung cancer"

    Article Title: Expression of aquaporin 5 in primary carcinoma and lymph node metastatic carcinoma of non-small cell lung cancer

    Journal: Oncology Letters

    doi: 10.3892/ol.2015.3108

    Aquaporin 5 expression in (A) adenocarcinoma and (B) lymph node metastasis (labeled streptavidin biotin staining; magnification, x200).
    Figure Legend Snippet: Aquaporin 5 expression in (A) adenocarcinoma and (B) lymph node metastasis (labeled streptavidin biotin staining; magnification, x200).

    Techniques Used: Expressing, Labeling, Staining

    15) Product Images from "Caspase inhibition impaired the neural stem/progenitor cell response after cortical ischemia in mice"

    Article Title: Caspase inhibition impaired the neural stem/progenitor cell response after cortical ischemia in mice

    Journal: Oncotarget

    doi: 10.18632/oncotarget.6803

    Assessment of cortical neurogenesis and migration after treatment with Q-VD-OPh late after stroke A. The experimental design where animals subjected to cortical ischemia and treated either with Q-VD-OPh (QVD) or vehicle (Veh). P = postnatal day B. Confocal images show BrdU (green) and NeuN (red) staining in the peri-infarct cortex. The arrowhead in B1. indicates a BrdU+ cell for which no colocalization with NeuN was detected, while the arrow in B2. points to one of the rare cells where colocalization was considered. C Analysis of DCX+ cells in the peri-infarct cortex 16 weeks after induction of ischemia. The images show DCX+ cells in the peri-infarct cortex of the treatment groups, and the bar graph shows quantification data. * P = 0.02, *** P
    Figure Legend Snippet: Assessment of cortical neurogenesis and migration after treatment with Q-VD-OPh late after stroke A. The experimental design where animals subjected to cortical ischemia and treated either with Q-VD-OPh (QVD) or vehicle (Veh). P = postnatal day B. Confocal images show BrdU (green) and NeuN (red) staining in the peri-infarct cortex. The arrowhead in B1. indicates a BrdU+ cell for which no colocalization with NeuN was detected, while the arrow in B2. points to one of the rare cells where colocalization was considered. C Analysis of DCX+ cells in the peri-infarct cortex 16 weeks after induction of ischemia. The images show DCX+ cells in the peri-infarct cortex of the treatment groups, and the bar graph shows quantification data. * P = 0.02, *** P

    Techniques Used: Migration, Staining

    16) Product Images from "Keratectasia After Laser In Situ Keratomileusis"

    Article Title: Keratectasia After Laser In Situ Keratomileusis

    Journal:

    doi: 10.1001/archophthalmol.2008.544

    Semiquantitative immunostaining results for all antibodies. A, Staining intensity for α 1 -proteinase inhibitor (α 1 -PI). B, Nuclear staining intensity for Sp1 in corneal epithelial cells and keratocytes in the corneas with keratectasia (open
    Figure Legend Snippet: Semiquantitative immunostaining results for all antibodies. A, Staining intensity for α 1 -proteinase inhibitor (α 1 -PI). B, Nuclear staining intensity for Sp1 in corneal epithelial cells and keratocytes in the corneas with keratectasia (open

    Techniques Used: Immunostaining, Staining

    Immunostaining for Sp1. A, Healthy control. B, Cornea with keratectasia. C, Cornea with keratoconus. Note that the intensity of the Sp1 nuclear staining is much lower in the epithelium and keratocytes of the healthy cornea and the cornea with keratectasia
    Figure Legend Snippet: Immunostaining for Sp1. A, Healthy control. B, Cornea with keratectasia. C, Cornea with keratoconus. Note that the intensity of the Sp1 nuclear staining is much lower in the epithelium and keratocytes of the healthy cornea and the cornea with keratectasia

    Techniques Used: Immunostaining, Staining

    17) Product Images from "An Immunohistochemical Method for Identifying Fibroblasts in Formalin-fixed, Paraffin-embedded Tissue"

    Article Title: An Immunohistochemical Method for Identifying Fibroblasts in Formalin-fixed, Paraffin-embedded Tissue

    Journal: Journal of Histochemistry and Cytochemistry

    doi: 10.1369/jhc.7A7287.2007

    TE-7 stains cells below the epidermis in normal skin tissue. Human dermis was collected from breast tissue, fixed, and paraffin-embedded. Slides were cut and stained with an IgG1 isotype control or the TE-7 antibody as described in Materials and Methods.
    Figure Legend Snippet: TE-7 stains cells below the epidermis in normal skin tissue. Human dermis was collected from breast tissue, fixed, and paraffin-embedded. Slides were cut and stained with an IgG1 isotype control or the TE-7 antibody as described in Materials and Methods.

    Techniques Used: Staining

    18) Product Images from "Dysregulation of follicle development in a mouse model of premature ovarian insufficiency"

    Article Title: Dysregulation of follicle development in a mouse model of premature ovarian insufficiency

    Journal: Reproduction (Cambridge, England)

    doi: 10.1530/REP-16-0091

    Analysis of basal lamina, theca cells and laminin by immunohistochemistry. (A) Representative images defining how follicle BL was classified as either ≤50% or > 50 BL defined. (B) Proportion of Control and DM follicles at 9 weeks of age (Control n = 11 follicles; n = 3 mice, DM n = 9 follicles; n = 3 mice) classified as having less than or equal to 50% or more than 50% BL defined. (C and D) The theca cell depth and the number of theca cell layers are both reduced in DM follicles compared with Controls at 9 weeks of age (Control n = 106 follicles; n = 3 mice, DM n = 28 follicles; n = 3 mice). (E) Laminin detection in ovary sections using IHC revealed that DM follicles at the secondary stage (stage 4) have a higher laminin content in the theca compartment than Controls at 9 weeks of age. Results are expressed as mean ± s.e.m . Numbers in columns represent number of follicles. * P ≤ 0.05.
    Figure Legend Snippet: Analysis of basal lamina, theca cells and laminin by immunohistochemistry. (A) Representative images defining how follicle BL was classified as either ≤50% or > 50 BL defined. (B) Proportion of Control and DM follicles at 9 weeks of age (Control n = 11 follicles; n = 3 mice, DM n = 9 follicles; n = 3 mice) classified as having less than or equal to 50% or more than 50% BL defined. (C and D) The theca cell depth and the number of theca cell layers are both reduced in DM follicles compared with Controls at 9 weeks of age (Control n = 106 follicles; n = 3 mice, DM n = 28 follicles; n = 3 mice). (E) Laminin detection in ovary sections using IHC revealed that DM follicles at the secondary stage (stage 4) have a higher laminin content in the theca compartment than Controls at 9 weeks of age. Results are expressed as mean ± s.e.m . Numbers in columns represent number of follicles. * P ≤ 0.05.

    Techniques Used: Immunohistochemistry, Mouse Assay

    19) Product Images from "Vascular endothelial growth factor-B expression in postischemic rat brain"

    Article Title: Vascular endothelial growth factor-B expression in postischemic rat brain

    Journal: Vascular Cell

    doi: 10.1186/2045-824X-5-8

    VEGF-B (left column, green), cell-type marker (second column from left, red), DAPI (third column from left, blue), and merged (right column, white arrows) staining of cells in the cerebral cortex ischemic border zone 1 and 7 days after MCAO. Cell-type markers are ( A ) MAP2 (neurons), ( B ) CD11b (macrophages/microglia), ( C ) GFAP (astrocytes), and ( D ) vWF (endothelial cells). Colocalization of VEGF-B with MAP2 and CD11b, but not GFAP or vWF, was detected. Bars, 20 μm.
    Figure Legend Snippet: VEGF-B (left column, green), cell-type marker (second column from left, red), DAPI (third column from left, blue), and merged (right column, white arrows) staining of cells in the cerebral cortex ischemic border zone 1 and 7 days after MCAO. Cell-type markers are ( A ) MAP2 (neurons), ( B ) CD11b (macrophages/microglia), ( C ) GFAP (astrocytes), and ( D ) vWF (endothelial cells). Colocalization of VEGF-B with MAP2 and CD11b, but not GFAP or vWF, was detected. Bars, 20 μm.

    Techniques Used: Marker, Staining

    20) Product Images from "Retinoic Acid and Environmental Enrichment Alter Subventricular Zone and Striatal Neurogenesis after Stroke"

    Article Title: Retinoic Acid and Environmental Enrichment Alter Subventricular Zone and Striatal Neurogenesis after Stroke

    Journal: Experimental neurology

    doi: 10.1016/j.expneurol.2008.08.006

    SVZ PSA-NCAM expression and neuroblast proliferation after stroke
    Figure Legend Snippet: SVZ PSA-NCAM expression and neuroblast proliferation after stroke

    Techniques Used: Expressing

    21) Product Images from "Protective Role of Surfactant Protein-D Against Lung Injury and Oxidative Stress Induced by Nitrogen Mustard"

    Article Title: Protective Role of Surfactant Protein-D Against Lung Injury and Oxidative Stress Induced by Nitrogen Mustard

    Journal: Toxicological Sciences

    doi: 10.1093/toxsci/kfy188

    Effects of loss of SP-D on NM-induced COX-2 and Pro-SP-C expression. Histological sections, prepared 14 days after treatment of WT and SP-D −/− mice with PBS or NM, were stained with antibody to COX-2 (upper panels) or Pro-SP-C (lower panels) . Binding was visualized using a DAB peroxidase substrate kit. One representative section (staining intensity, 2) from 3 to 4 mice/treatment group is shown. Magnification, 60×; arrows, macrophages; arrowheads, Type II cells.
    Figure Legend Snippet: Effects of loss of SP-D on NM-induced COX-2 and Pro-SP-C expression. Histological sections, prepared 14 days after treatment of WT and SP-D −/− mice with PBS or NM, were stained with antibody to COX-2 (upper panels) or Pro-SP-C (lower panels) . Binding was visualized using a DAB peroxidase substrate kit. One representative section (staining intensity, 2) from 3 to 4 mice/treatment group is shown. Magnification, 60×; arrows, macrophages; arrowheads, Type II cells.

    Techniques Used: Expressing, Mouse Assay, Staining, Binding Assay

    22) Product Images from "Subacute administration of both methcathinone and manganese causes basal ganglia damage in mice resembling that in methcathinone abusers"

    Article Title: Subacute administration of both methcathinone and manganese causes basal ganglia damage in mice resembling that in methcathinone abusers

    Journal: Journal of Neural Transmission

    doi: 10.1007/s00702-019-02110-z

    Expression levels of DAT, VMAT2 and GAD 65/67 in the striatum in Mcat-, Mn- and Mcat/Mn-treated animals. Immunostaining of the striatum was measured as optical density using Image J. *** p
    Figure Legend Snippet: Expression levels of DAT, VMAT2 and GAD 65/67 in the striatum in Mcat-, Mn- and Mcat/Mn-treated animals. Immunostaining of the striatum was measured as optical density using Image J. *** p

    Techniques Used: Expressing, Immunostaining

    23) Product Images from "Co-culturing of follicles with interstitial cells in collagen gel reproduce follicular development accompanied with theca cell layer formation"

    Article Title: Co-culturing of follicles with interstitial cells in collagen gel reproduce follicular development accompanied with theca cell layer formation

    Journal: Reproductive Biology and Endocrinology : RB & E

    doi: 10.1186/1477-7827-9-159

    Immunohistochemical localization of the cell markers in mouse ovaries . Immunohistochemistry of (a) Flk-1, (b) F4/80, (c) fibronectin, (d) laminin, (e) tenascin, (f) collagen type IV, (g) THY1, and (h) CYP 17A-1 in mouse ovaries. (a, b, d-h) visualized by immunofluorescence and (c) visualized by ABC staining. O, oocyte; G, granulosa cells; T, theca cells. Scale bars = 25 μm.
    Figure Legend Snippet: Immunohistochemical localization of the cell markers in mouse ovaries . Immunohistochemistry of (a) Flk-1, (b) F4/80, (c) fibronectin, (d) laminin, (e) tenascin, (f) collagen type IV, (g) THY1, and (h) CYP 17A-1 in mouse ovaries. (a, b, d-h) visualized by immunofluorescence and (c) visualized by ABC staining. O, oocyte; G, granulosa cells; T, theca cells. Scale bars = 25 μm.

    Techniques Used: Immunohistochemistry, Immunofluorescence, Staining

    Immunohistochemical localization of the theca cell markers in cultured follicles . Immunohistochemistry of (a-c) fibronectin, (d-f) laminin, (g-i) tenascin, (j-l) collagen type IV, (m-o) THY1, and (p-r) CYP17A-1. (f, f'), (i, i'), (l, l'), (o, o'), and (r, r'), are same view respectively. (f', i', l', o', r') are DAPI staining. (d-r') visualized by immunofluorescence and (a-c) visualized by ABC staining. (a, d, g, j, m, p) were cultured follicles for 5 days, (b, e, h, k, n, q) were cultured follicles for 0 day (isolated follicle), and (c, f, f', i, i', l, l', o, o', r, r') were interstitial cells distanced from follicles. The arrowheads indicate each signal. O, oocyte; G, granulosa cells; T, theca cells. Scale bars = 25 μm.
    Figure Legend Snippet: Immunohistochemical localization of the theca cell markers in cultured follicles . Immunohistochemistry of (a-c) fibronectin, (d-f) laminin, (g-i) tenascin, (j-l) collagen type IV, (m-o) THY1, and (p-r) CYP17A-1. (f, f'), (i, i'), (l, l'), (o, o'), and (r, r'), are same view respectively. (f', i', l', o', r') are DAPI staining. (d-r') visualized by immunofluorescence and (a-c) visualized by ABC staining. (a, d, g, j, m, p) were cultured follicles for 5 days, (b, e, h, k, n, q) were cultured follicles for 0 day (isolated follicle), and (c, f, f', i, i', l, l', o, o', r, r') were interstitial cells distanced from follicles. The arrowheads indicate each signal. O, oocyte; G, granulosa cells; T, theca cells. Scale bars = 25 μm.

    Techniques Used: Immunohistochemistry, Cell Culture, Staining, Immunofluorescence, Isolation

    24) Product Images from "Beta-4 tubulin identifies a primitive cell source for oligodendrocytes in the mammalian brain"

    Article Title: Beta-4 tubulin identifies a primitive cell source for oligodendrocytes in the mammalian brain

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    doi: 10.1523/JNEUROSCI.1027-09.2009

    Antibodies to beta-4 tubulin (βT4) identify a population of undifferentiated cells in the subventricular zone (SVZ) of the adult human brain. The SVZ in control brain contains sparse cells that label intensely with antibody to βT4 ( A , arrows). βT4-positive cells in the SVZ have scant cytoplasm and occasional thin processes ( B ). The SVZ adjacent to demyelinated lesions in multiple sclerosis (MS) brain contains numerous βT4 cells that are often in doublets and clusters ( C , D ). The asterisks in A and C show that ciliated ependymal cells are also βT4-positive. The bar graph in Panel E demonstrates that the number (mean ± s.d.) of βT4 cells in SVZ adjacent to lesions of MS is significantly increased compared to SVZs bordering myelinated white matter ( P
    Figure Legend Snippet: Antibodies to beta-4 tubulin (βT4) identify a population of undifferentiated cells in the subventricular zone (SVZ) of the adult human brain. The SVZ in control brain contains sparse cells that label intensely with antibody to βT4 ( A , arrows). βT4-positive cells in the SVZ have scant cytoplasm and occasional thin processes ( B ). The SVZ adjacent to demyelinated lesions in multiple sclerosis (MS) brain contains numerous βT4 cells that are often in doublets and clusters ( C , D ). The asterisks in A and C show that ciliated ependymal cells are also βT4-positive. The bar graph in Panel E demonstrates that the number (mean ± s.d.) of βT4 cells in SVZ adjacent to lesions of MS is significantly increased compared to SVZs bordering myelinated white matter ( P

    Techniques Used: Mass Spectrometry

    25) Product Images from "Mn (III) Tetrakis (4-Benzoic Acid) Porphyrin Protects Against Neuronal and Glial Oxidative Stress and Death after Spinal Cord Injury"

    Article Title: Mn (III) Tetrakis (4-Benzoic Acid) Porphyrin Protects Against Neuronal and Glial Oxidative Stress and Death after Spinal Cord Injury

    Journal: CNS & neurological disorders drug targets

    doi:

    MnTBAP protection against the death of oligodendrocytes. Upper panel, photomicrographs of rat spinal cord sections from the animals treated with MnTBAP or saline at 2.3 mm rostral to the epicenter immuno-stained with anti-CC1. A-B , lower magnificat-ion; A’-B’ , higher magnification of A-B . A-A’ , saline-treated and B-B’ are MnTBAP treated sections. Scale, 100 µm. Lower panel, quantitative comparison of numbers of oligodendrocytes between MnTBAP and saline treatments by counting CC1-positive cells in the sections at different distances from the epicenter. The optimal dose of MnTBAP significantly increased the number of oligodendrocytes in the sections 1.8 to 2.8 mm rostral from the epicenter as indicated by asterisks (*).
    Figure Legend Snippet: MnTBAP protection against the death of oligodendrocytes. Upper panel, photomicrographs of rat spinal cord sections from the animals treated with MnTBAP or saline at 2.3 mm rostral to the epicenter immuno-stained with anti-CC1. A-B , lower magnificat-ion; A’-B’ , higher magnification of A-B . A-A’ , saline-treated and B-B’ are MnTBAP treated sections. Scale, 100 µm. Lower panel, quantitative comparison of numbers of oligodendrocytes between MnTBAP and saline treatments by counting CC1-positive cells in the sections at different distances from the epicenter. The optimal dose of MnTBAP significantly increased the number of oligodendrocytes in the sections 1.8 to 2.8 mm rostral from the epicenter as indicated by asterisks (*).

    Techniques Used: Staining

    26) Product Images from "Enhanced NMDA receptor NR1 phosphorylation and neuronal activity in the arcuate nucleus of hypothalamus following peripheral inflammation"

    Article Title: Enhanced NMDA receptor NR1 phosphorylation and neuronal activity in the arcuate nucleus of hypothalamus following peripheral inflammation

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2010.190

    MK-801 (NMDA receptor antagonist) and CNQX (non-NMDA receptor antagonist) inhibit spontaneous discharge of ARC neurons in inflamed rats. (A) A significant decrease in neuronal discharge frequency was observed following MK-801 application (300 μmol/L) in inflamed rats ( n =11; P
    Figure Legend Snippet: MK-801 (NMDA receptor antagonist) and CNQX (non-NMDA receptor antagonist) inhibit spontaneous discharge of ARC neurons in inflamed rats. (A) A significant decrease in neuronal discharge frequency was observed following MK-801 application (300 μmol/L) in inflamed rats ( n =11; P

    Techniques Used:

    27) Product Images from "Overexpression of neuritin in gastric cancer"

    Article Title: Overexpression of neuritin in gastric cancer

    Journal: Oncology Letters

    doi: 10.3892/ol.2015.3793

    Expression of neuritin and β-actin in GC and adjacent NC tissues, as determined using western blot analysis. β-actin acted as an internal control. GC, gastric cancer; NC, normal control.
    Figure Legend Snippet: Expression of neuritin and β-actin in GC and adjacent NC tissues, as determined using western blot analysis. β-actin acted as an internal control. GC, gastric cancer; NC, normal control.

    Techniques Used: Expressing, Western Blot

    Representative images of neuritin expression in adjacent normal tissues in (A) patient 1 and (B) patient 2 (magnification, ×200).
    Figure Legend Snippet: Representative images of neuritin expression in adjacent normal tissues in (A) patient 1 and (B) patient 2 (magnification, ×200).

    Techniques Used: Expressing

    mRNA expression of neuritin in GC and adjacent NC tissues, as determined by reverse transcription-polymerase chain reaction. GC, gastric cancer; NC, normal control.
    Figure Legend Snippet: mRNA expression of neuritin in GC and adjacent NC tissues, as determined by reverse transcription-polymerase chain reaction. GC, gastric cancer; NC, normal control.

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction

    Represent image of negative control staining for neuritin, with no neuritin expression (magnification, ×200).
    Figure Legend Snippet: Represent image of negative control staining for neuritin, with no neuritin expression (magnification, ×200).

    Techniques Used: Negative Control, Staining, Expressing

    Representative images of neuritin expression in gastric cancer tissues in (A) patient 1 and (B) patient 2 (magnification, ×200).
    Figure Legend Snippet: Representative images of neuritin expression in gastric cancer tissues in (A) patient 1 and (B) patient 2 (magnification, ×200).

    Techniques Used: Expressing

    Association between neuritin expression and the clinicopathological parameters of the patients
    Figure Legend Snippet: Association between neuritin expression and the clinicopathological parameters of the patients

    Techniques Used: Expressing

    28) Product Images from "Stem cell marker TRA-1-60 is expressed in foetal and adult kidney and upregulated in tubulo-interstitial disease"

    Article Title: Stem cell marker TRA-1-60 is expressed in foetal and adult kidney and upregulated in tubulo-interstitial disease

    Journal: Histochemistry and cell biology

    doi: 10.1007/s00418-010-0741-7

    TRA-1-60 antigen expression in tubulo-interstitial damage. Serial sections of areas of renal cortex with tubulo-interstitial damage were stained for EMA ( a , d , g ), TRA-1-60 ( b , e , h ) and LTA ( c , f , i ). b Shows normal kidney with accumulation of TRA-1-60 expressing cells ( arrows ) in scarred areas marked by lymphocyte infiltration ( arrowheads ). The TRA-1-60 expressing tubules were also positive for EMA ( a arrows ) but not LTA lectin ( c arrows ) on serial sections. Increased TRA-1-60 expression by tubular cells in the cortex affected by ATN ( e arrows ) and GN ( h arrows ). On serial sections the TRA-1-60 expressing tubules were EMA positive ( d and g , respectively, arrows ) and LTA lectin negative ( f and i , respectively, arrows ). j – l Show negative controls: mouse IgG2 for EMA antibody ( j ), mouse IgM for TRA-1-60, with TBS only for LTA lectin. Scale bar 60 μm
    Figure Legend Snippet: TRA-1-60 antigen expression in tubulo-interstitial damage. Serial sections of areas of renal cortex with tubulo-interstitial damage were stained for EMA ( a , d , g ), TRA-1-60 ( b , e , h ) and LTA ( c , f , i ). b Shows normal kidney with accumulation of TRA-1-60 expressing cells ( arrows ) in scarred areas marked by lymphocyte infiltration ( arrowheads ). The TRA-1-60 expressing tubules were also positive for EMA ( a arrows ) but not LTA lectin ( c arrows ) on serial sections. Increased TRA-1-60 expression by tubular cells in the cortex affected by ATN ( e arrows ) and GN ( h arrows ). On serial sections the TRA-1-60 expressing tubules were EMA positive ( d and g , respectively, arrows ) and LTA lectin negative ( f and i , respectively, arrows ). j – l Show negative controls: mouse IgG2 for EMA antibody ( j ), mouse IgM for TRA-1-60, with TBS only for LTA lectin. Scale bar 60 μm

    Techniques Used: Expressing, Staining

    TRA-1-60 and Pax-2 immunostaining of normal human kidney at 10 weeks of gestation. a and c show TRA-1-60 expression in the nephrogenic zone. a TRA-1-60 was intensely expressed on the apical surface of the ureteric bud and putative collecting ducts. c TRA-1-60 expression in the ureteric bud tip at higher magnification. b and d show Pax-2 expression in the nephrogenic zone. b Transcription factor Pax-2 was strongly expressed in the ureteric bud, collecting duct and also in condensing metanephric mesenchyme and derivatives including comma-shaped bodies. A lower level of expression was noticeable in maturing nephrons. d Pax-2 expression in the ureteric bud, condensing mesenchyme and S-shaped bodies at higher magnification. e Mouse IgM, isotype control for TRA-1-60 immunostaining. f Rabbit IgG negative control for Pax-2 staining. ub ureteric bud, cd collecting duct, mm metanephric mesenchyme, cb comma-shaped body, Sb S-shaped body, nephr nephron. Scale bars 60 μm
    Figure Legend Snippet: TRA-1-60 and Pax-2 immunostaining of normal human kidney at 10 weeks of gestation. a and c show TRA-1-60 expression in the nephrogenic zone. a TRA-1-60 was intensely expressed on the apical surface of the ureteric bud and putative collecting ducts. c TRA-1-60 expression in the ureteric bud tip at higher magnification. b and d show Pax-2 expression in the nephrogenic zone. b Transcription factor Pax-2 was strongly expressed in the ureteric bud, collecting duct and also in condensing metanephric mesenchyme and derivatives including comma-shaped bodies. A lower level of expression was noticeable in maturing nephrons. d Pax-2 expression in the ureteric bud, condensing mesenchyme and S-shaped bodies at higher magnification. e Mouse IgM, isotype control for TRA-1-60 immunostaining. f Rabbit IgG negative control for Pax-2 staining. ub ureteric bud, cd collecting duct, mm metanephric mesenchyme, cb comma-shaped body, Sb S-shaped body, nephr nephron. Scale bars 60 μm

    Techniques Used: Immunostaining, Expressing, Negative Control, Staining

    29) Product Images from "DECONSTRUCTING THE PERINEURONAL NET: CELLULAR CONTRIBUTIONS AND MOLECULAR COMPOSITION OF THE NEURONAL EXTRACELLULAR MATRIX"

    Article Title: DECONSTRUCTING THE PERINEURONAL NET: CELLULAR CONTRIBUTIONS AND MOLECULAR COMPOSITION OF THE NEURONAL EXTRACELLULAR MATRIX

    Journal: Neuroscience

    doi: 10.1016/j.neuroscience.2012.05.055

    Treatment with AraC and KCl did not disrupt neuronal development and survival. (A–D) Cells at 12 DIV were stained for MAP2 (red) and activated caspase-3 (green) to assess the gross morphology of neurons and the rate of cell death in each treatment
    Figure Legend Snippet: Treatment with AraC and KCl did not disrupt neuronal development and survival. (A–D) Cells at 12 DIV were stained for MAP2 (red) and activated caspase-3 (green) to assess the gross morphology of neurons and the rate of cell death in each treatment

    Techniques Used: Staining

    30) Product Images from "The influence of the lack of insulin receptor substrate 2 (IRS2) on the thyroid gland"

    Article Title: The influence of the lack of insulin receptor substrate 2 (IRS2) on the thyroid gland

    Journal: Scientific Reports

    doi: 10.1038/s41598-019-42198-7

    Immunohistochemical reaction for active caspase-3 and TUNEL assay in thyroid follicular cells. Follicular active caspase 3-positive cells in WT female ( A ) and male animals ( D ), and IRS2-KO female ( B–C arrows) and male ( E – F arrows) mice. TUNEL-positive follicular cells were less numerous in the WT female ( G ) and male ( I ) mice than in the IRS2-KO female ( H , arrows) and male ( J , arrows) animals. Scale bars: A, B, D, E = 60 µm; C, F = 20 µm; G–J = 12 µm.
    Figure Legend Snippet: Immunohistochemical reaction for active caspase-3 and TUNEL assay in thyroid follicular cells. Follicular active caspase 3-positive cells in WT female ( A ) and male animals ( D ), and IRS2-KO female ( B–C arrows) and male ( E – F arrows) mice. TUNEL-positive follicular cells were less numerous in the WT female ( G ) and male ( I ) mice than in the IRS2-KO female ( H , arrows) and male ( J , arrows) animals. Scale bars: A, B, D, E = 60 µm; C, F = 20 µm; G–J = 12 µm.

    Techniques Used: Immunohistochemistry, TUNEL Assay, Mouse Assay

    Percentage of apoptosis in thyroid follicular cells of WT and IRS2-KO mice of both sexes. The plots show the comparison between wild-type (WT) and IRS2 deficient animals (KO), regarding the gender and regions of the gland (MM: male marginal; MC: male central; FM: female marginal; FC: female central), and the values are expressed as mean ± SEM. ( a ) Graphic showing the percentage of apoptosis by active caspase-3-positive follicular cells. Significant differences are defined as: * p
    Figure Legend Snippet: Percentage of apoptosis in thyroid follicular cells of WT and IRS2-KO mice of both sexes. The plots show the comparison between wild-type (WT) and IRS2 deficient animals (KO), regarding the gender and regions of the gland (MM: male marginal; MC: male central; FM: female marginal; FC: female central), and the values are expressed as mean ± SEM. ( a ) Graphic showing the percentage of apoptosis by active caspase-3-positive follicular cells. Significant differences are defined as: * p

    Techniques Used: Mouse Assay

    31) Product Images from "Voluntary Exercise Induces Astrocytic Structural Plasticity in the Globus Pallidus"

    Article Title: Voluntary Exercise Induces Astrocytic Structural Plasticity in the Globus Pallidus

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2016.00165

    Olig2-lineage astrocytes are relatively abundant in the GP. (A) Diagram showing the GP and cortex (Cx) of a mouse coronal section (0.46 mm posterior to the bregma). (B) Low-magnification view of GFP-positive Olig2-lineage cells in Olig2 KICreER/WT ; ROSA26-GAP43-EGFP mice (the section is at the same level as that in A ). Olig2-lineage cells preferentially cluster in the GP (demarcated with a dotted white line). (C,D) Higher-magnification views of Olig2-lineage cells in the Cx (C) and the GP (D) . Arrows indicate cells with polydendric morphology and arrowheads indicate cells with bushy morphology. Note that bushy-type cells predominate in the GP, while polydendric-type cells do so in the Cx (see also I ). (E–H) Double immunofluorescence with cell marker antibodies shows that polydendric-type cells in the Cx are NG2 proteoglycan-positive ( E2 ; arrowhead, OPC/NG2 glia) or APC-positive ( F2 ; arrowhead, oligodendrocyte). The polydendric-type cells in the GP are also positive for APC ( G2 ; arrowhead, oligodendrocyte) and bushy-type cells in the cortex are S100β-positive ( H2 ; arrowhead, mature astrocyte). Scale bars: (B) 1 mm; (C) 30 μm (also for D ); (H) 30 μm (also for E–G ). (I) Quantitative analyses of Olig2-lineage cells in the Cx and the GP revealed that 88% of cells are polydendric-type (OPCs/NG2 glia or mature oligodendrocytes) in the Cx, while 87% are bushy-type (mature astrocytes) in the GP. (J) Lower-magnification views of a triple-immunolabeled section. The GP had many PV-positive (GABAergic) neurons (J1) , while the neighboring striatum showed fewer. The border between the two regions is indicated by a dotted line. The GP also expressed GAT-3 strongly (J2) . Olig2-lineage astrocytes were visualized by their GFP immunoreactivity (J3) , which co-localized with GAT-3. Panel (J4) is the merged image of (J1–J3). (K) An Olig2-lineage astrocyte in the cerebral cortex also expresses GAT-3. PV, parvalbumin; CPu; caudate-putamen; GP, globus pallidus. Scale bar: (J) 200 μm; (K) 20 μm.
    Figure Legend Snippet: Olig2-lineage astrocytes are relatively abundant in the GP. (A) Diagram showing the GP and cortex (Cx) of a mouse coronal section (0.46 mm posterior to the bregma). (B) Low-magnification view of GFP-positive Olig2-lineage cells in Olig2 KICreER/WT ; ROSA26-GAP43-EGFP mice (the section is at the same level as that in A ). Olig2-lineage cells preferentially cluster in the GP (demarcated with a dotted white line). (C,D) Higher-magnification views of Olig2-lineage cells in the Cx (C) and the GP (D) . Arrows indicate cells with polydendric morphology and arrowheads indicate cells with bushy morphology. Note that bushy-type cells predominate in the GP, while polydendric-type cells do so in the Cx (see also I ). (E–H) Double immunofluorescence with cell marker antibodies shows that polydendric-type cells in the Cx are NG2 proteoglycan-positive ( E2 ; arrowhead, OPC/NG2 glia) or APC-positive ( F2 ; arrowhead, oligodendrocyte). The polydendric-type cells in the GP are also positive for APC ( G2 ; arrowhead, oligodendrocyte) and bushy-type cells in the cortex are S100β-positive ( H2 ; arrowhead, mature astrocyte). Scale bars: (B) 1 mm; (C) 30 μm (also for D ); (H) 30 μm (also for E–G ). (I) Quantitative analyses of Olig2-lineage cells in the Cx and the GP revealed that 88% of cells are polydendric-type (OPCs/NG2 glia or mature oligodendrocytes) in the Cx, while 87% are bushy-type (mature astrocytes) in the GP. (J) Lower-magnification views of a triple-immunolabeled section. The GP had many PV-positive (GABAergic) neurons (J1) , while the neighboring striatum showed fewer. The border between the two regions is indicated by a dotted line. The GP also expressed GAT-3 strongly (J2) . Olig2-lineage astrocytes were visualized by their GFP immunoreactivity (J3) , which co-localized with GAT-3. Panel (J4) is the merged image of (J1–J3). (K) An Olig2-lineage astrocyte in the cerebral cortex also expresses GAT-3. PV, parvalbumin; CPu; caudate-putamen; GP, globus pallidus. Scale bar: (J) 200 μm; (K) 20 μm.

    Techniques Used: Mouse Assay, Immunofluorescence, Marker, Immunolabeling

    32) Product Images from "Contextual Effect of Repression of Bone Morphogenetic Protein Activity in Prostate Cancer"

    Article Title: Contextual Effect of Repression of Bone Morphogenetic Protein Activity in Prostate Cancer

    Journal: Endocrine-related cancer

    doi: 10.1530/ERC-13-0100

    Overexpression of Noggin in CAF cells promotes anaplastic growth of tumor cells. Co-immunofluorescence staining showing presence of de-differentiated cells with CK8 (green) and Vimentin (red) taken at 200×. Arrow , co-localized expression. Bar
    Figure Legend Snippet: Overexpression of Noggin in CAF cells promotes anaplastic growth of tumor cells. Co-immunofluorescence staining showing presence of de-differentiated cells with CK8 (green) and Vimentin (red) taken at 200×. Arrow , co-localized expression. Bar

    Techniques Used: Over Expression, Immunofluorescence, Staining, Expressing

    33) Product Images from "Pentosan Polysulfate Treatment of Mucopolysaccharidosis Type IIIA Mice"

    Article Title: Pentosan Polysulfate Treatment of Mucopolysaccharidosis Type IIIA Mice

    Journal: JIMD Reports

    doi: 10.1007/8904_2018_96

    IL-B4 staining in MPS IIIA mice treated with PPS by ICV infusion. Panels ( a – d ) show representative images from 16-week-old, sham treated MPS IIIA mice (ventricle, cortex, hippocampus and lateral septum, respectively). Panels ( e – h ) show representative images from MPS IIIA mice of the same age that received ICV PPS infusions. A schematic showing the site of injection (arrow) is provided in the lower left
    Figure Legend Snippet: IL-B4 staining in MPS IIIA mice treated with PPS by ICV infusion. Panels ( a – d ) show representative images from 16-week-old, sham treated MPS IIIA mice (ventricle, cortex, hippocampus and lateral septum, respectively). Panels ( e – h ) show representative images from MPS IIIA mice of the same age that received ICV PPS infusions. A schematic showing the site of injection (arrow) is provided in the lower left

    Techniques Used: Staining, Mouse Assay, Injection

    34) Product Images from "Orexin A-Mediated Modulation of Reproductive Activities in Testis of Normal and Cryptorchid Dogs: Possible Model for Studying Relationships Between Energy Metabolism and Reproductive Control"

    Article Title: Orexin A-Mediated Modulation of Reproductive Activities in Testis of Normal and Cryptorchid Dogs: Possible Model for Studying Relationships Between Energy Metabolism and Reproductive Control

    Journal: Frontiers in Endocrinology

    doi: 10.3389/fendo.2019.00816

    17βE secretion in vitro carried out in normal, cryptorchid, and contralateral dog testis. Testicular slices were incubated with OxA alone or with OxA and the OX1R antagonist SB-408124 and the 17βE level in the media monitored after 12 h. Values are normalized per ml of incubation medium. Data are expressed as mean ± SD ( n = 5 samples/group), * p
    Figure Legend Snippet: 17βE secretion in vitro carried out in normal, cryptorchid, and contralateral dog testis. Testicular slices were incubated with OxA alone or with OxA and the OX1R antagonist SB-408124 and the 17βE level in the media monitored after 12 h. Values are normalized per ml of incubation medium. Data are expressed as mean ± SD ( n = 5 samples/group), * p

    Techniques Used: In Vitro, Incubation

    ARO activity evaluated with in vitro tests carried out in normal, cryptorchid, and contralateral dog testis. Testicular slices were incubated in presence of testosterone alone, with OxA, or with both OxA and the OX1R antagonist SB-408124 and 17βE production monitored. Values are normalized per g tissue per hour. Data are expressed as mean ± SD ( n = 5 samples/group), * p
    Figure Legend Snippet: ARO activity evaluated with in vitro tests carried out in normal, cryptorchid, and contralateral dog testis. Testicular slices were incubated in presence of testosterone alone, with OxA, or with both OxA and the OX1R antagonist SB-408124 and 17βE production monitored. Values are normalized per g tissue per hour. Data are expressed as mean ± SD ( n = 5 samples/group), * p

    Techniques Used: Activity Assay, In Vitro, Incubation

    35) Product Images from "Biochemical features of the adhesion G protein-coupled receptor CD97 related to its auto-proteolysis and HeLa cell attachment activities"

    Article Title: Biochemical features of the adhesion G protein-coupled receptor CD97 related to its auto-proteolysis and HeLa cell attachment activities

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2016.89

    HeLa cell attachment assay for Fc-CD97ECD WT and its GPS site mutant and truncated forms. (A) FACS profile of attachment of Fc-CD97ECD WT with several cell lines. Biotin-RA/RB/OVA/BSA and Fc fragment marginally attached to HeLa cells (bottom right panel). (B) FACS profile of HeLa cell attachment with four Fc-CD97ECD proteins. (C) Mean fluorescence intense (MFI) data of HeLa cell attachment with four Fc-CD97ECD proteins. Quantification from three independent experiments: mean±SD. ** P
    Figure Legend Snippet: HeLa cell attachment assay for Fc-CD97ECD WT and its GPS site mutant and truncated forms. (A) FACS profile of attachment of Fc-CD97ECD WT with several cell lines. Biotin-RA/RB/OVA/BSA and Fc fragment marginally attached to HeLa cells (bottom right panel). (B) FACS profile of HeLa cell attachment with four Fc-CD97ECD proteins. (C) Mean fluorescence intense (MFI) data of HeLa cell attachment with four Fc-CD97ECD proteins. Quantification from three independent experiments: mean±SD. ** P

    Techniques Used: Cell Attachment Assay, Mutagenesis, FACS, Fluorescence

    36) Product Images from "Complement system activation contributes to the ependymal damage induced by microbial neuraminidase"

    Article Title: Complement system activation contributes to the ependymal damage induced by microbial neuraminidase

    Journal: Journal of Neuroinflammation

    doi: 10.1186/s12974-016-0576-9

    Quantification of ependymal epithelium disruption in different experimental conditions. a The graph shows the proportion of disrupted ependyma relative to the total ependymal perimeter measured in histological sections. Four experimental situations were analyzed: sham-operated rats ( SHAM ), NA-injected wild-type rats ( WT-NA ), NA-injected C5-inhibitor-treated rats ( INH-NA ), and NA-injected C6-deficient rats ( C6-NA ). Photographs show the appearance of intact ( b ), damaged ( c ), and disrupted ( d ) ependymal epithelium immunostained with anti-vimentin. NA-injected WT rats display 53.5 ± 8.5 % of ependymal epithelium disruption. However, in rats with the complement system inhibited (IHN-NA and C6-NA), this proportion decreases significantly (11.3 ± 2.5 and 7.1 ± 3.3, respectively). Bars represent the mean ± SEM. Different treatments were compared by one-way ANOVA ( F (3,11) = 25,872, P
    Figure Legend Snippet: Quantification of ependymal epithelium disruption in different experimental conditions. a The graph shows the proportion of disrupted ependyma relative to the total ependymal perimeter measured in histological sections. Four experimental situations were analyzed: sham-operated rats ( SHAM ), NA-injected wild-type rats ( WT-NA ), NA-injected C5-inhibitor-treated rats ( INH-NA ), and NA-injected C6-deficient rats ( C6-NA ). Photographs show the appearance of intact ( b ), damaged ( c ), and disrupted ( d ) ependymal epithelium immunostained with anti-vimentin. NA-injected WT rats display 53.5 ± 8.5 % of ependymal epithelium disruption. However, in rats with the complement system inhibited (IHN-NA and C6-NA), this proportion decreases significantly (11.3 ± 2.5 and 7.1 ± 3.3, respectively). Bars represent the mean ± SEM. Different treatments were compared by one-way ANOVA ( F (3,11) = 25,872, P

    Techniques Used: Injection

    Detection of C5b-9 complex and C9 on the ependymal epithelium of rats injected with NA. a – d Immunohistochemistry using anti-C5b-9 showing the injected ( a , c ) and the contralateral ( b , d ) ventricles. Two hours after NA injection, a positive label could be observed on the ependymal surface of the injected ventricle ( c ), which was absent in the contralateral one ( d ). e – g Cryostat 10-μm sections double labeled with anti-C9 ( green ), anti-vimentin ( red ), and the nuclear stain DAPI ( blue ). The ependymal cells of the injected ventricle showed C9 deposits on the apical surface and cilia ( e and g ) that were not present in the contralateral ventricle ( f ). LV lateral ventricle, DAPI , 4,6-diamidine-2-phenylindole dihydrochloride, Ep ependyma, NP nervous parenchyma, CP choroid plexus, Str striatum, Sp septum. ( Arrows ) Damaged cells
    Figure Legend Snippet: Detection of C5b-9 complex and C9 on the ependymal epithelium of rats injected with NA. a – d Immunohistochemistry using anti-C5b-9 showing the injected ( a , c ) and the contralateral ( b , d ) ventricles. Two hours after NA injection, a positive label could be observed on the ependymal surface of the injected ventricle ( c ), which was absent in the contralateral one ( d ). e – g Cryostat 10-μm sections double labeled with anti-C9 ( green ), anti-vimentin ( red ), and the nuclear stain DAPI ( blue ). The ependymal cells of the injected ventricle showed C9 deposits on the apical surface and cilia ( e and g ) that were not present in the contralateral ventricle ( f ). LV lateral ventricle, DAPI , 4,6-diamidine-2-phenylindole dihydrochloride, Ep ependyma, NP nervous parenchyma, CP choroid plexus, Str striatum, Sp septum. ( Arrows ) Damaged cells

    Techniques Used: Injection, Immunohistochemistry, Labeling, Staining

    In vitro effects of NA and complement on the ependymal epithelium. Explants from the septal side of the lateral ventricle wall were placed in culture and treated with NA and/or complement for 2 h. Rat serum was used as a source of complement. The ependyma in the explants was then evaluated by histology. Anti-vimentin allowed the location of the ependyma in the explants ( a , d , g , j ). The squared regions are those magnified in the hematoxylin-eosin staining ( b , e , h , k ). The sialic acid removal by NA was confirmed by binding of the lectin PNA (peanut agglutinin; c , f , i , l ). Ependymal damage occurred in explants treated with NA ( e , k ) and was worsened by the presence of serum ( k ). The concurrence of NA and serum resulted in the loss of epithelium integrity, where gaps could be seen ( arrowheads in l ). Serum alone did not produce such damage ( e ). CM culture medium, NA neuraminidase, Ep ependyma, NP nervous parenchyma. ( Arrows ) Damaged ependymal cells
    Figure Legend Snippet: In vitro effects of NA and complement on the ependymal epithelium. Explants from the septal side of the lateral ventricle wall were placed in culture and treated with NA and/or complement for 2 h. Rat serum was used as a source of complement. The ependyma in the explants was then evaluated by histology. Anti-vimentin allowed the location of the ependyma in the explants ( a , d , g , j ). The squared regions are those magnified in the hematoxylin-eosin staining ( b , e , h , k ). The sialic acid removal by NA was confirmed by binding of the lectin PNA (peanut agglutinin; c , f , i , l ). Ependymal damage occurred in explants treated with NA ( e , k ) and was worsened by the presence of serum ( k ). The concurrence of NA and serum resulted in the loss of epithelium integrity, where gaps could be seen ( arrowheads in l ). Serum alone did not produce such damage ( e ). CM culture medium, NA neuraminidase, Ep ependyma, NP nervous parenchyma. ( Arrows ) Damaged ependymal cells

    Techniques Used: In Vitro, Staining, Binding Assay

    37) Product Images from "Downstream-of-FGFR Is a Fibroblast Growth Factor-Specific Scaffolding Protein and Recruits Corkscrew upon Receptor Activation"

    Article Title: Downstream-of-FGFR Is a Fibroblast Growth Factor-Specific Scaffolding Protein and Recruits Corkscrew upon Receptor Activation

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.24.9.3769-3781.2004

    (A) Activation of the MAPK pathway is important but not sufficient to direct cell migration. Activation of the MAPK pathway wasvisualized with anti-dpERK antibodies (subpanels a to d), the lumen of the tracheal system with the 2A12 antibody in red and terminal cells with the anti-DSRF antibody in green (subpanels e and f). Confocal projections are shown for embryos expressing the following transgenes under the control of the pannier Gal4 driver: UAS dof (subpanel a), UAS dof and UAS btl act (subpanel b), UAS dof600 ΔAR and UAS btl act (subpanel c) and UAS dof600Y515F and UAS btl act (subpanel d). (Subpanels e and f) Embryos expressing UAS dof600 ΔAR or UAS dof600Y515F in a dof −/− background under the control of the btl Gal4 driver are shown. (B) Summary table of the capacity of each transgene to activate dpERK in combination with an activated form of btl . The capacity of each dof transgene to rescue cell migration in dof −/− embryos is also shown in the second column.
    Figure Legend Snippet: (A) Activation of the MAPK pathway is important but not sufficient to direct cell migration. Activation of the MAPK pathway wasvisualized with anti-dpERK antibodies (subpanels a to d), the lumen of the tracheal system with the 2A12 antibody in red and terminal cells with the anti-DSRF antibody in green (subpanels e and f). Confocal projections are shown for embryos expressing the following transgenes under the control of the pannier Gal4 driver: UAS dof (subpanel a), UAS dof and UAS btl act (subpanel b), UAS dof600 ΔAR and UAS btl act (subpanel c) and UAS dof600Y515F and UAS btl act (subpanel d). (Subpanels e and f) Embryos expressing UAS dof600 ΔAR or UAS dof600Y515F in a dof −/− background under the control of the btl Gal4 driver are shown. (B) Summary table of the capacity of each transgene to activate dpERK in combination with an activated form of btl . The capacity of each dof transgene to rescue cell migration in dof −/− embryos is also shown in the second column.

    Techniques Used: Activation Assay, Migration, Expressing, Activated Clotting Time Assay

    (A) Rescue of tracheal cell migration by altered versions of the Dof protein. The lumen of the tracheal system of embryos was visualized with the 2A12 antibody (red) (subpanels a to h and a′ to h′), and terminal cells were visualized with the anti-DSRF antibody (green) (subpanels a′ to h′). Confocal projections of a representative embryo are shown for a wt embryo (subpanels a and a′), for a dof −/− embryo (subpanels b and b′), and for rescued embryos expressing the following transgenes in a dof −/− background under the control of the btl Gal4 driver: UAS dof (subpanels c and c′), UAS dof850 (subpanels d and d′), UAS dof600 (subpanels e and e′), UAS dof484 (subpanels f and f′), UAS dof485-1012 (subpanels g and g′), and UAS dof ΔARΔCC (subpanels h and h′). Abbreviations: DB, dorsal branch; TC, transverse connective; VB, visceral branch; LT, lateral trunk; GB, ganglionic branch. The arrow in subpanel c points to the misrouted VB. (B) Rescue of mesodermal cell migration by altered versions of the Dof protein. The lumen of the tracheal system of embryos was visualized with the 2A12 antibody and the pericardial cells with anti-Evenskipped antibodies (subpanels a to f). Sections of representative embryos are shown for a wt embryo (subpanel a), for a dof −/− embryo (subpanel b), and for rescued embryos expressing the following transgenes in a dof −/− background under the control of the twi Gal4 driver: UAS dof (subpanel c), UAS dof600 (subpanel d), UAS dof484 (subpanel e), and UAS dof485-1012 (subpanel f). Arrows point to the presence of Eve-positive cells (subpanels a, c, and d).
    Figure Legend Snippet: (A) Rescue of tracheal cell migration by altered versions of the Dof protein. The lumen of the tracheal system of embryos was visualized with the 2A12 antibody (red) (subpanels a to h and a′ to h′), and terminal cells were visualized with the anti-DSRF antibody (green) (subpanels a′ to h′). Confocal projections of a representative embryo are shown for a wt embryo (subpanels a and a′), for a dof −/− embryo (subpanels b and b′), and for rescued embryos expressing the following transgenes in a dof −/− background under the control of the btl Gal4 driver: UAS dof (subpanels c and c′), UAS dof850 (subpanels d and d′), UAS dof600 (subpanels e and e′), UAS dof484 (subpanels f and f′), UAS dof485-1012 (subpanels g and g′), and UAS dof ΔARΔCC (subpanels h and h′). Abbreviations: DB, dorsal branch; TC, transverse connective; VB, visceral branch; LT, lateral trunk; GB, ganglionic branch. The arrow in subpanel c points to the misrouted VB. (B) Rescue of mesodermal cell migration by altered versions of the Dof protein. The lumen of the tracheal system of embryos was visualized with the 2A12 antibody and the pericardial cells with anti-Evenskipped antibodies (subpanels a to f). Sections of representative embryos are shown for a wt embryo (subpanel a), for a dof −/− embryo (subpanel b), and for rescued embryos expressing the following transgenes in a dof −/− background under the control of the twi Gal4 driver: UAS dof (subpanel c), UAS dof600 (subpanel d), UAS dof484 (subpanel e), and UAS dof485-1012 (subpanel f). Arrows point to the presence of Eve-positive cells (subpanels a, c, and d).

    Techniques Used: Migration, Expressing

    (A) Rescue of tracheal and mesodermal cell migration by altered versions of the Dof600 protein. The lumen of the tracheal system of embryos was visualized with the 2A12 antibody in red (subpanels a to c and a′ to c′) or in brown (subpanels a
    Figure Legend Snippet: (A) Rescue of tracheal and mesodermal cell migration by altered versions of the Dof600 protein. The lumen of the tracheal system of embryos was visualized with the 2A12 antibody in red (subpanels a to c and a′ to c′) or in brown (subpanels a" to c"), terminal cells were visualizedwith the anti-DSRF antibody in green (subpanels a′ to c′) and the pericardial cells with anti-Evenskipped antibodies in brown (subpanels a" to c"). Confocal projections are shown for a representative rescued embryo expressing the following transgenes in a dof −/− background under the control of the btl Gal4 driver: UAS dof600 (subpanels a and a′), UAS dof600Y515F (b and b′) and UAS dof600Y486F (subpanels c and c′). Sections are shown for representative rescued embryos expressing the following transgenes in a dof −/− background under the control of the twi Gal4 driver: UAS dof600 (subpanel a"), UAS dof600Y515F (subpanel b"), and UAS dof600Y486F (subpanel c"). (B) Tyrosine 515 serves as a Csw binding site. S2 cells cotransfected with csw and the different forms of V5-tagged dof600 as indicated on the figure, with or without myc-btl act , were lysed after 8 h of induction with 0.6 mM CuSO 4 . Whole-cell lysates were immunoprecipitated with anti-Csw antibodies, subjected to SDS-PAGE and immunoblotted with anti-V5 antibodies (upper panel) and anti-Csw antibodies (bottom panel).

    Techniques Used: Migration, Expressing, Binding Assay, Activated Clotting Time Assay, Immunoprecipitation, SDS Page

    38) Product Images from "A Sandwich ELISA for the Detection of Wnt5a"

    Article Title: A Sandwich ELISA for the Detection of Wnt5a

    Journal: Journal of immunological methods

    doi: 10.1016/j.jim.2009.11.005

    Titration curve of the sandwich ELISA. The sandwich ELISA, using biotinylated goat anti-mouse Wnt5a and HRP-streptavidin detection system, was used to detect different concentrations of rm-Wnt5a (0 to 10 μg/ml). The absorbance was measured after
    Figure Legend Snippet: Titration curve of the sandwich ELISA. The sandwich ELISA, using biotinylated goat anti-mouse Wnt5a and HRP-streptavidin detection system, was used to detect different concentrations of rm-Wnt5a (0 to 10 μg/ml). The absorbance was measured after

    Techniques Used: Titration, Sandwich ELISA

    39) Product Images from "Enhanced NMDA receptor NR1 phosphorylation and neuronal activity in the arcuate nucleus of hypothalamus following peripheral inflammation"

    Article Title: Enhanced NMDA receptor NR1 phosphorylation and neuronal activity in the arcuate nucleus of hypothalamus following peripheral inflammation

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2010.190

    Enhanced pNR1 but not NR1 expression in the ARC from CFA-inflamed rats. (A) Immunoblots of phosphorylated NR1 (pNR1) and NR1 in the ARC of control and CFA-inflamed rats. β-actin was as control. (B) The relative density of pNR1 protein was significantly
    Figure Legend Snippet: Enhanced pNR1 but not NR1 expression in the ARC from CFA-inflamed rats. (A) Immunoblots of phosphorylated NR1 (pNR1) and NR1 in the ARC of control and CFA-inflamed rats. β-actin was as control. (B) The relative density of pNR1 protein was significantly

    Techniques Used: Expressing, Western Blot

    40) Product Images from "Arachidonic Acid Pathway Members PLA2G7, HPGD, EPHX2, and CYP4F8 Identified as Putative Novel Therapeutic Targets in Prostate Cancer"

    Article Title: Arachidonic Acid Pathway Members PLA2G7, HPGD, EPHX2, and CYP4F8 Identified as Putative Novel Therapeutic Targets in Prostate Cancer

    Journal: The American Journal of Pathology

    doi: 10.1016/j.ajpath.2010.10.002

    Heatmap visualization of the gene-wise scaled relative mRNA expression values for CYP4F8, EPHX2, HPGD, PLA2G7, ERG, and AR in 33 primary prostate cancer tissues. The heatmap is drawn based on unsupervised hierarchical clustering of the expression values.
    Figure Legend Snippet: Heatmap visualization of the gene-wise scaled relative mRNA expression values for CYP4F8, EPHX2, HPGD, PLA2G7, ERG, and AR in 33 primary prostate cancer tissues. The heatmap is drawn based on unsupervised hierarchical clustering of the expression values.

    Techniques Used: Expressing

    Related Articles

    Irradiation:

    Article Title: Mutant IDH1 downregulates ATM and alters DNA repair and sensitivity to DNA damage independent of TET2
    Article Snippet: .. Irradiated LT-HSC were plated onto poly-D-lysine-coated coverslips (BD Bioscience, Cat.No: CACB354087) for 30 min, fixed with 2% paraformaldehyde, 0.2% Triton X-100/PBS for 30 min, permeabilized with 0.5% NP-40/PBS for 20 min, and incubated overnight at 4°C with mouse anti-γH2AX Ab (Millipore, clone JBW301, Cat. No: 05–636, 1:100) or rabbit anti-53BP1 Ab (Bethyl Laboratories; 1:3,000). .. After 1 hr at room temperature, cells were washed with PBS and incubated for 35 min in goat Cy2-anti-mouse Ab (Jackson Immuno Research, Cat. No: 115–225–146, 1:750) and goat Cy3-anti-rabbit Ab (Jackson Immuno Research, Cat. No: 111–165–144, 1:750).

    Centrifugation:

    Article Title: Replication stress induces specific enrichment of RECQ1 at common fragile sites FRA3B and FRA16D
    Article Snippet: .. After centrifugation at 20,000X g for 15 min to remove any debris, the supernatant was pre-cleared with protein-G-sepharose/salmon sperm DNA beads (Millipore) at 4°C for 1 h. For each immunoprecipitation, 600 μl (equivalent of 3 × 106 cells) of the pre-cleared chromatin was incubated overnight at 4°C with 3 μg of antibodies specific for either RECQ1 (Bethyl Lab, A300-450A), γH2AX (Millipore, 05-636, clone JBW301), or ORC2 (Enzo Life Science, ADI-KAM-cc235); antibodies were confirmed for their immunoprecipitation specificity using Western blot. ..

    Immunoprecipitation:

    Article Title: Replication stress induces specific enrichment of RECQ1 at common fragile sites FRA3B and FRA16D
    Article Snippet: .. After centrifugation at 20,000X g for 15 min to remove any debris, the supernatant was pre-cleared with protein-G-sepharose/salmon sperm DNA beads (Millipore) at 4°C for 1 h. For each immunoprecipitation, 600 μl (equivalent of 3 × 106 cells) of the pre-cleared chromatin was incubated overnight at 4°C with 3 μg of antibodies specific for either RECQ1 (Bethyl Lab, A300-450A), γH2AX (Millipore, 05-636, clone JBW301), or ORC2 (Enzo Life Science, ADI-KAM-cc235); antibodies were confirmed for their immunoprecipitation specificity using Western blot. ..

    Incubation:

    Article Title: Replication stress induces specific enrichment of RECQ1 at common fragile sites FRA3B and FRA16D
    Article Snippet: .. After centrifugation at 20,000X g for 15 min to remove any debris, the supernatant was pre-cleared with protein-G-sepharose/salmon sperm DNA beads (Millipore) at 4°C for 1 h. For each immunoprecipitation, 600 μl (equivalent of 3 × 106 cells) of the pre-cleared chromatin was incubated overnight at 4°C with 3 μg of antibodies specific for either RECQ1 (Bethyl Lab, A300-450A), γH2AX (Millipore, 05-636, clone JBW301), or ORC2 (Enzo Life Science, ADI-KAM-cc235); antibodies were confirmed for their immunoprecipitation specificity using Western blot. ..

    Article Title: Mutant IDH1 downregulates ATM and alters DNA repair and sensitivity to DNA damage independent of TET2
    Article Snippet: .. Irradiated LT-HSC were plated onto poly-D-lysine-coated coverslips (BD Bioscience, Cat.No: CACB354087) for 30 min, fixed with 2% paraformaldehyde, 0.2% Triton X-100/PBS for 30 min, permeabilized with 0.5% NP-40/PBS for 20 min, and incubated overnight at 4°C with mouse anti-γH2AX Ab (Millipore, clone JBW301, Cat. No: 05–636, 1:100) or rabbit anti-53BP1 Ab (Bethyl Laboratories; 1:3,000). .. After 1 hr at room temperature, cells were washed with PBS and incubated for 35 min in goat Cy2-anti-mouse Ab (Jackson Immuno Research, Cat. No: 115–225–146, 1:750) and goat Cy3-anti-rabbit Ab (Jackson Immuno Research, Cat. No: 111–165–144, 1:750).

    Article Title: Loss of tumor suppressor STAG2 promotes telomere recombination and extends the replicative lifespan of normal human cells
    Article Snippet: .. Cells were fixed in 2% paraformaldehyde in PBS for 10 min at RT, permeabilized in 0.5% NP-40/PBS for 10 min at RT, blocked in 1% BSA/PBS, and incubated with mouse anti-γH2AX #05-636 (0.2 µg/ml) (Millipore) and rabbit anti-53BP1 NB 100–304 (0.1 µg/ml) (Bovus Biologicals) or mouse anti-PML sc966 (2.0 µg/ml) (Santa Cruz) and rabbit anti-TRF1 415 serum (1:1000). .. For staining RAD51 foci, cells were permeabilized in Triton X-100 buffer (0.5% Triton X-100, 20 mM Hepes-KOH at pH 7.9, 50 mM NaCl, 3 mM MgCl2, 300 mM sucrose) for 5 min at RT, fixed in 3% paraformaldehyde (in PBS, 2% sucrose) for 10 min at RT, permeabilized in Triton X-100 buffer for 10 min RT, blocked in 1% BSA/PBS, and incubated with rabbit anti-RAD51 (4 µg/ml) (Santa Cruz Biotechnology, 8349) for 2hr.

    Article Title: Inhibition of Estrogen Signaling Reduces the Incidence of BRCA1-associated Mammary Tumor Formation
    Article Snippet: .. Cells grown on chamber slides (BD Biosciences) were fixed in 3% paraformaldehyde and incubated with an antibody against γ-H2AX (Millipore, #05-636). .. Immunoreactivity was detected with an Alexa Fluor 647-conjugated secondary antibody (Molecular Probes), and cells were counterstained with DAPI (4,6-diamidino-2-phenylindole) to label nuclei.

    Western Blot:

    Article Title: Replication stress induces specific enrichment of RECQ1 at common fragile sites FRA3B and FRA16D
    Article Snippet: .. After centrifugation at 20,000X g for 15 min to remove any debris, the supernatant was pre-cleared with protein-G-sepharose/salmon sperm DNA beads (Millipore) at 4°C for 1 h. For each immunoprecipitation, 600 μl (equivalent of 3 × 106 cells) of the pre-cleared chromatin was incubated overnight at 4°C with 3 μg of antibodies specific for either RECQ1 (Bethyl Lab, A300-450A), γH2AX (Millipore, 05-636, clone JBW301), or ORC2 (Enzo Life Science, ADI-KAM-cc235); antibodies were confirmed for their immunoprecipitation specificity using Western blot. ..

    Staining:

    Article Title: Covalent Inhibition of Ubc13 Affects Ubiquitin Signaling and Reveals Active Site Elements Important for Targeting
    Article Snippet: .. Cells were fixed using 4 % paraformaldehyde and stained with either an anti-p65 antibody (Santa Cruz, sc-372), or anti-53BP1 (Santa Cruz, sc-22760) and anti-γH2AX (Millipore, 05–636) antibodies. .. Invitrogen (37–1100) anti-Ubc13 antibody was used for Western blotting.

    Chloramphenicol Acetyltransferase Assay:

    Article Title: Mutant IDH1 downregulates ATM and alters DNA repair and sensitivity to DNA damage independent of TET2
    Article Snippet: .. Irradiated LT-HSC were plated onto poly-D-lysine-coated coverslips (BD Bioscience, Cat.No: CACB354087) for 30 min, fixed with 2% paraformaldehyde, 0.2% Triton X-100/PBS for 30 min, permeabilized with 0.5% NP-40/PBS for 20 min, and incubated overnight at 4°C with mouse anti-γH2AX Ab (Millipore, clone JBW301, Cat. No: 05–636, 1:100) or rabbit anti-53BP1 Ab (Bethyl Laboratories; 1:3,000). .. After 1 hr at room temperature, cells were washed with PBS and incubated for 35 min in goat Cy2-anti-mouse Ab (Jackson Immuno Research, Cat. No: 115–225–146, 1:750) and goat Cy3-anti-rabbit Ab (Jackson Immuno Research, Cat. No: 111–165–144, 1:750).

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