Structured Review

JEOL 100 cx electron microscope
The expression and phenotypes of mbo are cell-specific. ( A,B ) Confocal images of a stage-16 embryo carrying one copy of the mbo–lacZ reporter stained with anti-β-galactosidase (red) and mAb 2A12 to visualize the tracheal lumen (green). ( A ) lacZ expression is detected in fusion cells (asterisks) of the dorsal branches (DB) forming the dorsal anastomosis (DA). mbo–lacZ is not expressed in the stalk cells of the DB or the cells extending terminal branches (TB). ( B ) mbo–lacZ is expressed in the fusion cells (asterisks) of the dorsal trunk (DT) but not in the stalk cells of the DB or in the transverse connective (TC). The DB is out of focus; its position is drawn with a broken line. Bars, 5 μm ( A ); 2 μm ( B ). ( C,D ) In situ hybridization to mbo mRNA in third instar larval CNS. In wild type ( C ) mbo is expressed in proliferating cells of the nerve cord (brackets), in the optic lobes (OL) of the brain, and the imaginal discs shown attached to the lobes. mbo RNA is not detectable in the CNS of mbo mutants ( D ), and the size of the CNS is reduced. Bars in C and D ; <t>100</t> mm. ( E,K ) Dorsal anastomoses in late stage-16 wild-type (asterisk in E ) and mbo mutant ( K ) embryos. In mbo mutant embryos, 20% of the dorsal branches fail to connect (arrowhead in K ) Bar, 10 μm. ( F,L ) Dorsal anastomoses in third instar wild-type (asterisk in F ) and mbo mutant ( L ) larvae. In mutants the DBs are disconnected (arrowhead), but terminal branching is not affected (arrows in F,L ). Bar, 50 μm. ( G,M ) Dorsal anastomoses in stage-16 embryos carrying one copy of the esg–lacZ marker. esg–lacZ is expressed in the fusion cells of both wild type ( G ) and mbo mutants ( M ). Bars in G and M , 2 μm. ( H,N ) Segments of the dorsal trunks of wild-type and mbo third instar larvae. In mutants the cuticular lining of the dorsal trunks is disrupted at the positions of the fusion junctions (arrowheads in N ) compared to junctions in the wild type (asterisks in H ). Bar, 50 μm ( I–P ) Dnup88 expression in larval fat body detected with the antiserum against the amino-terminal part of the protein. Nuclear staining is detected in wild-type larvae ( I ) but absent in mbo mutants ( O ). The nuclei are visualized by DAPI staining in the adjacent panels J and P . Bar in I,J,O , and P , 40 μm.
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1) Product Images from "members only encodes a Drosophila nucleoporin required for Rel protein import and immune response activation"

Article Title: members only encodes a Drosophila nucleoporin required for Rel protein import and immune response activation

Journal: Genes & Development

doi:

The expression and phenotypes of mbo are cell-specific. ( A,B ) Confocal images of a stage-16 embryo carrying one copy of the mbo–lacZ reporter stained with anti-β-galactosidase (red) and mAb 2A12 to visualize the tracheal lumen (green). ( A ) lacZ expression is detected in fusion cells (asterisks) of the dorsal branches (DB) forming the dorsal anastomosis (DA). mbo–lacZ is not expressed in the stalk cells of the DB or the cells extending terminal branches (TB). ( B ) mbo–lacZ is expressed in the fusion cells (asterisks) of the dorsal trunk (DT) but not in the stalk cells of the DB or in the transverse connective (TC). The DB is out of focus; its position is drawn with a broken line. Bars, 5 μm ( A ); 2 μm ( B ). ( C,D ) In situ hybridization to mbo mRNA in third instar larval CNS. In wild type ( C ) mbo is expressed in proliferating cells of the nerve cord (brackets), in the optic lobes (OL) of the brain, and the imaginal discs shown attached to the lobes. mbo RNA is not detectable in the CNS of mbo mutants ( D ), and the size of the CNS is reduced. Bars in C and D ; 100 mm. ( E,K ) Dorsal anastomoses in late stage-16 wild-type (asterisk in E ) and mbo mutant ( K ) embryos. In mbo mutant embryos, 20% of the dorsal branches fail to connect (arrowhead in K ) Bar, 10 μm. ( F,L ) Dorsal anastomoses in third instar wild-type (asterisk in F ) and mbo mutant ( L ) larvae. In mutants the DBs are disconnected (arrowhead), but terminal branching is not affected (arrows in F,L ). Bar, 50 μm. ( G,M ) Dorsal anastomoses in stage-16 embryos carrying one copy of the esg–lacZ marker. esg–lacZ is expressed in the fusion cells of both wild type ( G ) and mbo mutants ( M ). Bars in G and M , 2 μm. ( H,N ) Segments of the dorsal trunks of wild-type and mbo third instar larvae. In mutants the cuticular lining of the dorsal trunks is disrupted at the positions of the fusion junctions (arrowheads in N ) compared to junctions in the wild type (asterisks in H ). Bar, 50 μm ( I–P ) Dnup88 expression in larval fat body detected with the antiserum against the amino-terminal part of the protein. Nuclear staining is detected in wild-type larvae ( I ) but absent in mbo mutants ( O ). The nuclei are visualized by DAPI staining in the adjacent panels J and P . Bar in I,J,O , and P , 40 μm.
Figure Legend Snippet: The expression and phenotypes of mbo are cell-specific. ( A,B ) Confocal images of a stage-16 embryo carrying one copy of the mbo–lacZ reporter stained with anti-β-galactosidase (red) and mAb 2A12 to visualize the tracheal lumen (green). ( A ) lacZ expression is detected in fusion cells (asterisks) of the dorsal branches (DB) forming the dorsal anastomosis (DA). mbo–lacZ is not expressed in the stalk cells of the DB or the cells extending terminal branches (TB). ( B ) mbo–lacZ is expressed in the fusion cells (asterisks) of the dorsal trunk (DT) but not in the stalk cells of the DB or in the transverse connective (TC). The DB is out of focus; its position is drawn with a broken line. Bars, 5 μm ( A ); 2 μm ( B ). ( C,D ) In situ hybridization to mbo mRNA in third instar larval CNS. In wild type ( C ) mbo is expressed in proliferating cells of the nerve cord (brackets), in the optic lobes (OL) of the brain, and the imaginal discs shown attached to the lobes. mbo RNA is not detectable in the CNS of mbo mutants ( D ), and the size of the CNS is reduced. Bars in C and D ; 100 mm. ( E,K ) Dorsal anastomoses in late stage-16 wild-type (asterisk in E ) and mbo mutant ( K ) embryos. In mbo mutant embryos, 20% of the dorsal branches fail to connect (arrowhead in K ) Bar, 10 μm. ( F,L ) Dorsal anastomoses in third instar wild-type (asterisk in F ) and mbo mutant ( L ) larvae. In mutants the DBs are disconnected (arrowhead), but terminal branching is not affected (arrows in F,L ). Bar, 50 μm. ( G,M ) Dorsal anastomoses in stage-16 embryos carrying one copy of the esg–lacZ marker. esg–lacZ is expressed in the fusion cells of both wild type ( G ) and mbo mutants ( M ). Bars in G and M , 2 μm. ( H,N ) Segments of the dorsal trunks of wild-type and mbo third instar larvae. In mutants the cuticular lining of the dorsal trunks is disrupted at the positions of the fusion junctions (arrowheads in N ) compared to junctions in the wild type (asterisks in H ). Bar, 50 μm ( I–P ) Dnup88 expression in larval fat body detected with the antiserum against the amino-terminal part of the protein. Nuclear staining is detected in wild-type larvae ( I ) but absent in mbo mutants ( O ). The nuclei are visualized by DAPI staining in the adjacent panels J and P . Bar in I,J,O , and P , 40 μm.

Techniques Used: Expressing, Staining, In Situ Hybridization, Mutagenesis, Marker

mbo is not required for mRNA export. ( A–C ) In situ hybridization to lacZ RNA in wild-type and mbo larvae carrying the hs–GAL4 and UAS–lacZNLS transgenes. The lacZ RNA is detected in the proventriculus of wild-type ( B ) and mbo mutant ( C ) larvae after heat shock and does not accumulate in the nucleus (arrowheads). The dark spot inside each nucleus is likely to correlate with the site of transcription. lacZ expression is reduced in some of the cells of mbo mutants (arrows). Bar, 10 μm. ( D–F ) Heat shock-induced expression of Hdc protein in wild-type and mbo mutants. Fat bodies from untreated wild-type ( D ) and heat-shocked wild-type ( E ) and mbo ( F ) larvae carrying the hs–hdc transgene were stained with an antibody against the Hdc protein. Bar, 50 μm. ( G ) Electron micrograph of a section through the lymph gland of an mbo larva. In this tangential section, several NPCs (arrow) can be identified in the space between the cytoplasm (Cyt) and the nucleus (Nuc). Their distribution and morphology are indistinguishable from wild type at this level. Bar, 100 nm.
Figure Legend Snippet: mbo is not required for mRNA export. ( A–C ) In situ hybridization to lacZ RNA in wild-type and mbo larvae carrying the hs–GAL4 and UAS–lacZNLS transgenes. The lacZ RNA is detected in the proventriculus of wild-type ( B ) and mbo mutant ( C ) larvae after heat shock and does not accumulate in the nucleus (arrowheads). The dark spot inside each nucleus is likely to correlate with the site of transcription. lacZ expression is reduced in some of the cells of mbo mutants (arrows). Bar, 10 μm. ( D–F ) Heat shock-induced expression of Hdc protein in wild-type and mbo mutants. Fat bodies from untreated wild-type ( D ) and heat-shocked wild-type ( E ) and mbo ( F ) larvae carrying the hs–hdc transgene were stained with an antibody against the Hdc protein. Bar, 50 μm. ( G ) Electron micrograph of a section through the lymph gland of an mbo larva. In this tangential section, several NPCs (arrow) can be identified in the space between the cytoplasm (Cyt) and the nucleus (Nuc). Their distribution and morphology are indistinguishable from wild type at this level. Bar, 100 nm.

Techniques Used: In Situ Hybridization, Mutagenesis, Expressing, Staining

2) Product Images from "Peripherin Is a Subunit of Peripheral Nerve Neurofilaments: Implications for Differential Vulnerability of CNS and PNS Axons"

Article Title: Peripherin Is a Subunit of Peripheral Nerve Neurofilaments: Implications for Differential Vulnerability of CNS and PNS Axons

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.1081-12.2012

Ultrastructural colocalization of peripherin and NFL on the same neurofilament in sciatic nerve by pre-embedding immuno-EM Paraformaldehyde-fixed samples were incubated with rabbit anti-peripherin and mouse anti-NFL antibodies and probed with goat anti-rabbit IgG and goat anti-mouse IgG conjugated to 0.6nm gold beads. Single (for anti-mouse IgG)- or double (for anti-rabbit IgG)-silver enhancement of gold particles resulted in irregular-shaped electron-dense particles that could be distinguished by their size. As expected, for the immunodetection of peripherin and NFL in normal mice ( A ), linear arrays of two sizes of gold particles (large for peripherin and samll for NFL) decorate most 10-nm filaments in the axon and negligible numbers are detected in peripherin knockout mice ( E ). Higher magnification shows that gold particles of two sizes overlie a single filament in the background ( B, C, D ). Arrows point to small particles (NFL) and arrowheads to large ones (peripherin). Scale bars, 100 nm in A ; 60 nm in B ; 40 nm in C ; 50 nm in D ; 200 nm in E .
Figure Legend Snippet: Ultrastructural colocalization of peripherin and NFL on the same neurofilament in sciatic nerve by pre-embedding immuno-EM Paraformaldehyde-fixed samples were incubated with rabbit anti-peripherin and mouse anti-NFL antibodies and probed with goat anti-rabbit IgG and goat anti-mouse IgG conjugated to 0.6nm gold beads. Single (for anti-mouse IgG)- or double (for anti-rabbit IgG)-silver enhancement of gold particles resulted in irregular-shaped electron-dense particles that could be distinguished by their size. As expected, for the immunodetection of peripherin and NFL in normal mice ( A ), linear arrays of two sizes of gold particles (large for peripherin and samll for NFL) decorate most 10-nm filaments in the axon and negligible numbers are detected in peripherin knockout mice ( E ). Higher magnification shows that gold particles of two sizes overlie a single filament in the background ( B, C, D ). Arrows point to small particles (NFL) and arrowheads to large ones (peripherin). Scale bars, 100 nm in A ; 60 nm in B ; 40 nm in C ; 50 nm in D ; 200 nm in E .

Techniques Used: Incubation, Immunodetection, Mouse Assay, Knock-Out

3) Product Images from "Effects of temperature on the wall strength and compliance of frog mesenteric microvessels"

Article Title: Effects of temperature on the wall strength and compliance of frog mesenteric microvessels

Journal: The Journal of Physiology

doi: 10.1111/j.1469-7793.2000.00613.x

Ultrastructure of microvessels after perfusion with detergent solution and the measurement of compliance A , electron micrograph of part of a transverse section of a frog mesenteric capillary after perfusion with 1 % Triton X-100 for 7 min followed by perfusion with FC80 and the silicone oil mixture. No intact cells can be seen. Collagen fibres (c) of the mesenteric interstitium are clearly visible and the basement membrane (bm) can be seen at the interface between the interstitium (i) and the vessel lumen (l). B , electron micrograph to show the normal appearance of part of a transverse section of a frog mesenteric capillary. Here the microvascular endothelium (e) clearly defines the boundary between the interstitium and the vessel lumen. Scale bars, 500 nm.
Figure Legend Snippet: Ultrastructure of microvessels after perfusion with detergent solution and the measurement of compliance A , electron micrograph of part of a transverse section of a frog mesenteric capillary after perfusion with 1 % Triton X-100 for 7 min followed by perfusion with FC80 and the silicone oil mixture. No intact cells can be seen. Collagen fibres (c) of the mesenteric interstitium are clearly visible and the basement membrane (bm) can be seen at the interface between the interstitium (i) and the vessel lumen (l). B , electron micrograph to show the normal appearance of part of a transverse section of a frog mesenteric capillary. Here the microvascular endothelium (e) clearly defines the boundary between the interstitium and the vessel lumen. Scale bars, 500 nm.

Techniques Used:

4) Product Images from "Saposin C Coupled Lipid Nanovesicles Enable Cancer-Selective Optical and Magnetic Resonance Imaging"

Article Title: Saposin C Coupled Lipid Nanovesicles Enable Cancer-Selective Optical and Magnetic Resonance Imaging

Journal: Molecular imaging and biology : MIB : the official publication of the Academy of Molecular Imaging

doi: 10.1007/s11307-010-0417-7

In vivo MR imaging of SapC–DOPS–IO in mice with xenografts. a – c Human neuroblastoma (CHLA-20) tumors. a Image strip shows T 2 * weighted FLASH image of tumor before and after injection of contrast agent (TE=5 ms/TR=20 ms/FA=10°), 16 averages; resolution: 100 μm isotropic. b Normalized tumor signal intensity (dimensionless) is plotted at the time points of image acquisition, obtained over a 3D slab. The tumor signal intensity is normalized against an ROI chosen just below the tumor tissue at each time point. c ICP-AES data representing iron concentration in excised tumor of mouse treated with SapC shows nearly 5-fold iron concentration when compared with the iron in an untreated mouse. d Human pancreatic (MiaPaCa-2) tumor. Representative T 2 map of tumor was imaged before and after injections (4 h) of SapC–DOPS–IO. An average change in T 2 of approximately 29 ms was seen, from 91.4±11.6 to 62.8±8.6 ms in a manually drawn ROI of approximately the same slice of tumor ( n =5).
Figure Legend Snippet: In vivo MR imaging of SapC–DOPS–IO in mice with xenografts. a – c Human neuroblastoma (CHLA-20) tumors. a Image strip shows T 2 * weighted FLASH image of tumor before and after injection of contrast agent (TE=5 ms/TR=20 ms/FA=10°), 16 averages; resolution: 100 μm isotropic. b Normalized tumor signal intensity (dimensionless) is plotted at the time points of image acquisition, obtained over a 3D slab. The tumor signal intensity is normalized against an ROI chosen just below the tumor tissue at each time point. c ICP-AES data representing iron concentration in excised tumor of mouse treated with SapC shows nearly 5-fold iron concentration when compared with the iron in an untreated mouse. d Human pancreatic (MiaPaCa-2) tumor. Representative T 2 map of tumor was imaged before and after injections (4 h) of SapC–DOPS–IO. An average change in T 2 of approximately 29 ms was seen, from 91.4±11.6 to 62.8±8.6 ms in a manually drawn ROI of approximately the same slice of tumor ( n =5).

Techniques Used: In Vivo, Imaging, Mouse Assay, Stripping Membranes, Injection, Mass Spectrometry, Concentration Assay

Electron micrograph and size distribution of SapC–DOPS and SapC–DOPS–IO nanovesicles. a Freeze-fracture electron micrograph of SapC–DOPS nanovesicles. The bars represent 100 nm, and the shadow direction is running from bottom to top . b Transmission electron microscope images of vesicles loaded with USPIO contrast particles. c and d N4 plus particle size analysis. Sample containing free USPIO particles and vesicles ( c ). The two peaks indicate the relative numbers of USPIO and vesicles on an arbitrary scale and the location of the peaks represent the mean diameter of USPIO and vesicles. d Sample passed through a Con-A Sepharose column and passed through Liposofast® Extruder. Free USPIO is eliminated and a monodisperse nanovesicle solution is obtained. Mean vesicle diameter is approximately 230 nm.
Figure Legend Snippet: Electron micrograph and size distribution of SapC–DOPS and SapC–DOPS–IO nanovesicles. a Freeze-fracture electron micrograph of SapC–DOPS nanovesicles. The bars represent 100 nm, and the shadow direction is running from bottom to top . b Transmission electron microscope images of vesicles loaded with USPIO contrast particles. c and d N4 plus particle size analysis. Sample containing free USPIO particles and vesicles ( c ). The two peaks indicate the relative numbers of USPIO and vesicles on an arbitrary scale and the location of the peaks represent the mean diameter of USPIO and vesicles. d Sample passed through a Con-A Sepharose column and passed through Liposofast® Extruder. Free USPIO is eliminated and a monodisperse nanovesicle solution is obtained. Mean vesicle diameter is approximately 230 nm.

Techniques Used: Transmission Assay, Microscopy, Particle Size Analysis

Tumor-selective imaging of fluorescent labeled SapC–DOPS nanovesicles in animals. a Biodistribution of intravenously administered CVM-labeled SapC–DOPS to mice bearing pancreatic xenografts indicates tumor-targeting potential. Athymic nude mice bearing pancreatic xenografts ( circled 1 and 2 ) and a nontumor-bearing animal ( 3 ) were treated with coupled CVM-labeled SapC–DOPS nanovesicles. Imaging time points were 0, 2, 5, 24, 52, and 100 h after injection. b Fluorescence and photo mages of neuroblastoma xenografts treated with (from left to right ): coupled CVM-labeled SapC–DOPS ( circled 1 ), SapC and CVM-labeled DOPS ( circled 2 ), and CVM-labeled DOPS alone ( circled 3 ). c Fluorescence and photo images of CVM-labeled SapC–DOPS in murine rhabdomyosarcoma (MR366) allografts. Fluorescence filters: Ex=640 nm, Em=700 nm. SapC=4.2 mg/kg, DOPS=2 mg/kg, CVM=6 μmol. Images were acquired 24 h after injection.
Figure Legend Snippet: Tumor-selective imaging of fluorescent labeled SapC–DOPS nanovesicles in animals. a Biodistribution of intravenously administered CVM-labeled SapC–DOPS to mice bearing pancreatic xenografts indicates tumor-targeting potential. Athymic nude mice bearing pancreatic xenografts ( circled 1 and 2 ) and a nontumor-bearing animal ( 3 ) were treated with coupled CVM-labeled SapC–DOPS nanovesicles. Imaging time points were 0, 2, 5, 24, 52, and 100 h after injection. b Fluorescence and photo mages of neuroblastoma xenografts treated with (from left to right ): coupled CVM-labeled SapC–DOPS ( circled 1 ), SapC and CVM-labeled DOPS ( circled 2 ), and CVM-labeled DOPS alone ( circled 3 ). c Fluorescence and photo images of CVM-labeled SapC–DOPS in murine rhabdomyosarcoma (MR366) allografts. Fluorescence filters: Ex=640 nm, Em=700 nm. SapC=4.2 mg/kg, DOPS=2 mg/kg, CVM=6 μmol. Images were acquired 24 h after injection.

Techniques Used: Imaging, Labeling, Mouse Assay, Injection, Fluorescence

5) Product Images from "Purification and Partial Characterization of an Entomopoxvirus (DlEPV) from a Parasitic Wasp of Tephritid Fruit Flies."

Article Title: Purification and Partial Characterization of an Entomopoxvirus (DlEPV) from a Parasitic Wasp of Tephritid Fruit Flies.

Journal: Journal of Insect Science

doi:

Immunodetection of DlEPV proteins in whole body homogenates (5µl) of male (B) and female (C) D. longicaudata. Molecular mass in kiloDaltons (kD). Unparasitized (A) and 48h-52 h-old parasitized (96 hpp) (E) respectively, pharate pupal hemolymph of A. suspensa . D= Purified DlEPV from one 53–55% sucrose fraction. One major (or two closely migrating) band(s) of H
Figure Legend Snippet: Immunodetection of DlEPV proteins in whole body homogenates (5µl) of male (B) and female (C) D. longicaudata. Molecular mass in kiloDaltons (kD). Unparasitized (A) and 48h-52 h-old parasitized (96 hpp) (E) respectively, pharate pupal hemolymph of A. suspensa . D= Purified DlEPV from one 53–55% sucrose fraction. One major (or two closely migrating) band(s) of H"60 kD is detected in male and female wasps, while four bands, two of H"100 kD and two of H"54 kD, occur in the hemolymph of parasitized A. suspensa and in the single DlEPV sucrose fraction (positive control).

Techniques Used: Immunodetection, Purification, Positive Control

6) Product Images from "Distinct Properties of Neuronal and Astrocytic Endopeptidase 3.4.24.16: A Study on Differentiation, Subcellular Distribution, and Secretion Processes"

Article Title: Distinct Properties of Neuronal and Astrocytic Endopeptidase 3.4.24.16: A Study on Differentiation, Subcellular Distribution, and Secretion Processes

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.16-16-05049.1996

Effect of cryoprotection on endopeptidase 3.4.24.16 immunoreactivity in primary cultured neurons and astrocytes. Four-day-old plated neurons and 15-d-old plated astrocytes were fixed with glutaraldehyde, cryoprotected (+) or not (−) with NaK 2 buffer containing 30% sucrose, and processed for immunochemical detection of endopeptidase 3.4.24.16 as described in Materials and Methods. Photographs were taken with Kodacolor 100 film at 200× magnification.
Figure Legend Snippet: Effect of cryoprotection on endopeptidase 3.4.24.16 immunoreactivity in primary cultured neurons and astrocytes. Four-day-old plated neurons and 15-d-old plated astrocytes were fixed with glutaraldehyde, cryoprotected (+) or not (−) with NaK 2 buffer containing 30% sucrose, and processed for immunochemical detection of endopeptidase 3.4.24.16 as described in Materials and Methods. Photographs were taken with Kodacolor 100 film at 200× magnification.

Techniques Used: Cell Culture

Immunolabeling of endopeptidase 3.4.24.16 in primary cultures of neurons and astrocytes. Neurons and astrocytes were cultured for 4 and 15 d, respectively, in the conditions described in Materials and Methods. After fixation and cryoprotection, cells were incubated overnight at 4°C with the IgG-purified fractions of the immune ( top panels ) or preimmune ( bottom panels ) rabbit antiserum developed against rat brain endopeptidase 3.4.24.16. After exposure to a goat anti-rabbit IgG coupled to peroxidase, endopeptidase 3.4.24.16-bearing cells were revealed with diaminobenzidine ( brown cells ) as described, and immunonegative cells still reacted with cresyl violet ( blue cells ). Photographs were taken with Kodacolor 100 film at 200× magnification.
Figure Legend Snippet: Immunolabeling of endopeptidase 3.4.24.16 in primary cultures of neurons and astrocytes. Neurons and astrocytes were cultured for 4 and 15 d, respectively, in the conditions described in Materials and Methods. After fixation and cryoprotection, cells were incubated overnight at 4°C with the IgG-purified fractions of the immune ( top panels ) or preimmune ( bottom panels ) rabbit antiserum developed against rat brain endopeptidase 3.4.24.16. After exposure to a goat anti-rabbit IgG coupled to peroxidase, endopeptidase 3.4.24.16-bearing cells were revealed with diaminobenzidine ( brown cells ) as described, and immunonegative cells still reacted with cresyl violet ( blue cells ). Photographs were taken with Kodacolor 100 film at 200× magnification.

Techniques Used: Immunolabeling, Cell Culture, Incubation, Purification

7) Product Images from "siRNA-containing liposomes modified with polyarginine effectively silence the targeted gene"

Article Title: siRNA-containing liposomes modified with polyarginine effectively silence the targeted gene

Journal: Journal of Controlled Release

doi: 10.1016/j.jconrel.2006.01.022

Effect of HDM2-siRNA in R8-liposomes on the growth inhibition of SK-MES-1 cells. Cells were treated using R8-lipo-HDM2-siRNA and R8-lipo-mock siRNA, where the siRNA concentrations varied from 50 to 100 and 200 nM, the corresponding lipid concentrations were from 7.5 to 15 and 30 μg/ml. Cell viability in R8-liposomes-free medium was taken as 100%.
Figure Legend Snippet: Effect of HDM2-siRNA in R8-liposomes on the growth inhibition of SK-MES-1 cells. Cells were treated using R8-lipo-HDM2-siRNA and R8-lipo-mock siRNA, where the siRNA concentrations varied from 50 to 100 and 200 nM, the corresponding lipid concentrations were from 7.5 to 15 and 30 μg/ml. Cell viability in R8-liposomes-free medium was taken as 100%.

Techniques Used: Inhibition

8) Product Images from "FTY720 induces apoptosis in B16F10-NEX2 murine melanoma cells, limits metastatic development in vivo, and modulates the immune system"

Article Title: FTY720 induces apoptosis in B16F10-NEX2 murine melanoma cells, limits metastatic development in vivo, and modulates the immune system

Journal: Clinics

doi: 10.6061/clinics/2013(07)21

FTY720 induces apoptosis in murine melanoma B16F10-Nex2. A) Murine melanoma cells were treated with 6 μM FTY720 for 4 h, and chromatin condensation was analyzed by fluorescence microscopy after DNA staining with Hoechst 33342. Arrows indicate cells, shown in the images on the right side, with nuclear condensation apparent in FTY720-treated cells. B) Transmission electron microscopy of B16F10-Nex2 cells after treatment with 12 μM FTY720 for 3 h. (a) Control and (b) FTY720. Squares indicate regions shown in images on the right side. C) Melanoma cells were treated with 6 μM FTY720 for 6 h, and DNA degradation was observed with TUNEL assay by fluorescent microscopy. Images of treated (right) and control (left) cells in phase contrast and after DAPI nuclear staining, TUNEL staining, and merging of both images. D) In the same conditions described in (C), activation of caspase-3 by FTY720 in B16F10-Nex2 cells was determined by colorimetric assay. E) B16F10-Nex2 cells were treated with 12 μM FTY720 for 24 h in the presence or absence of 100 or 150 μM necrostatin-1. * p
Figure Legend Snippet: FTY720 induces apoptosis in murine melanoma B16F10-Nex2. A) Murine melanoma cells were treated with 6 μM FTY720 for 4 h, and chromatin condensation was analyzed by fluorescence microscopy after DNA staining with Hoechst 33342. Arrows indicate cells, shown in the images on the right side, with nuclear condensation apparent in FTY720-treated cells. B) Transmission electron microscopy of B16F10-Nex2 cells after treatment with 12 μM FTY720 for 3 h. (a) Control and (b) FTY720. Squares indicate regions shown in images on the right side. C) Melanoma cells were treated with 6 μM FTY720 for 6 h, and DNA degradation was observed with TUNEL assay by fluorescent microscopy. Images of treated (right) and control (left) cells in phase contrast and after DAPI nuclear staining, TUNEL staining, and merging of both images. D) In the same conditions described in (C), activation of caspase-3 by FTY720 in B16F10-Nex2 cells was determined by colorimetric assay. E) B16F10-Nex2 cells were treated with 12 μM FTY720 for 24 h in the presence or absence of 100 or 150 μM necrostatin-1. * p

Techniques Used: Fluorescence, Microscopy, Staining, Transmission Assay, Electron Microscopy, TUNEL Assay, Activation Assay, Colorimetric Assay

9) Product Images from "The molecular cloning and clarification of a photorespiratory mutant, oscdm1, using enhancer trapping"

Article Title: The molecular cloning and clarification of a photorespiratory mutant, oscdm1, using enhancer trapping

Journal: Frontiers in Genetics

doi: 10.3389/fgene.2015.00226

Transmission electron microscopic images of chloroplasts from 1-month-old wild-type and oscdm1 plants. (A) Wild-type mesophyll cells. (B) The mesophyll cells of oscdm1 plants. (C) Wild-type chloroplasts. (D,E) The chloroplasts of oscdm1 plants. The chloroplasts of the wild-type plants had abundant, well-ordered membrane stacks, whereas the chloroplasts of the oscdm1 mutant had almost no normal stacked membranous structures or grana (D) . The mutant chloroplasts also exhibited vacuolation (E) , p, plastoglobule; g, grana stack; sl, stroma lamellae; v, vacuolation. Bar = 1 μm in (A,B) , and 100 nm in (C–E) .
Figure Legend Snippet: Transmission electron microscopic images of chloroplasts from 1-month-old wild-type and oscdm1 plants. (A) Wild-type mesophyll cells. (B) The mesophyll cells of oscdm1 plants. (C) Wild-type chloroplasts. (D,E) The chloroplasts of oscdm1 plants. The chloroplasts of the wild-type plants had abundant, well-ordered membrane stacks, whereas the chloroplasts of the oscdm1 mutant had almost no normal stacked membranous structures or grana (D) . The mutant chloroplasts also exhibited vacuolation (E) , p, plastoglobule; g, grana stack; sl, stroma lamellae; v, vacuolation. Bar = 1 μm in (A,B) , and 100 nm in (C–E) .

Techniques Used: Transmission Assay, Mutagenesis

10) Product Images from "The nucleoporin Nup98 associates with the intranuclear filamentous protein network of TPR"

Article Title: The nucleoporin Nup98 associates with the intranuclear filamentous protein network of TPR

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.061014698

Colocalization of TPR and the myc-PK-6kDa fusion protein. HeLa cells were transiently transfected with the myc-PK-6kDa construct and prepared for double-immunoelectron microscopy. The 10-nm gold particles represent TPR, and the 5-nm gold particles represent the myc-PK-6kDa fusion protein. Note the colocalization of particles in rows. (Bar = 100 nm.)
Figure Legend Snippet: Colocalization of TPR and the myc-PK-6kDa fusion protein. HeLa cells were transiently transfected with the myc-PK-6kDa construct and prepared for double-immunoelectron microscopy. The 10-nm gold particles represent TPR, and the 5-nm gold particles represent the myc-PK-6kDa fusion protein. Note the colocalization of particles in rows. (Bar = 100 nm.)

Techniques Used: Transfection, Construct, Immuno-Electron Microscopy

11) Product Images from "Immunization with a Pentameric L1 Fusion Protein Protects against Papillomavirus Infection"

Article Title: Immunization with a Pentameric L1 Fusion Protein Protects against Papillomavirus Infection

Journal: Journal of Virology

doi: 10.1128/JVI.75.17.7848-7853.2001

Morphology of purified GST-COPV L1 and COPV L1 preparations. The GST-L1 (A) and thrombin-cleaved L1 (B) proteins were negatively stained and examined by electron microscopy as described in Materials and Methods. Both preparations formed 11- to 12-nm capsomeric structures, with the characteristic donut appearance being less obvious in GST-COPV L1. Bars, 100 nm.
Figure Legend Snippet: Morphology of purified GST-COPV L1 and COPV L1 preparations. The GST-L1 (A) and thrombin-cleaved L1 (B) proteins were negatively stained and examined by electron microscopy as described in Materials and Methods. Both preparations formed 11- to 12-nm capsomeric structures, with the characteristic donut appearance being less obvious in GST-COPV L1. Bars, 100 nm.

Techniques Used: Purification, Staining, Electron Microscopy

12) Product Images from "Atypical Membrane Topology and Heteromeric Function of Drosophila Odorant Receptors In VivoA Novel Design Principle for the Insect Odorant Receptor"

Article Title: Atypical Membrane Topology and Heteromeric Function of Drosophila Odorant Receptors In VivoA Novel Design Principle for the Insect Odorant Receptor

Journal: PLoS Biology

doi: 10.1371/journal.pbio.0040020

Probing OR83b Topology by Antibody Epitope Staining (A) Left panel: whole-mount view of a third instar larval salivary gland expressing GFP:OR83b (green) counterstained with DAPI (blue) to visualize the cell nuclei. Genotype in this and subsequent panels: AB1-Gal4/+;UAS-GFP:Or83b/+ . The white box marks the approximate field of view of this tissue shown in all subsequent panels. Right bar graphic: snake plot of OR83b showing the predicted topological location of the N-terminal GFP epitope and the OR83b α-EC2 antibody epitope. (B) Immunostaining of GFP:OR83b (intrinsic fluorescence in green) in larval salivary gland cells with α-EC2 (red) and α-GFP (purple) when permeabilized (0.25% Triton X-100 detergent, top row) or unpermeabilized (no detergent, middle row). The cell membrane staining of OR83b α-EC2 under unpermeabilized conditions is not detected in control salivary glands ( AB1-Gal4/+ ) (bottom). Images are single confocal sections of cells in a plane through or just above the cell nuclei (visualized with DAPI staining, blue). (C) Salivary glands expressing GFP:OR83b ( AB1-Gal4/+;UAS-GFP:Or83b/+ ) were stained with antibodies against the epitopes, illustrated in red in the snake plots on the left, under permeabilized or unpermeabilized conditions. For clarity, only the red channel is shown. None of the antibodies stain control salivary glands under permeabilized conditions (unpublished data). (D) Horizontal section of an antennal sensillum viewed by conventional EM reveals cross-sections of dendritic membranes (scale bar = 1 μm). C, cuticle; P, pore; D, dendrite; SL, sensillum lymph. (E) ImmunoEM on a horizontal section of an antennal sensillum using OR83b α-EC2 and a secondary antibody conjugated to 5 nm colloidal gold reveals distribution of the EC2 epitope on the extracellular face of the dendritic membranes (scale bar = 200 nm). (F) Quantification of gold particle distribution scored from four sections obtained in two independent experiments.
Figure Legend Snippet: Probing OR83b Topology by Antibody Epitope Staining (A) Left panel: whole-mount view of a third instar larval salivary gland expressing GFP:OR83b (green) counterstained with DAPI (blue) to visualize the cell nuclei. Genotype in this and subsequent panels: AB1-Gal4/+;UAS-GFP:Or83b/+ . The white box marks the approximate field of view of this tissue shown in all subsequent panels. Right bar graphic: snake plot of OR83b showing the predicted topological location of the N-terminal GFP epitope and the OR83b α-EC2 antibody epitope. (B) Immunostaining of GFP:OR83b (intrinsic fluorescence in green) in larval salivary gland cells with α-EC2 (red) and α-GFP (purple) when permeabilized (0.25% Triton X-100 detergent, top row) or unpermeabilized (no detergent, middle row). The cell membrane staining of OR83b α-EC2 under unpermeabilized conditions is not detected in control salivary glands ( AB1-Gal4/+ ) (bottom). Images are single confocal sections of cells in a plane through or just above the cell nuclei (visualized with DAPI staining, blue). (C) Salivary glands expressing GFP:OR83b ( AB1-Gal4/+;UAS-GFP:Or83b/+ ) were stained with antibodies against the epitopes, illustrated in red in the snake plots on the left, under permeabilized or unpermeabilized conditions. For clarity, only the red channel is shown. None of the antibodies stain control salivary glands under permeabilized conditions (unpublished data). (D) Horizontal section of an antennal sensillum viewed by conventional EM reveals cross-sections of dendritic membranes (scale bar = 1 μm). C, cuticle; P, pore; D, dendrite; SL, sensillum lymph. (E) ImmunoEM on a horizontal section of an antennal sensillum using OR83b α-EC2 and a secondary antibody conjugated to 5 nm colloidal gold reveals distribution of the EC2 epitope on the extracellular face of the dendritic membranes (scale bar = 200 nm). (F) Quantification of gold particle distribution scored from four sections obtained in two independent experiments.

Techniques Used: Staining, Expressing, Immunostaining, Fluorescence

13) Product Images from "Genetic Dissection of Cadherin Function during Nephrogenesis"

Article Title: Genetic Dissection of Cadherin Function during Nephrogenesis

Journal: Molecular and Cellular Biology

doi:

Morphogenesis of the ureteric bud is affected in R-cadherin-deficient mice. (A and B) Stainings of sagittal sections of 15.5-dpc wild-type (A, +/+) and R-cadherin-deficient (B, −/−) kidneys with hematoxylin-eosin. (C and D) Higher magnification of images presented in panels A and B, respectively. An apoptotic cell is indicated by an arrowhead. (E and F) TUNEL stainings of sagittal sections of 15.5-dpc wild-type (E, +/+) and R-cadherin-deficient (F, −/−) kidneys. Sections from wild-type and mutant kidneys were from the same region, i.e., the central part of the medulla visualizing the proximal parts of the ureteric tubules. Epithelium, mesenchyme, and border between epithelium and mesenchyme are indicated by E, M, and dotted line, respectively. Bars: 100 μm (A) (bar length also applies to panel B); 20 μm (C) (bar length also applies to panel D); 20 μm (E) (bar length also applies to panel F).
Figure Legend Snippet: Morphogenesis of the ureteric bud is affected in R-cadherin-deficient mice. (A and B) Stainings of sagittal sections of 15.5-dpc wild-type (A, +/+) and R-cadherin-deficient (B, −/−) kidneys with hematoxylin-eosin. (C and D) Higher magnification of images presented in panels A and B, respectively. An apoptotic cell is indicated by an arrowhead. (E and F) TUNEL stainings of sagittal sections of 15.5-dpc wild-type (E, +/+) and R-cadherin-deficient (F, −/−) kidneys. Sections from wild-type and mutant kidneys were from the same region, i.e., the central part of the medulla visualizing the proximal parts of the ureteric tubules. Epithelium, mesenchyme, and border between epithelium and mesenchyme are indicated by E, M, and dotted line, respectively. Bars: 100 μm (A) (bar length also applies to panel B); 20 μm (C) (bar length also applies to panel D); 20 μm (E) (bar length also applies to panel F).

Techniques Used: Mouse Assay, TUNEL Assay, Mutagenesis

14) Product Images from "Novel Biogenic Silver Nanoparticle-Induced Reactive Oxygen Species Inhibit the Biofilm Formation and Virulence Activities of Methicillin-Resistant Staphylococcus aureus (MRSA) Strain"

Article Title: Novel Biogenic Silver Nanoparticle-Induced Reactive Oxygen Species Inhibit the Biofilm Formation and Virulence Activities of Methicillin-Resistant Staphylococcus aureus (MRSA) Strain

Journal: Frontiers in Bioengineering and Biotechnology

doi: 10.3389/fbioe.2020.00433

TEM micrograph of SNPs synthesized by Desertifilum IPPAS B-1220 demonstrating the spherical shape and distribution of D-SNPs with a size range from 4.5 to 26 nm. Scale bar, 100 nm.
Figure Legend Snippet: TEM micrograph of SNPs synthesized by Desertifilum IPPAS B-1220 demonstrating the spherical shape and distribution of D-SNPs with a size range from 4.5 to 26 nm. Scale bar, 100 nm.

Techniques Used: Transmission Electron Microscopy, Synthesized

15) Product Images from "Fliposomes: pH-Sensitive Liposomes Containing a trans-2-morpholinocyclohexanol-Based Lipid That Performs a Conformational Flip and Triggers an Instant Cargo Release in Acidic Medium"

Article Title: Fliposomes: pH-Sensitive Liposomes Containing a trans-2-morpholinocyclohexanol-Based Lipid That Performs a Conformational Flip and Triggers an Instant Cargo Release in Acidic Medium

Journal: Pharmaceutics

doi: 10.3390/pharmaceutics3030379

Freeze-fracture electron microscopy of the 1 /POPC/PEG-ceramide fliposome formulation at pH 7.4 ( A ) and 5 minutes after adjusting the pH to 5.5 with diluted acetic acid ( B , C ). Examples of division, buds, and stripes are shown with white, black, and yellow arrows respectively. The bars represent 100 nm.
Figure Legend Snippet: Freeze-fracture electron microscopy of the 1 /POPC/PEG-ceramide fliposome formulation at pH 7.4 ( A ) and 5 minutes after adjusting the pH to 5.5 with diluted acetic acid ( B , C ). Examples of division, buds, and stripes are shown with white, black, and yellow arrows respectively. The bars represent 100 nm.

Techniques Used: Electron Microscopy

16) Product Images from "Assembling filamentous phage occlude pIV channels"

Article Title: Assembling filamentous phage occlude pIV channels

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.161170398

PG6 hydrolysis with varying pIV S324G levels. ( A ) DKM2 cells with plasmids encoding MalS and pIV S324G were grown in the presence of 0 μM IPTG (circles)/10 μM IPTG (inverted triangles)/50 μM IPTG (squares)/100 μM IPTG (diamonds) or 1 mM IPTG (triangles) for 2 h before withdrawal of IPTG and addition of 2 mM PG6. The cultures were sampled at the times indicated, and the OD 405 was determined as described in Materials and Methods . ( B ) Equivalent densities of cells grown for 2 h with IPTG at the indicated concentration were analyzed by Western blot as described in Materials and Methods . One of three representative experiments is shown.
Figure Legend Snippet: PG6 hydrolysis with varying pIV S324G levels. ( A ) DKM2 cells with plasmids encoding MalS and pIV S324G were grown in the presence of 0 μM IPTG (circles)/10 μM IPTG (inverted triangles)/50 μM IPTG (squares)/100 μM IPTG (diamonds) or 1 mM IPTG (triangles) for 2 h before withdrawal of IPTG and addition of 2 mM PG6. The cultures were sampled at the times indicated, and the OD 405 was determined as described in Materials and Methods . ( B ) Equivalent densities of cells grown for 2 h with IPTG at the indicated concentration were analyzed by Western blot as described in Materials and Methods . One of three representative experiments is shown.

Techniques Used: Concentration Assay, Western Blot

17) Product Images from "AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model"

Article Title: AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model

Journal: FEBS Open Bio

doi: 10.1002/2211-5463.12080

AC ‐1001 H3 inhibits cell migration. B16F10‐Nex2 cells treated with 0.35 m m AC ‐1001 H3 were labeled with 5 μ m lysotracker. Images were taken every 5 min in a confocal microscope in real time. White asterisks indicate untreated cells migrating and duplicating in contrast with treated cells. Bar, 100 μm. The time of incubation in each image is indicated.
Figure Legend Snippet: AC ‐1001 H3 inhibits cell migration. B16F10‐Nex2 cells treated with 0.35 m m AC ‐1001 H3 were labeled with 5 μ m lysotracker. Images were taken every 5 min in a confocal microscope in real time. White asterisks indicate untreated cells migrating and duplicating in contrast with treated cells. Bar, 100 μm. The time of incubation in each image is indicated.

Techniques Used: Migration, Labeling, Microscopy, Incubation

AC ‐1001 H3 induces apoptosis. B16F10‐Nex2 cells were treated with AC ‐1001 H3 (0.35 m m ) and examined for apoptosis hallmarks. (A) Untreated (a) and treated (b) cells were stained with Hoechst 33342. Chromatin condensation was observed in treated cells (arrows indicate cells highlighted in inserts, zoom 700%). Bar, 100 μm. (B) TUNEL assay showing DNA degradation in treated cells (d–f) as compared to untreated cells (a–c); arrows indicate cells highlighted in inserts, zoom (700%). Bar, 100 μm. (C) Caspase‐3, ‐8 and ‐9 activation after peptide treatment, * P
Figure Legend Snippet: AC ‐1001 H3 induces apoptosis. B16F10‐Nex2 cells were treated with AC ‐1001 H3 (0.35 m m ) and examined for apoptosis hallmarks. (A) Untreated (a) and treated (b) cells were stained with Hoechst 33342. Chromatin condensation was observed in treated cells (arrows indicate cells highlighted in inserts, zoom 700%). Bar, 100 μm. (B) TUNEL assay showing DNA degradation in treated cells (d–f) as compared to untreated cells (a–c); arrows indicate cells highlighted in inserts, zoom (700%). Bar, 100 μm. (C) Caspase‐3, ‐8 and ‐9 activation after peptide treatment, * P

Techniques Used: Staining, TUNEL Assay, Activation Assay

18) Product Images from "Anopheles gambiae salivary gland proteins as putative targets for blocking transmission of malaria parasites"

Article Title: Anopheles gambiae salivary gland proteins as putative targets for blocking transmission of malaria parasites

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi:

Immunoelectron and indirect immunofluorescence microscopy of female A. gambiae salivary glands. A and B show the binding of 2A3 and C26 to the distal lateral lobes of the salivary glands respectively (×15,600 magnification). C and D show the diffuse dispersion of the 29-kDa and 100-kDa proteins on the female-specific lobes of the salivary glands as revealed by immunofluorescence assay.
Figure Legend Snippet: Immunoelectron and indirect immunofluorescence microscopy of female A. gambiae salivary glands. A and B show the binding of 2A3 and C26 to the distal lateral lobes of the salivary glands respectively (×15,600 magnification). C and D show the diffuse dispersion of the 29-kDa and 100-kDa proteins on the female-specific lobes of the salivary glands as revealed by immunofluorescence assay.

Techniques Used: Immunofluorescence, Microscopy, Binding Assay

( A ) Silver-stained SDS/PAGE gel of male (M) and female (F) A. gambiae and A. stephensi salivary gland extracts. ( B ) Immunoprecipitation of [ 35 S]methionine-labeled A. gambiae salivary gland extracts with monoclonal antibodies 2A3 and C26. ( C ) Silver-stained SDS/PAGE gel of salivary glands isolated from A. gambiae females at the indicated time points (T = hours) after a blood meal. Arrows in A indicate the position of the 25-kDa, 29-kDa, 42-kDa, and 67-kDa proteins, and those in B and C indicate the position of the 29-kDa and 100-kDa proteins. Numbers on the left indicate molecular mass standards.
Figure Legend Snippet: ( A ) Silver-stained SDS/PAGE gel of male (M) and female (F) A. gambiae and A. stephensi salivary gland extracts. ( B ) Immunoprecipitation of [ 35 S]methionine-labeled A. gambiae salivary gland extracts with monoclonal antibodies 2A3 and C26. ( C ) Silver-stained SDS/PAGE gel of salivary glands isolated from A. gambiae females at the indicated time points (T = hours) after a blood meal. Arrows in A indicate the position of the 25-kDa, 29-kDa, 42-kDa, and 67-kDa proteins, and those in B and C indicate the position of the 29-kDa and 100-kDa proteins. Numbers on the left indicate molecular mass standards.

Techniques Used: Staining, SDS Page, Immunoprecipitation, Labeling, Isolation

19) Product Images from "Cell transfection in vitro and in vivo with nontoxic TAT peptide-liposome-DNA complexes"

Article Title: Cell transfection in vitro and in vivo with nontoxic TAT peptide-liposome-DNA complexes

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.0435906100

( A ) Gel-electrophoresis results of free pEGFP-N1 plasmid (lane 1), TATp-liposome–pEGFP-N1 complex (lane 2), and Triton X-100-treated TATp-liposome–pEGFP complex (lane 3). ( B ) Freeze-etching electron microscopy of TATp-liposomes ( a ) and TATp-liposome–pEGFP-N1 complex ( b ). For details, see Materials and Methods .
Figure Legend Snippet: ( A ) Gel-electrophoresis results of free pEGFP-N1 plasmid (lane 1), TATp-liposome–pEGFP-N1 complex (lane 2), and Triton X-100-treated TATp-liposome–pEGFP complex (lane 3). ( B ) Freeze-etching electron microscopy of TATp-liposomes ( a ) and TATp-liposome–pEGFP-N1 complex ( b ). For details, see Materials and Methods .

Techniques Used: Nucleic Acid Electrophoresis, Plasmid Preparation, Electron Microscopy

Cytotoxicity test. ( A ) Comparative cytotoxicity of low-cationic TATp-liposomes and Lipofectin toward NIH/3T3 cells at different lipid concentrations. Incubation for 24 h: Cell viability in the presence of 21 μg/ml TATp-liposomes was taken as 100%. ( B ) Relative viability of NIH/3T3 cells treated with equal quantities (as DNA, at 5 μg) of TATp-liposome–pEGFP-N1 complex and Lipofectin–pEGFP-N1 lipoplex. Incubation for 4 h: Cell viability in the presence of TATp-liposome–plasmid complex was taken as 100%. For details, see Materials and Methods .
Figure Legend Snippet: Cytotoxicity test. ( A ) Comparative cytotoxicity of low-cationic TATp-liposomes and Lipofectin toward NIH/3T3 cells at different lipid concentrations. Incubation for 24 h: Cell viability in the presence of 21 μg/ml TATp-liposomes was taken as 100%. ( B ) Relative viability of NIH/3T3 cells treated with equal quantities (as DNA, at 5 μg) of TATp-liposome–pEGFP-N1 complex and Lipofectin–pEGFP-N1 lipoplex. Incubation for 4 h: Cell viability in the presence of TATp-liposome–plasmid complex was taken as 100%. For details, see Materials and Methods .

Techniques Used: Incubation, Plasmid Preparation

20) Product Images from "Complexin Mutants Reveal Partial Segregation between Recycling Pathways That Drive Evoked and Spontaneous Neurotransmission"

Article Title: Complexin Mutants Reveal Partial Segregation between Recycling Pathways That Drive Evoked and Spontaneous Neurotransmission

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.1854-16.2016

Selective depletion of docked vesicles in the vicinity of T-bars in cpx −/− boutons. A , Micrograph illustrating morphometric analysis of vesicle numbers at different layers surrounding the T-bar. Scale bar, 150 nm. B , In cpx −/− boutons, vesicle numbers are unaltered in the immediate proximity to T-bars (50–200 nm) but significantly depleted at a distance of 250–400 nm from the T-bar. C , Subsequent serial sections showing an AZ (arrow) with a T-bar at the synaptic membrane surrounded by vesicles. Scale bar, 100 nm. D , Micrograph illustrating the vesicle classification according to their position at the T-bar: docked and attached to the T-bar (“Attached,” red); docked in the vicinity of the T-bar but not attached to it (“Docked at AZ,” green); around the T-bar (“Around T-bar,” within a 150 nm radius outlined by the black circle, blue); intraterminal vesicles not situated in the vicinity or around T-bars (“Internal,” cyan). Scale bar, 100 nm. C , 3D reconstruction of a T-bar surrounded by vesicles shows a selective depletion in the pool of vesicles docked at AZ (green) and around T-bar (blue). For clarity, left panels for control and cpx −/− AZs represent only the T-bar with docked vesicles. F–H , Vesicle numbers quantified from 3D reconstructions. D , The number of attached vesicles (red) is unaffected by Cpx deletion. E , The number of vesicles docked at AZ (green) is reduced in cpx −/− boutons. G , The number of vesicles around T-bar are reduced in cpx −/− boutons. All the vesicles for each AZ are counted from complete 3D reconstructions of AZs. Data collected from 56 WT and 57 cpx −/− AZs (4 larvae for each line). *** p
Figure Legend Snippet: Selective depletion of docked vesicles in the vicinity of T-bars in cpx −/− boutons. A , Micrograph illustrating morphometric analysis of vesicle numbers at different layers surrounding the T-bar. Scale bar, 150 nm. B , In cpx −/− boutons, vesicle numbers are unaltered in the immediate proximity to T-bars (50–200 nm) but significantly depleted at a distance of 250–400 nm from the T-bar. C , Subsequent serial sections showing an AZ (arrow) with a T-bar at the synaptic membrane surrounded by vesicles. Scale bar, 100 nm. D , Micrograph illustrating the vesicle classification according to their position at the T-bar: docked and attached to the T-bar (“Attached,” red); docked in the vicinity of the T-bar but not attached to it (“Docked at AZ,” green); around the T-bar (“Around T-bar,” within a 150 nm radius outlined by the black circle, blue); intraterminal vesicles not situated in the vicinity or around T-bars (“Internal,” cyan). Scale bar, 100 nm. C , 3D reconstruction of a T-bar surrounded by vesicles shows a selective depletion in the pool of vesicles docked at AZ (green) and around T-bar (blue). For clarity, left panels for control and cpx −/− AZs represent only the T-bar with docked vesicles. F–H , Vesicle numbers quantified from 3D reconstructions. D , The number of attached vesicles (red) is unaffected by Cpx deletion. E , The number of vesicles docked at AZ (green) is reduced in cpx −/− boutons. G , The number of vesicles around T-bar are reduced in cpx −/− boutons. All the vesicles for each AZ are counted from complete 3D reconstructions of AZs. Data collected from 56 WT and 57 cpx −/− AZs (4 larvae for each line). *** p

Techniques Used:

21) Product Images from "Chronic stress alters synaptic terminal structure in hippocampus"

Article Title: Chronic stress alters synaptic terminal structure in hippocampus

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi:

Localization of the hippocampal stratum lucidum area used for electron microscopic studies. ( A ) Durcupan-embedded blocks containing 100-μm-thick sections of the dorsal hippocampus were trimmed at the level of the CA3 region (see box). ( B ) Semithin sections (1.5 μm) stained with toluidine blue were used as a guide to further trim the blocks to an area containing the stratum lucidum (SL). (Bar = 17.5 μm.) ( C ). DG, dentate gyrus, SO, stratum oriens, SP, stratum pyramidale, SL, stratum lucidum, SR stratum radiatum.
Figure Legend Snippet: Localization of the hippocampal stratum lucidum area used for electron microscopic studies. ( A ) Durcupan-embedded blocks containing 100-μm-thick sections of the dorsal hippocampus were trimmed at the level of the CA3 region (see box). ( B ) Semithin sections (1.5 μm) stained with toluidine blue were used as a guide to further trim the blocks to an area containing the stratum lucidum (SL). (Bar = 17.5 μm.) ( C ). DG, dentate gyrus, SO, stratum oriens, SP, stratum pyramidale, SL, stratum lucidum, SR stratum radiatum.

Techniques Used: Staining

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Mutagenesis:

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Article Snippet: .. Wild-type and mbo mutant larvae were prepared for EM as described ( ) and examined with a Jeol 100 CX electron microscope. .. One hundred excision strains from l(3)5043 were generated as described ( ) and balanced either over TM3UbxLacZ or Tm6b. hs–mbo transgenic fly strains were generated by P-element-mediated transformation ( ) using the 2514-bp mbo cDNA insert cloned into the Stu I and Eco RI sites of pPCaSpeR-hs.

Staining:

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Microscopy:

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Blocking Assay:

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    JEOL 100 cx electron microscope
    The expression and phenotypes of mbo are cell-specific. ( A,B ) Confocal images of a stage-16 embryo carrying one copy of the mbo–lacZ reporter stained with anti-β-galactosidase (red) and mAb 2A12 to visualize the tracheal lumen (green). ( A ) lacZ expression is detected in fusion cells (asterisks) of the dorsal branches (DB) forming the dorsal anastomosis (DA). mbo–lacZ is not expressed in the stalk cells of the DB or the cells extending terminal branches (TB). ( B ) mbo–lacZ is expressed in the fusion cells (asterisks) of the dorsal trunk (DT) but not in the stalk cells of the DB or in the transverse connective (TC). The DB is out of focus; its position is drawn with a broken line. Bars, 5 μm ( A ); 2 μm ( B ). ( C,D ) In situ hybridization to mbo mRNA in third instar larval CNS. In wild type ( C ) mbo is expressed in proliferating cells of the nerve cord (brackets), in the optic lobes (OL) of the brain, and the imaginal discs shown attached to the lobes. mbo RNA is not detectable in the CNS of mbo mutants ( D ), and the size of the CNS is reduced. Bars in C and D ; <t>100</t> mm. ( E,K ) Dorsal anastomoses in late stage-16 wild-type (asterisk in E ) and mbo mutant ( K ) embryos. In mbo mutant embryos, 20% of the dorsal branches fail to connect (arrowhead in K ) Bar, 10 μm. ( F,L ) Dorsal anastomoses in third instar wild-type (asterisk in F ) and mbo mutant ( L ) larvae. In mutants the DBs are disconnected (arrowhead), but terminal branching is not affected (arrows in F,L ). Bar, 50 μm. ( G,M ) Dorsal anastomoses in stage-16 embryos carrying one copy of the esg–lacZ marker. esg–lacZ is expressed in the fusion cells of both wild type ( G ) and mbo mutants ( M ). Bars in G and M , 2 μm. ( H,N ) Segments of the dorsal trunks of wild-type and mbo third instar larvae. In mutants the cuticular lining of the dorsal trunks is disrupted at the positions of the fusion junctions (arrowheads in N ) compared to junctions in the wild type (asterisks in H ). Bar, 50 μm ( I–P ) Dnup88 expression in larval fat body detected with the antiserum against the amino-terminal part of the protein. Nuclear staining is detected in wild-type larvae ( I ) but absent in mbo mutants ( O ). The nuclei are visualized by DAPI staining in the adjacent panels J and P . Bar in I,J,O , and P , 40 μm.
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    The expression and phenotypes of mbo are cell-specific. ( A,B ) Confocal images of a stage-16 embryo carrying one copy of the mbo–lacZ reporter stained with anti-β-galactosidase (red) and mAb 2A12 to visualize the tracheal lumen (green). ( A ) lacZ expression is detected in fusion cells (asterisks) of the dorsal branches (DB) forming the dorsal anastomosis (DA). mbo–lacZ is not expressed in the stalk cells of the DB or the cells extending terminal branches (TB). ( B ) mbo–lacZ is expressed in the fusion cells (asterisks) of the dorsal trunk (DT) but not in the stalk cells of the DB or in the transverse connective (TC). The DB is out of focus; its position is drawn with a broken line. Bars, 5 μm ( A ); 2 μm ( B ). ( C,D ) In situ hybridization to mbo mRNA in third instar larval CNS. In wild type ( C ) mbo is expressed in proliferating cells of the nerve cord (brackets), in the optic lobes (OL) of the brain, and the imaginal discs shown attached to the lobes. mbo RNA is not detectable in the CNS of mbo mutants ( D ), and the size of the CNS is reduced. Bars in C and D ; 100 mm. ( E,K ) Dorsal anastomoses in late stage-16 wild-type (asterisk in E ) and mbo mutant ( K ) embryos. In mbo mutant embryos, 20% of the dorsal branches fail to connect (arrowhead in K ) Bar, 10 μm. ( F,L ) Dorsal anastomoses in third instar wild-type (asterisk in F ) and mbo mutant ( L ) larvae. In mutants the DBs are disconnected (arrowhead), but terminal branching is not affected (arrows in F,L ). Bar, 50 μm. ( G,M ) Dorsal anastomoses in stage-16 embryos carrying one copy of the esg–lacZ marker. esg–lacZ is expressed in the fusion cells of both wild type ( G ) and mbo mutants ( M ). Bars in G and M , 2 μm. ( H,N ) Segments of the dorsal trunks of wild-type and mbo third instar larvae. In mutants the cuticular lining of the dorsal trunks is disrupted at the positions of the fusion junctions (arrowheads in N ) compared to junctions in the wild type (asterisks in H ). Bar, 50 μm ( I–P ) Dnup88 expression in larval fat body detected with the antiserum against the amino-terminal part of the protein. Nuclear staining is detected in wild-type larvae ( I ) but absent in mbo mutants ( O ). The nuclei are visualized by DAPI staining in the adjacent panels J and P . Bar in I,J,O , and P , 40 μm.

    Journal: Genes & Development

    Article Title: members only encodes a Drosophila nucleoporin required for Rel protein import and immune response activation

    doi:

    Figure Lengend Snippet: The expression and phenotypes of mbo are cell-specific. ( A,B ) Confocal images of a stage-16 embryo carrying one copy of the mbo–lacZ reporter stained with anti-β-galactosidase (red) and mAb 2A12 to visualize the tracheal lumen (green). ( A ) lacZ expression is detected in fusion cells (asterisks) of the dorsal branches (DB) forming the dorsal anastomosis (DA). mbo–lacZ is not expressed in the stalk cells of the DB or the cells extending terminal branches (TB). ( B ) mbo–lacZ is expressed in the fusion cells (asterisks) of the dorsal trunk (DT) but not in the stalk cells of the DB or in the transverse connective (TC). The DB is out of focus; its position is drawn with a broken line. Bars, 5 μm ( A ); 2 μm ( B ). ( C,D ) In situ hybridization to mbo mRNA in third instar larval CNS. In wild type ( C ) mbo is expressed in proliferating cells of the nerve cord (brackets), in the optic lobes (OL) of the brain, and the imaginal discs shown attached to the lobes. mbo RNA is not detectable in the CNS of mbo mutants ( D ), and the size of the CNS is reduced. Bars in C and D ; 100 mm. ( E,K ) Dorsal anastomoses in late stage-16 wild-type (asterisk in E ) and mbo mutant ( K ) embryos. In mbo mutant embryos, 20% of the dorsal branches fail to connect (arrowhead in K ) Bar, 10 μm. ( F,L ) Dorsal anastomoses in third instar wild-type (asterisk in F ) and mbo mutant ( L ) larvae. In mutants the DBs are disconnected (arrowhead), but terminal branching is not affected (arrows in F,L ). Bar, 50 μm. ( G,M ) Dorsal anastomoses in stage-16 embryos carrying one copy of the esg–lacZ marker. esg–lacZ is expressed in the fusion cells of both wild type ( G ) and mbo mutants ( M ). Bars in G and M , 2 μm. ( H,N ) Segments of the dorsal trunks of wild-type and mbo third instar larvae. In mutants the cuticular lining of the dorsal trunks is disrupted at the positions of the fusion junctions (arrowheads in N ) compared to junctions in the wild type (asterisks in H ). Bar, 50 μm ( I–P ) Dnup88 expression in larval fat body detected with the antiserum against the amino-terminal part of the protein. Nuclear staining is detected in wild-type larvae ( I ) but absent in mbo mutants ( O ). The nuclei are visualized by DAPI staining in the adjacent panels J and P . Bar in I,J,O , and P , 40 μm.

    Article Snippet: Wild-type and mbo mutant larvae were prepared for EM as described ( ) and examined with a Jeol 100 CX electron microscope.

    Techniques: Expressing, Staining, In Situ Hybridization, Mutagenesis, Marker

    mbo is not required for mRNA export. ( A–C ) In situ hybridization to lacZ RNA in wild-type and mbo larvae carrying the hs–GAL4 and UAS–lacZNLS transgenes. The lacZ RNA is detected in the proventriculus of wild-type ( B ) and mbo mutant ( C ) larvae after heat shock and does not accumulate in the nucleus (arrowheads). The dark spot inside each nucleus is likely to correlate with the site of transcription. lacZ expression is reduced in some of the cells of mbo mutants (arrows). Bar, 10 μm. ( D–F ) Heat shock-induced expression of Hdc protein in wild-type and mbo mutants. Fat bodies from untreated wild-type ( D ) and heat-shocked wild-type ( E ) and mbo ( F ) larvae carrying the hs–hdc transgene were stained with an antibody against the Hdc protein. Bar, 50 μm. ( G ) Electron micrograph of a section through the lymph gland of an mbo larva. In this tangential section, several NPCs (arrow) can be identified in the space between the cytoplasm (Cyt) and the nucleus (Nuc). Their distribution and morphology are indistinguishable from wild type at this level. Bar, 100 nm.

    Journal: Genes & Development

    Article Title: members only encodes a Drosophila nucleoporin required for Rel protein import and immune response activation

    doi:

    Figure Lengend Snippet: mbo is not required for mRNA export. ( A–C ) In situ hybridization to lacZ RNA in wild-type and mbo larvae carrying the hs–GAL4 and UAS–lacZNLS transgenes. The lacZ RNA is detected in the proventriculus of wild-type ( B ) and mbo mutant ( C ) larvae after heat shock and does not accumulate in the nucleus (arrowheads). The dark spot inside each nucleus is likely to correlate with the site of transcription. lacZ expression is reduced in some of the cells of mbo mutants (arrows). Bar, 10 μm. ( D–F ) Heat shock-induced expression of Hdc protein in wild-type and mbo mutants. Fat bodies from untreated wild-type ( D ) and heat-shocked wild-type ( E ) and mbo ( F ) larvae carrying the hs–hdc transgene were stained with an antibody against the Hdc protein. Bar, 50 μm. ( G ) Electron micrograph of a section through the lymph gland of an mbo larva. In this tangential section, several NPCs (arrow) can be identified in the space between the cytoplasm (Cyt) and the nucleus (Nuc). Their distribution and morphology are indistinguishable from wild type at this level. Bar, 100 nm.

    Article Snippet: Wild-type and mbo mutant larvae were prepared for EM as described ( ) and examined with a Jeol 100 CX electron microscope.

    Techniques: In Situ Hybridization, Mutagenesis, Expressing, Staining

    Ultrastructural colocalization of peripherin and NFL on the same neurofilament in sciatic nerve by pre-embedding immuno-EM Paraformaldehyde-fixed samples were incubated with rabbit anti-peripherin and mouse anti-NFL antibodies and probed with goat anti-rabbit IgG and goat anti-mouse IgG conjugated to 0.6nm gold beads. Single (for anti-mouse IgG)- or double (for anti-rabbit IgG)-silver enhancement of gold particles resulted in irregular-shaped electron-dense particles that could be distinguished by their size. As expected, for the immunodetection of peripherin and NFL in normal mice ( A ), linear arrays of two sizes of gold particles (large for peripherin and samll for NFL) decorate most 10-nm filaments in the axon and negligible numbers are detected in peripherin knockout mice ( E ). Higher magnification shows that gold particles of two sizes overlie a single filament in the background ( B, C, D ). Arrows point to small particles (NFL) and arrowheads to large ones (peripherin). Scale bars, 100 nm in A ; 60 nm in B ; 40 nm in C ; 50 nm in D ; 200 nm in E .

    Journal: The Journal of Neuroscience

    Article Title: Peripherin Is a Subunit of Peripheral Nerve Neurofilaments: Implications for Differential Vulnerability of CNS and PNS Axons

    doi: 10.1523/JNEUROSCI.1081-12.2012

    Figure Lengend Snippet: Ultrastructural colocalization of peripherin and NFL on the same neurofilament in sciatic nerve by pre-embedding immuno-EM Paraformaldehyde-fixed samples were incubated with rabbit anti-peripherin and mouse anti-NFL antibodies and probed with goat anti-rabbit IgG and goat anti-mouse IgG conjugated to 0.6nm gold beads. Single (for anti-mouse IgG)- or double (for anti-rabbit IgG)-silver enhancement of gold particles resulted in irregular-shaped electron-dense particles that could be distinguished by their size. As expected, for the immunodetection of peripherin and NFL in normal mice ( A ), linear arrays of two sizes of gold particles (large for peripherin and samll for NFL) decorate most 10-nm filaments in the axon and negligible numbers are detected in peripherin knockout mice ( E ). Higher magnification shows that gold particles of two sizes overlie a single filament in the background ( B, C, D ). Arrows point to small particles (NFL) and arrowheads to large ones (peripherin). Scale bars, 100 nm in A ; 60 nm in B ; 40 nm in C ; 50 nm in D ; 200 nm in E .

    Article Snippet: The grids were photographed on a JEOL 100 cx electron microscope operated at 80 kV.

    Techniques: Incubation, Immunodetection, Mouse Assay, Knock-Out

    Knockdown of SR-BI/CLA-1 in Caco-2/TC7 cells impairs PPM-induced ERK1/2 phosphorylation and apoB chase. (A) Caco-2/TC7 Cell populations 63 and 64, expressing lentiviral shRNA 63 and 64 respectively, were analyzed at passage 4 after transfection in the absence of PPM or after 10 min of PPM supply. Cell lysates were analyzed by immunoblot with antibodies against SR-BI/CLA-1 and E-cadherin (E-cadh, used as loading control). The lower panel shows the level of SR-BI/CLA-1 expression normalized to the level of E-cadherin expression set at 100% for control Caco-2/TC7 cells. Results are from two independent sets of experiments. (B) Cell populations 63 and 64 were cultured on semi-permeable filters and incubated in the absence or presence of PPM or IPM in the apical compartment for the indicated times. An early (63E) and a late (63L) passage (corresponding respectively to passage 6 and 28 after transfection) of Cell population 63 were compared to Cell population 64 at passage 28. Cell lysates were analyzed in SR-BI/CLA-1 and phospho-ERK1/2 (P-ERK) immunoblots. Total ERK (ERK) and E-cadherin (E-cadh) were used as loading controls. Lower panel, the ratio of P-ERK expression normalized to total ERK expression in PPM-treated cells versus IPM-treated cells, set at 100% for Cell population 64. Results show the means±SEM of three independent sets of experiments. *P

    Journal: PLoS ONE

    Article Title: Sensing of Dietary Lipids by Enterocytes: A New Role for SR-BI/CLA-1

    doi: 10.1371/journal.pone.0004278

    Figure Lengend Snippet: Knockdown of SR-BI/CLA-1 in Caco-2/TC7 cells impairs PPM-induced ERK1/2 phosphorylation and apoB chase. (A) Caco-2/TC7 Cell populations 63 and 64, expressing lentiviral shRNA 63 and 64 respectively, were analyzed at passage 4 after transfection in the absence of PPM or after 10 min of PPM supply. Cell lysates were analyzed by immunoblot with antibodies against SR-BI/CLA-1 and E-cadherin (E-cadh, used as loading control). The lower panel shows the level of SR-BI/CLA-1 expression normalized to the level of E-cadherin expression set at 100% for control Caco-2/TC7 cells. Results are from two independent sets of experiments. (B) Cell populations 63 and 64 were cultured on semi-permeable filters and incubated in the absence or presence of PPM or IPM in the apical compartment for the indicated times. An early (63E) and a late (63L) passage (corresponding respectively to passage 6 and 28 after transfection) of Cell population 63 were compared to Cell population 64 at passage 28. Cell lysates were analyzed in SR-BI/CLA-1 and phospho-ERK1/2 (P-ERK) immunoblots. Total ERK (ERK) and E-cadherin (E-cadh) were used as loading controls. Lower panel, the ratio of P-ERK expression normalized to total ERK expression in PPM-treated cells versus IPM-treated cells, set at 100% for Cell population 64. Results show the means±SEM of three independent sets of experiments. *P

    Article Snippet: Sections were analyzed in a Jeol 100 CX II electron microscope.

    Techniques: Expressing, shRNA, Transfection, Cell Culture, Incubation, Western Blot

    Subcellular localization of SR-BI/CLA-1 after the supply of postprandial micelles. (A) Immunoelectron micrograph of SR-BI/CLA-1 in untreated differentiated Caco-2/TC7 cells. MV, microvilli; TW, terminal web (bar, 0.5 µm). Note the significant amount of intracellular trafficking SR-BI/CLA-1 in addition to its main apical localization (arrowheads). (B) Immunolocalization of SR-BI/CLA-1 (green channel) and sucrase isomaltase (SI, red channel) in differentiated Caco-2/TC7 cells before (T0) and after 5, 10 and 15 min of apical PPM supply. Panels represent XY acquisitions at the apical level (bar, 10 µm). Arrowheads show clusters of SR-BI/CLA-1. (C) Immunolocalization of SR-BI/CLA-1 in differentiated Caco-2/TC7 cells in the absence (control) or presence of PPM or IPM for 20 min (bar, 20 µm). Arrowheads show clusters of SR-BI/CLA-1 (D) Immunoelectron micrograph of SR-BI/CLA-1 in Caco-2/TC7 cells supplied with PPM (MV, microvilli). Arrowheads indicate SR-BI/CLA-1 clusters (bar, 100 nm). (E) Cell surface biotinylation assay for apical SR-BI/CLA-1. Caco-2/TC7 cells were cultured in the absence (0) or presence of PPM for the indicated times. Cells were then selectively labeled with non-permeant biotin at the apical (left panel) or basal surface (right panel). Biotinylated fractions were obtained as described in Material and Methods . Total cell lysates (total), apical and basal biotinylated fractions (left and right panel respectively) and non-apical fractions (non-apical) were analyzed in immunoblots of SR-BI/CLA-1, E-cadherin being used as a basolateral membrane marker.

    Journal: PLoS ONE

    Article Title: Sensing of Dietary Lipids by Enterocytes: A New Role for SR-BI/CLA-1

    doi: 10.1371/journal.pone.0004278

    Figure Lengend Snippet: Subcellular localization of SR-BI/CLA-1 after the supply of postprandial micelles. (A) Immunoelectron micrograph of SR-BI/CLA-1 in untreated differentiated Caco-2/TC7 cells. MV, microvilli; TW, terminal web (bar, 0.5 µm). Note the significant amount of intracellular trafficking SR-BI/CLA-1 in addition to its main apical localization (arrowheads). (B) Immunolocalization of SR-BI/CLA-1 (green channel) and sucrase isomaltase (SI, red channel) in differentiated Caco-2/TC7 cells before (T0) and after 5, 10 and 15 min of apical PPM supply. Panels represent XY acquisitions at the apical level (bar, 10 µm). Arrowheads show clusters of SR-BI/CLA-1. (C) Immunolocalization of SR-BI/CLA-1 in differentiated Caco-2/TC7 cells in the absence (control) or presence of PPM or IPM for 20 min (bar, 20 µm). Arrowheads show clusters of SR-BI/CLA-1 (D) Immunoelectron micrograph of SR-BI/CLA-1 in Caco-2/TC7 cells supplied with PPM (MV, microvilli). Arrowheads indicate SR-BI/CLA-1 clusters (bar, 100 nm). (E) Cell surface biotinylation assay for apical SR-BI/CLA-1. Caco-2/TC7 cells were cultured in the absence (0) or presence of PPM for the indicated times. Cells were then selectively labeled with non-permeant biotin at the apical (left panel) or basal surface (right panel). Biotinylated fractions were obtained as described in Material and Methods . Total cell lysates (total), apical and basal biotinylated fractions (left and right panel respectively) and non-apical fractions (non-apical) were analyzed in immunoblots of SR-BI/CLA-1, E-cadherin being used as a basolateral membrane marker.

    Article Snippet: Sections were analyzed in a Jeol 100 CX II electron microscope.

    Techniques: Cell Surface Biotinylation Assay, Cell Culture, Labeling, Western Blot, Marker

    PPM supply induces movement of SR-BI/CLA-1 towards raft microdomains. (A) Caco-2/TC7 cells were harvested in the presence of Triton X-100 and the lysate fractionated on a 5–40% sucrose gradient. Eleven fractions were collected for immunoblots of SR-BI/CLA-1, EEA1 (early endosome antigen 1) and flottilin-1 (raft marker). (B) Caco-2/TC7 cells were cultured in the absence (control) or presence of PPM or IPM for 10 min and then harvested in the presence of Triton X-100. Cell lysates were applied to a 5–40% sucrose gradient and eleven fractions collected. Fractions 3 to 8 were analyzed by immunoblotting with antibodies against SR-BI/CLA-1 (left panel) and flottilin-1 (right panel). (C) Immunolocalization of SR-BI/CLA-1 and alkaline phosphatase (PLAP, used as raft marker) in the brush border of Caco-2/TC7 cells supplied with PPM. SR-BI/CLA-1 is labelled with anti-rabbit immunoglobulin-gold complexes (18-nm particles) and PLAP with anti-sheep immunoglobulin-gold complexes (12-nm particles). MV, microvilli; bar, 100 nm.

    Journal: PLoS ONE

    Article Title: Sensing of Dietary Lipids by Enterocytes: A New Role for SR-BI/CLA-1

    doi: 10.1371/journal.pone.0004278

    Figure Lengend Snippet: PPM supply induces movement of SR-BI/CLA-1 towards raft microdomains. (A) Caco-2/TC7 cells were harvested in the presence of Triton X-100 and the lysate fractionated on a 5–40% sucrose gradient. Eleven fractions were collected for immunoblots of SR-BI/CLA-1, EEA1 (early endosome antigen 1) and flottilin-1 (raft marker). (B) Caco-2/TC7 cells were cultured in the absence (control) or presence of PPM or IPM for 10 min and then harvested in the presence of Triton X-100. Cell lysates were applied to a 5–40% sucrose gradient and eleven fractions collected. Fractions 3 to 8 were analyzed by immunoblotting with antibodies against SR-BI/CLA-1 (left panel) and flottilin-1 (right panel). (C) Immunolocalization of SR-BI/CLA-1 and alkaline phosphatase (PLAP, used as raft marker) in the brush border of Caco-2/TC7 cells supplied with PPM. SR-BI/CLA-1 is labelled with anti-rabbit immunoglobulin-gold complexes (18-nm particles) and PLAP with anti-sheep immunoglobulin-gold complexes (12-nm particles). MV, microvilli; bar, 100 nm.

    Article Snippet: Sections were analyzed in a Jeol 100 CX II electron microscope.

    Techniques: Western Blot, Marker, Cell Culture

    Immunoreactive COX-2 expression in vasculature-associated cells in response to IL-1 versus LPS. Bright-field images of COX-2-ir cells associated with the vasculature in the forebrain ( top ) and medulla ( bottom ) from rats killed 4 hr after intravenous injection of IL-1 (1.87 μg, left ) or LPS (100 μg/kg, right ). As with IL-1, at 4 hr after LPS treatment, a clear increase in the number and staining intensity of COX-2-positive cells is seen within perivascular regions throughout the brain. However, the predominant cell types manifesting enzyme expression after each treatment are morphologically distinct. COX-2-positive polygonal/multipolar cells ( open arrows ) are seen in response to each treatment and exclusively in material from IL-1-treated animals. COX-2-positive round cells ( arrowheads ) are evident only in rats treated with LPS. Scale bar, 100 μm.

    Journal: The Journal of Neuroscience

    Article Title: Distinct Brain Vascular Cell Types Manifest Inducible Cyclooxygenase Expression as a Function of the Strength and Nature of Immune Insults

    doi: 10.1523/JNEUROSCI.22-13-05606.2002

    Figure Lengend Snippet: Immunoreactive COX-2 expression in vasculature-associated cells in response to IL-1 versus LPS. Bright-field images of COX-2-ir cells associated with the vasculature in the forebrain ( top ) and medulla ( bottom ) from rats killed 4 hr after intravenous injection of IL-1 (1.87 μg, left ) or LPS (100 μg/kg, right ). As with IL-1, at 4 hr after LPS treatment, a clear increase in the number and staining intensity of COX-2-positive cells is seen within perivascular regions throughout the brain. However, the predominant cell types manifesting enzyme expression after each treatment are morphologically distinct. COX-2-positive polygonal/multipolar cells ( open arrows ) are seen in response to each treatment and exclusively in material from IL-1-treated animals. COX-2-positive round cells ( arrowheads ) are evident only in rats treated with LPS. Scale bar, 100 μm.

    Article Snippet: The material was examined in a JEOL 100 CX II transmission electron microscope.

    Techniques: Expressing, Injection, Staining

    LPS-induced COX-2 expression in vasculature-associated cells. SCLM images show dual immunostaining for COX-2 ( green , left ) and RECA-1, a marker for endothelial cells ( red , middle ), in blood vessels in the forebrain. Results of dual immunolabeling of material from rats challenged with 100 μg/kg LPS revealed that many round COX-2-ir cells coexpress the endothelial marker RECA-1 ( right panel ). Another population of COX-2-ir cells, polygonal or multipolar in form, stained positively for the ED2 antigen (data not shown) in LPS-treated rats. The yellow color in the merged image ( right ) represents a positive signal for both markers and is consistent with a perinuclear distribution of COX-2-ir in activated endothelial cells. Arrowhead indicates a COX-2- and RECA-1-positive cell. Arrow indicates a multipolar COX-2-positive cell that did not express RECA-1. Scale bar, 50 μm.

    Journal: The Journal of Neuroscience

    Article Title: Distinct Brain Vascular Cell Types Manifest Inducible Cyclooxygenase Expression as a Function of the Strength and Nature of Immune Insults

    doi: 10.1523/JNEUROSCI.22-13-05606.2002

    Figure Lengend Snippet: LPS-induced COX-2 expression in vasculature-associated cells. SCLM images show dual immunostaining for COX-2 ( green , left ) and RECA-1, a marker for endothelial cells ( red , middle ), in blood vessels in the forebrain. Results of dual immunolabeling of material from rats challenged with 100 μg/kg LPS revealed that many round COX-2-ir cells coexpress the endothelial marker RECA-1 ( right panel ). Another population of COX-2-ir cells, polygonal or multipolar in form, stained positively for the ED2 antigen (data not shown) in LPS-treated rats. The yellow color in the merged image ( right ) represents a positive signal for both markers and is consistent with a perinuclear distribution of COX-2-ir in activated endothelial cells. Arrowhead indicates a COX-2- and RECA-1-positive cell. Arrow indicates a multipolar COX-2-positive cell that did not express RECA-1. Scale bar, 50 μm.

    Article Snippet: The material was examined in a JEOL 100 CX II transmission electron microscope.

    Techniques: Expressing, Immunostaining, Marker, Immunolabeling, Staining

    Fine structure of LPS-sensitive vasculature-associated cells. Electron micrographs showing pre-embedding immunoperoxidase labeling for COX-2 in vasculature-associated cells in the forebrain of a rat treated with 100 μg/kg LPS. COX-2-ir is distributed diffusely within the cytoplasm of a cell ( top panel , dotted line ) that is not an integral component of the vascular wall, is segregated from the brain parenchyma by a basal lamina, and displays morphological features similar to ED2-positive perivascular cells. The bottom panels show examples of COX-2-ir within endothelial cells. Note the perinuclear distribution of the reaction product, consistent with the light-level appearance of COX-2-ir in this cell type. Arrows indicate positive labeling for COX-2. N , Nucleus; bl , basal lamina; EC , endothelial cell; bv , blood vessel. Scale bar, 1 μm.

    Journal: The Journal of Neuroscience

    Article Title: Distinct Brain Vascular Cell Types Manifest Inducible Cyclooxygenase Expression as a Function of the Strength and Nature of Immune Insults

    doi: 10.1523/JNEUROSCI.22-13-05606.2002

    Figure Lengend Snippet: Fine structure of LPS-sensitive vasculature-associated cells. Electron micrographs showing pre-embedding immunoperoxidase labeling for COX-2 in vasculature-associated cells in the forebrain of a rat treated with 100 μg/kg LPS. COX-2-ir is distributed diffusely within the cytoplasm of a cell ( top panel , dotted line ) that is not an integral component of the vascular wall, is segregated from the brain parenchyma by a basal lamina, and displays morphological features similar to ED2-positive perivascular cells. The bottom panels show examples of COX-2-ir within endothelial cells. Note the perinuclear distribution of the reaction product, consistent with the light-level appearance of COX-2-ir in this cell type. Arrows indicate positive labeling for COX-2. N , Nucleus; bl , basal lamina; EC , endothelial cell; bv , blood vessel. Scale bar, 1 μm.

    Article Snippet: The material was examined in a JEOL 100 CX II transmission electron microscope.

    Techniques: Labeling

    Central prostaglandin synthesis blockade disrupts systemic IL-1-induced activation of the paraventricular nucleus and its aminergic afferents. Bright-field photomicrographs show IL-1-induced Fos-ir expression in the paraventricular nucleus ( PVH , top ) and the C1 region of the ventrolateral medulla ( VLM , bottom ) in rats pretreated by intracerebroventricular injection of vehicle ( left ) or indomethacin (10 μg/5 μl) ( right ). As reported previously, intravenous IL-1 (1.87 μg/kg) evokes a robust Fos response within the PVH and C1 regions. However, pretreatment with central infusion of indomethacin, a nonselective inhibitor of COX activity, results in a marked diminution of IL-1 effects at the levels of both medulla and hypothalamus. This finding supports the view that induced synthesis of prostaglandins within the brain is required for the activation of HPA control systems in response to systemic (intravenous) IL-1. Scale bar, 100 μm.

    Journal: The Journal of Neuroscience

    Article Title: Distinct Brain Vascular Cell Types Manifest Inducible Cyclooxygenase Expression as a Function of the Strength and Nature of Immune Insults

    doi: 10.1523/JNEUROSCI.22-13-05606.2002

    Figure Lengend Snippet: Central prostaglandin synthesis blockade disrupts systemic IL-1-induced activation of the paraventricular nucleus and its aminergic afferents. Bright-field photomicrographs show IL-1-induced Fos-ir expression in the paraventricular nucleus ( PVH , top ) and the C1 region of the ventrolateral medulla ( VLM , bottom ) in rats pretreated by intracerebroventricular injection of vehicle ( left ) or indomethacin (10 μg/5 μl) ( right ). As reported previously, intravenous IL-1 (1.87 μg/kg) evokes a robust Fos response within the PVH and C1 regions. However, pretreatment with central infusion of indomethacin, a nonselective inhibitor of COX activity, results in a marked diminution of IL-1 effects at the levels of both medulla and hypothalamus. This finding supports the view that induced synthesis of prostaglandins within the brain is required for the activation of HPA control systems in response to systemic (intravenous) IL-1. Scale bar, 100 μm.

    Article Snippet: The material was examined in a JEOL 100 CX II transmission electron microscope.

    Techniques: Activation Assay, Expressing, Injection, Activity Assay

    Vascular COX-2-ir induction as a function of IL-1 dose. Bright-field images show blood vessels stained for COX-2 ( top row ) or the PVN labeled for Fos-ir ( bottom row ), from rats given vehicle ( left panels ), 1.87 μg/kg ( middle panels ), or 30 μg/kg IL-1 ( right panels ). To provide an index of the strength of the stimulus, Fos-ir induction in the PVH seen in response to the same treatments is shown ( bottom row ). In vehicle-treated rats, few to no COX-2-ir cells are found in association with blood vessels ( top left ), and Fos expression is not detected within the PVH ( bottom left ). As documented previously, 1.87 μg/kg doses of IL-1 stimulate COX-2-expression within polygonal or multipolar cells presumed to conform to ED2-positive perivascular cells ( top , middle , open arrows ); moderate Fos-ir induction is localized principally to the medial parvocellular ( mp ) part of the PVH, with lesser involvement of the dorsal parvocellular ( dp )and posterior magnocellular ( pm ) subdivisions ( bottom , middle ). The 30 μg/kg IL-1 dose produces more robust Fos induction in the PVH ( bottom , right ), comparable to that seen in response to 2 μg/kg LPS. Nevertheless, only elements exhibiting perivascular cell morphology manifest COX-2-ir in response to the higher IL-1 dose ( top , right ). Scale bar, 100 μm.

    Journal: The Journal of Neuroscience

    Article Title: Distinct Brain Vascular Cell Types Manifest Inducible Cyclooxygenase Expression as a Function of the Strength and Nature of Immune Insults

    doi: 10.1523/JNEUROSCI.22-13-05606.2002

    Figure Lengend Snippet: Vascular COX-2-ir induction as a function of IL-1 dose. Bright-field images show blood vessels stained for COX-2 ( top row ) or the PVN labeled for Fos-ir ( bottom row ), from rats given vehicle ( left panels ), 1.87 μg/kg ( middle panels ), or 30 μg/kg IL-1 ( right panels ). To provide an index of the strength of the stimulus, Fos-ir induction in the PVH seen in response to the same treatments is shown ( bottom row ). In vehicle-treated rats, few to no COX-2-ir cells are found in association with blood vessels ( top left ), and Fos expression is not detected within the PVH ( bottom left ). As documented previously, 1.87 μg/kg doses of IL-1 stimulate COX-2-expression within polygonal or multipolar cells presumed to conform to ED2-positive perivascular cells ( top , middle , open arrows ); moderate Fos-ir induction is localized principally to the medial parvocellular ( mp ) part of the PVH, with lesser involvement of the dorsal parvocellular ( dp )and posterior magnocellular ( pm ) subdivisions ( bottom , middle ). The 30 μg/kg IL-1 dose produces more robust Fos induction in the PVH ( bottom , right ), comparable to that seen in response to 2 μg/kg LPS. Nevertheless, only elements exhibiting perivascular cell morphology manifest COX-2-ir in response to the higher IL-1 dose ( top , right ). Scale bar, 100 μm.

    Article Snippet: The material was examined in a JEOL 100 CX II transmission electron microscope.

    Techniques: Staining, Labeling, Expressing

    Strength and locus of COX-2 induction as a function of LPS dose. Bright-field images show vessels stained for COX-2 ( top row ) from rats given 0.1 μg/kg ( left ), 2 μg/kg ( middle ), or 100 μg/kg ( right ) LPS. In rats treated with 0.1 μg/kg LPS ( left ), only cells exhibiting perivascular cell morphology manifest COX-2-ir ( left , open arrows ). Even this low dose provokes significant activation of neurons within the PVH, especially its CRF-rich medial parvocellular ( mp ) subdivision. In response to the 2 μg/kg LPS dose ( middle ), both polygonal/multipolar ( open arrows ) and round-shaped cells ( closed arrowheads ) exhibit COX-2-ir, suggesting involvement of both perivascular and endothelial cells. Fos induction under this condition is marginally increased, with greater involvement of the dorsal parvocellular ( dp ) and posterior magnocellular ( pm ) aspects of the PVH. The 100 μg/kg LPS dose ( right ) also provokes COX-2-ir expression in both polygonal/multipolar ( open arrows ) and round ( arrowheads ) cells, whose number and staining intensity are enhanced. Fos induction in the PVH is most robust under this condition and distributed uniformly throughout all subregions of the nucleus. Scale bar, 100 μm.

    Journal: The Journal of Neuroscience

    Article Title: Distinct Brain Vascular Cell Types Manifest Inducible Cyclooxygenase Expression as a Function of the Strength and Nature of Immune Insults

    doi: 10.1523/JNEUROSCI.22-13-05606.2002

    Figure Lengend Snippet: Strength and locus of COX-2 induction as a function of LPS dose. Bright-field images show vessels stained for COX-2 ( top row ) from rats given 0.1 μg/kg ( left ), 2 μg/kg ( middle ), or 100 μg/kg ( right ) LPS. In rats treated with 0.1 μg/kg LPS ( left ), only cells exhibiting perivascular cell morphology manifest COX-2-ir ( left , open arrows ). Even this low dose provokes significant activation of neurons within the PVH, especially its CRF-rich medial parvocellular ( mp ) subdivision. In response to the 2 μg/kg LPS dose ( middle ), both polygonal/multipolar ( open arrows ) and round-shaped cells ( closed arrowheads ) exhibit COX-2-ir, suggesting involvement of both perivascular and endothelial cells. Fos induction under this condition is marginally increased, with greater involvement of the dorsal parvocellular ( dp ) and posterior magnocellular ( pm ) aspects of the PVH. The 100 μg/kg LPS dose ( right ) also provokes COX-2-ir expression in both polygonal/multipolar ( open arrows ) and round ( arrowheads ) cells, whose number and staining intensity are enhanced. Fos induction in the PVH is most robust under this condition and distributed uniformly throughout all subregions of the nucleus. Scale bar, 100 μm.

    Article Snippet: The material was examined in a JEOL 100 CX II transmission electron microscope.

    Techniques: Staining, Activation Assay, Expressing

    Basal and IL-1-stimulated COX-2 mRNA expression. Dark-field photomicrographs of sections from rats killed 1 hr after intravenous injection of vehicle ( top row ) or 1.87 μg/kg IL-1 ( bottom row ), at the levels of the preoptic area ( left ), paraventricular nucleus ( middle ), and medulla ( right ). In vehicle-treated rats, COX-2 mRNA is evident throughout the isocortex, hippocampal formation, and the area postrema. Some signal is also clearly evident within the meninges ( men ) and a few blood vessels ( bv ). IL-1 treatment does not appear to alter neuronal expression of COX-2 mRNA, although expression by cells associated with the vasculature and the meninges is clearly increased throughout the brain. Scale bar, 100 μm. ac , Anterior commissure; och , optic chiasm; men , meninges; OT , olfactory tubercule; CP , caudate putamen; Pir , piriform cortex; iso , isocortex; DG , dentate gyrus; CA3 , field CA3 of ammon's horn; NLOT , nucleus of lateral olfactory tract; AP , area postrema; cc , central canal; SNV , spinal nucleus of trigeminal.

    Journal: The Journal of Neuroscience

    Article Title: Distinct Brain Vascular Cell Types Manifest Inducible Cyclooxygenase Expression as a Function of the Strength and Nature of Immune Insults

    doi: 10.1523/JNEUROSCI.22-13-05606.2002

    Figure Lengend Snippet: Basal and IL-1-stimulated COX-2 mRNA expression. Dark-field photomicrographs of sections from rats killed 1 hr after intravenous injection of vehicle ( top row ) or 1.87 μg/kg IL-1 ( bottom row ), at the levels of the preoptic area ( left ), paraventricular nucleus ( middle ), and medulla ( right ). In vehicle-treated rats, COX-2 mRNA is evident throughout the isocortex, hippocampal formation, and the area postrema. Some signal is also clearly evident within the meninges ( men ) and a few blood vessels ( bv ). IL-1 treatment does not appear to alter neuronal expression of COX-2 mRNA, although expression by cells associated with the vasculature and the meninges is clearly increased throughout the brain. Scale bar, 100 μm. ac , Anterior commissure; och , optic chiasm; men , meninges; OT , olfactory tubercule; CP , caudate putamen; Pir , piriform cortex; iso , isocortex; DG , dentate gyrus; CA3 , field CA3 of ammon's horn; NLOT , nucleus of lateral olfactory tract; AP , area postrema; cc , central canal; SNV , spinal nucleus of trigeminal.

    Article Snippet: The material was examined in a JEOL 100 CX II transmission electron microscope.

    Techniques: Expressing, Injection

    Immunoreactive COX-2 expression in the brain. Bright-field images of COX-2-ir cells in the isocortex and meninges ( top ) and cells associated with the vasculature in the forebrain ( middle ) and medulla ( bottom ), from rats killed 4 hr after vehicle ( left ) or IL-1 injection ( right ). In agreement with findings at the mRNA level, constitutive COX-2-ir is seen within some cortical neurons and, at lower levels, in the meninges and perivascular regions. At 4 hr after IL-1 (1.87 μg/kg) treatment, a clear increase in the number and staining intensity of COX-2-positive cells is seen within the meninges and perivascular regions, but not in neurons. Scale bar, 100 μm.

    Journal: The Journal of Neuroscience

    Article Title: Distinct Brain Vascular Cell Types Manifest Inducible Cyclooxygenase Expression as a Function of the Strength and Nature of Immune Insults

    doi: 10.1523/JNEUROSCI.22-13-05606.2002

    Figure Lengend Snippet: Immunoreactive COX-2 expression in the brain. Bright-field images of COX-2-ir cells in the isocortex and meninges ( top ) and cells associated with the vasculature in the forebrain ( middle ) and medulla ( bottom ), from rats killed 4 hr after vehicle ( left ) or IL-1 injection ( right ). In agreement with findings at the mRNA level, constitutive COX-2-ir is seen within some cortical neurons and, at lower levels, in the meninges and perivascular regions. At 4 hr after IL-1 (1.87 μg/kg) treatment, a clear increase in the number and staining intensity of COX-2-positive cells is seen within the meninges and perivascular regions, but not in neurons. Scale bar, 100 μm.

    Article Snippet: The material was examined in a JEOL 100 CX II transmission electron microscope.

    Techniques: Expressing, Injection, Staining