Structured Review

Abcam synaptopodin
Expression and distribution of synapse-associated proteins in rat cortical tissue on P90. (A) Distribution of an actin-associated protein <t>synaptopodin</t> in the molecular layer of the parietal cortex, adult control rat. Scale: 10 μm. Indirect immunofluorescence, excitation—488 nm wavelength, emission—552–690 nm wavelength. ( B) Number of labile synaptopodin-labeled dendritic spines in the molecular layer of the parietal cortex in adult rats (P90). Ordinate: number of synaptopodin-positive spines per 100 × 100 μm area. * Statistically significant changes compared to the control ( p ≤ 0.001). (C) Immunoblotting of proteins from adult rat cortical tissue with antibodies against synaptopodin (100 kDa), PSD95 (95 kDa), synaptophysin (37 kDa), and actin (45 kDa). (D) Ratio of the intensity of the bands corresponding to the proteins of interest (white columns—spine-associated protein synaptopodin, gray columns—postsynaptic marker protein PSD95, dotted columns—presynaptic marker synaptophysin) to the intensity of the band of actin. Data presented as the mean ratio of optical density ± SEM. * Statistically significant decrease in synaptopodin expression in adult rats subjected to hypoxia on E14 compared to controls, p ≤ 0.05. No significant changes in PSD95 and synaptophysin can be seen n = 8 in each group of animals. (E) Electrophoretic separation of young (P30) rat cortical tissue proteins and subsequent immunoblotting against synaptopodin (100 kDa), PSD95 (95 kDa), and actin (45 kDa). (F) Ratio of the band intensity of the protein of interest (white, dotted columns—spine-associated protein synaptopodin, gray columns—the postsynaptic marker protein PSD95) to the actin band intensity in young (P30) rat cortical tissue. Data presented as mean optical density ratio ± SEM. Asterisk—significant difference in synaptopodin or PSD95 protein expression between control rats and rats exposed to hypoxia on E14 (two-tailed Mann–Whitney U -test with independent samples, p ≤ 0.05). No significant changes were shown in rats exposed to hypoxia on E18. N = 4 in each group of animals.
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Images

1) Product Images from "Prenatal Hypoxia in Different Periods of Embryogenesis Differentially Affects Cell Migration, Neuronal Plasticity, and Rat Behavior in Postnatal Ontogenesis"

Article Title: Prenatal Hypoxia in Different Periods of Embryogenesis Differentially Affects Cell Migration, Neuronal Plasticity, and Rat Behavior in Postnatal Ontogenesis

Journal: Frontiers in Neuroscience

doi: 10.3389/fnins.2016.00126

Expression and distribution of synapse-associated proteins in rat cortical tissue on P90. (A) Distribution of an actin-associated protein synaptopodin in the molecular layer of the parietal cortex, adult control rat. Scale: 10 μm. Indirect immunofluorescence, excitation—488 nm wavelength, emission—552–690 nm wavelength. ( B) Number of labile synaptopodin-labeled dendritic spines in the molecular layer of the parietal cortex in adult rats (P90). Ordinate: number of synaptopodin-positive spines per 100 × 100 μm area. * Statistically significant changes compared to the control ( p ≤ 0.001). (C) Immunoblotting of proteins from adult rat cortical tissue with antibodies against synaptopodin (100 kDa), PSD95 (95 kDa), synaptophysin (37 kDa), and actin (45 kDa). (D) Ratio of the intensity of the bands corresponding to the proteins of interest (white columns—spine-associated protein synaptopodin, gray columns—postsynaptic marker protein PSD95, dotted columns—presynaptic marker synaptophysin) to the intensity of the band of actin. Data presented as the mean ratio of optical density ± SEM. * Statistically significant decrease in synaptopodin expression in adult rats subjected to hypoxia on E14 compared to controls, p ≤ 0.05. No significant changes in PSD95 and synaptophysin can be seen n = 8 in each group of animals. (E) Electrophoretic separation of young (P30) rat cortical tissue proteins and subsequent immunoblotting against synaptopodin (100 kDa), PSD95 (95 kDa), and actin (45 kDa). (F) Ratio of the band intensity of the protein of interest (white, dotted columns—spine-associated protein synaptopodin, gray columns—the postsynaptic marker protein PSD95) to the actin band intensity in young (P30) rat cortical tissue. Data presented as mean optical density ratio ± SEM. Asterisk—significant difference in synaptopodin or PSD95 protein expression between control rats and rats exposed to hypoxia on E14 (two-tailed Mann–Whitney U -test with independent samples, p ≤ 0.05). No significant changes were shown in rats exposed to hypoxia on E18. N = 4 in each group of animals.
Figure Legend Snippet: Expression and distribution of synapse-associated proteins in rat cortical tissue on P90. (A) Distribution of an actin-associated protein synaptopodin in the molecular layer of the parietal cortex, adult control rat. Scale: 10 μm. Indirect immunofluorescence, excitation—488 nm wavelength, emission—552–690 nm wavelength. ( B) Number of labile synaptopodin-labeled dendritic spines in the molecular layer of the parietal cortex in adult rats (P90). Ordinate: number of synaptopodin-positive spines per 100 × 100 μm area. * Statistically significant changes compared to the control ( p ≤ 0.001). (C) Immunoblotting of proteins from adult rat cortical tissue with antibodies against synaptopodin (100 kDa), PSD95 (95 kDa), synaptophysin (37 kDa), and actin (45 kDa). (D) Ratio of the intensity of the bands corresponding to the proteins of interest (white columns—spine-associated protein synaptopodin, gray columns—postsynaptic marker protein PSD95, dotted columns—presynaptic marker synaptophysin) to the intensity of the band of actin. Data presented as the mean ratio of optical density ± SEM. * Statistically significant decrease in synaptopodin expression in adult rats subjected to hypoxia on E14 compared to controls, p ≤ 0.05. No significant changes in PSD95 and synaptophysin can be seen n = 8 in each group of animals. (E) Electrophoretic separation of young (P30) rat cortical tissue proteins and subsequent immunoblotting against synaptopodin (100 kDa), PSD95 (95 kDa), and actin (45 kDa). (F) Ratio of the band intensity of the protein of interest (white, dotted columns—spine-associated protein synaptopodin, gray columns—the postsynaptic marker protein PSD95) to the actin band intensity in young (P30) rat cortical tissue. Data presented as mean optical density ratio ± SEM. Asterisk—significant difference in synaptopodin or PSD95 protein expression between control rats and rats exposed to hypoxia on E14 (two-tailed Mann–Whitney U -test with independent samples, p ≤ 0.05). No significant changes were shown in rats exposed to hypoxia on E18. N = 4 in each group of animals.

Techniques Used: Expressing, Immunofluorescence, Labeling, Marker, Two Tailed Test, MANN-WHITNEY

2) Product Images from "Prenatal Hypoxia in Different Periods of Embryogenesis Differentially Affects Cell Migration, Neuronal Plasticity, and Rat Behavior in Postnatal Ontogenesis"

Article Title: Prenatal Hypoxia in Different Periods of Embryogenesis Differentially Affects Cell Migration, Neuronal Plasticity, and Rat Behavior in Postnatal Ontogenesis

Journal: Frontiers in Neuroscience

doi: 10.3389/fnins.2016.00126

Expression and distribution of synapse-associated proteins in rat cortical tissue on P90. (A) Distribution of an actin-associated protein synaptopodin in the molecular layer of the parietal cortex, adult control rat. Scale: 10 μm. Indirect immunofluorescence, excitation—488 nm wavelength, emission—552–690 nm wavelength. ( B) Number of labile synaptopodin-labeled dendritic spines in the molecular layer of the parietal cortex in adult rats (P90). Ordinate: number of synaptopodin-positive spines per 100 × 100 μm area. * Statistically significant changes compared to the control ( p ≤ 0.001). (C) Immunoblotting of proteins from adult rat cortical tissue with antibodies against synaptopodin (100 kDa), PSD95 (95 kDa), synaptophysin (37 kDa), and actin (45 kDa). (D) Ratio of the intensity of the bands corresponding to the proteins of interest (white columns—spine-associated protein synaptopodin, gray columns—postsynaptic marker protein PSD95, dotted columns—presynaptic marker synaptophysin) to the intensity of the band of actin. Data presented as the mean ratio of optical density ± SEM. * Statistically significant decrease in synaptopodin expression in adult rats subjected to hypoxia on E14 compared to controls, p ≤ 0.05. No significant changes in PSD95 and synaptophysin can be seen n = 8 in each group of animals. (E) Electrophoretic separation of young (P30) rat cortical tissue proteins and subsequent immunoblotting against synaptopodin (100 kDa), PSD95 (95 kDa), and actin (45 kDa). (F) Ratio of the band intensity of the protein of interest (white, dotted columns—spine-associated protein synaptopodin, gray columns—the postsynaptic marker protein PSD95) to the actin band intensity in young (P30) rat cortical tissue. Data presented as mean optical density ratio ± SEM. Asterisk—significant difference in synaptopodin or PSD95 protein expression between control rats and rats exposed to hypoxia on E14 (two-tailed Mann–Whitney U -test with independent samples, p ≤ 0.05). No significant changes were shown in rats exposed to hypoxia on E18. N = 4 in each group of animals.
Figure Legend Snippet: Expression and distribution of synapse-associated proteins in rat cortical tissue on P90. (A) Distribution of an actin-associated protein synaptopodin in the molecular layer of the parietal cortex, adult control rat. Scale: 10 μm. Indirect immunofluorescence, excitation—488 nm wavelength, emission—552–690 nm wavelength. ( B) Number of labile synaptopodin-labeled dendritic spines in the molecular layer of the parietal cortex in adult rats (P90). Ordinate: number of synaptopodin-positive spines per 100 × 100 μm area. * Statistically significant changes compared to the control ( p ≤ 0.001). (C) Immunoblotting of proteins from adult rat cortical tissue with antibodies against synaptopodin (100 kDa), PSD95 (95 kDa), synaptophysin (37 kDa), and actin (45 kDa). (D) Ratio of the intensity of the bands corresponding to the proteins of interest (white columns—spine-associated protein synaptopodin, gray columns—postsynaptic marker protein PSD95, dotted columns—presynaptic marker synaptophysin) to the intensity of the band of actin. Data presented as the mean ratio of optical density ± SEM. * Statistically significant decrease in synaptopodin expression in adult rats subjected to hypoxia on E14 compared to controls, p ≤ 0.05. No significant changes in PSD95 and synaptophysin can be seen n = 8 in each group of animals. (E) Electrophoretic separation of young (P30) rat cortical tissue proteins and subsequent immunoblotting against synaptopodin (100 kDa), PSD95 (95 kDa), and actin (45 kDa). (F) Ratio of the band intensity of the protein of interest (white, dotted columns—spine-associated protein synaptopodin, gray columns—the postsynaptic marker protein PSD95) to the actin band intensity in young (P30) rat cortical tissue. Data presented as mean optical density ratio ± SEM. Asterisk—significant difference in synaptopodin or PSD95 protein expression between control rats and rats exposed to hypoxia on E14 (two-tailed Mann–Whitney U -test with independent samples, p ≤ 0.05). No significant changes were shown in rats exposed to hypoxia on E18. N = 4 in each group of animals.

Techniques Used: Expressing, Immunofluorescence, Labeling, Marker, Two Tailed Test, MANN-WHITNEY

3) Product Images from "Combined Melatonin and Extracorporeal Shock Wave Therapy Enhances Podocyte Protection and Ameliorates Kidney Function in a Diabetic Nephropathy Rat Model"

Article Title: Combined Melatonin and Extracorporeal Shock Wave Therapy Enhances Podocyte Protection and Ameliorates Kidney Function in a Diabetic Nephropathy Rat Model

Journal: Antioxidants

doi: 10.3390/antiox10050733

Mel combined SW therapy significantly increased podocyte number and enhanced podocyte viability and glomerular function. ( A , B ) Western blot (WB) analyzed WT-1 expression in renal tissue and quantification of WB by densitometric analysis. ( C , D ) Representative fluorescent images of glomeruli by IF stained with synaptopodin (green) indicating podocytes and quantification of IF stained by image analysis; bar = 50 μm. ( E ) ELISA analyzed nephrin level in renal tissue to represent the degree of preserved podocyte viability and glomerular function in kidneys. ‡, p
Figure Legend Snippet: Mel combined SW therapy significantly increased podocyte number and enhanced podocyte viability and glomerular function. ( A , B ) Western blot (WB) analyzed WT-1 expression in renal tissue and quantification of WB by densitometric analysis. ( C , D ) Representative fluorescent images of glomeruli by IF stained with synaptopodin (green) indicating podocytes and quantification of IF stained by image analysis; bar = 50 μm. ( E ) ELISA analyzed nephrin level in renal tissue to represent the degree of preserved podocyte viability and glomerular function in kidneys. ‡, p

Techniques Used: Western Blot, Expressing, Staining, Enzyme-linked Immunosorbent Assay

4) Product Images from "Vitamin D/vitamin D receptor/Atg16L1 axis maintains podocyte autophagy and survival in diabetic kidney disease"

Article Title: Vitamin D/vitamin D receptor/Atg16L1 axis maintains podocyte autophagy and survival in diabetic kidney disease

Journal: Renal Failure

doi: 10.1080/0886022X.2022.2063744

Renal failure in STZ-induced diabetic rats and in vitro MPC-5 injury stimulated with high-glucose was alleviated by aVitD3. (A) PAS staining of kidney sections. SD male rats were intraperitoneally injected with 60 mg/kg streptozotocin. After 3 days, the rats with STZ treatment were garaged with 0.1μg/kg/d calcitriol or vehicle solution daily for consecutive 18 weeks. Kidney tissues were collected for histology. (B) Representative images of immunohistochemical staining for desmin in the renal cortex at 18th week (×400). (C) MPC-5 cells viability. After being administered with different doses of aVitD3 (1–500 nmol/L) for 24 h, the MPC-5 cells viability was determined by CCK-8 assay. MPC-5 were cultured for 24h in a medium with 30 mM glucose or 5.5 mM glucose in the absence or presence of 100 nmol/L aVitD3. (D) Representative western blot images of Nephrin, Podocin, Synaptopodin and Desmin expression. (E–I) Relative expression of proteins levels. Band densities were measured by the ImageJ program. The ratio of protein/actin density was calculated and normalized with the sham controls. Data were presented as mean ± SD. n = 4. ** p
Figure Legend Snippet: Renal failure in STZ-induced diabetic rats and in vitro MPC-5 injury stimulated with high-glucose was alleviated by aVitD3. (A) PAS staining of kidney sections. SD male rats were intraperitoneally injected with 60 mg/kg streptozotocin. After 3 days, the rats with STZ treatment were garaged with 0.1μg/kg/d calcitriol or vehicle solution daily for consecutive 18 weeks. Kidney tissues were collected for histology. (B) Representative images of immunohistochemical staining for desmin in the renal cortex at 18th week (×400). (C) MPC-5 cells viability. After being administered with different doses of aVitD3 (1–500 nmol/L) for 24 h, the MPC-5 cells viability was determined by CCK-8 assay. MPC-5 were cultured for 24h in a medium with 30 mM glucose or 5.5 mM glucose in the absence or presence of 100 nmol/L aVitD3. (D) Representative western blot images of Nephrin, Podocin, Synaptopodin and Desmin expression. (E–I) Relative expression of proteins levels. Band densities were measured by the ImageJ program. The ratio of protein/actin density was calculated and normalized with the sham controls. Data were presented as mean ± SD. n = 4. ** p

Techniques Used: In Vitro, Staining, Injection, Immunohistochemistry, CCK-8 Assay, Cell Culture, Western Blot, Expressing

Atg16L1 siRNA Knocked Down Atg16L1 and reduced protective effect of aVitD3 on MPC-5 injury Induced by high-glucose. MPC-5 cells were transfected with Atg16L1 siRNA (si-Atg16L1) or normal control siRNA (si-NC) and subjected to the indicated treatment. (A) Representative image of Atg16L1 immunoblot. Proteins were extracted from the cells, and Atg16L expression was detected by Western blotting. (B) The cell viability analysis. (C) Immunofluorescence (IF) assays of Synaptopodin (green) and DAPI (blue) images of cultured MPC-5 under high-glucose conditions or treated with aVitD3, si-NC, si-Atg16L1 respectively. (D) Representative immunoblot images of Nephrin, Podocin, Synaptopodin and Desmin. (E–I) Relative expression of proteins levels. Band densities were measured by the ImageJ program. The ratio of protein/actin density was calculated and normalized with the sham controls. Data were presented as mean ± SD. n = 5. ** p
Figure Legend Snippet: Atg16L1 siRNA Knocked Down Atg16L1 and reduced protective effect of aVitD3 on MPC-5 injury Induced by high-glucose. MPC-5 cells were transfected with Atg16L1 siRNA (si-Atg16L1) or normal control siRNA (si-NC) and subjected to the indicated treatment. (A) Representative image of Atg16L1 immunoblot. Proteins were extracted from the cells, and Atg16L expression was detected by Western blotting. (B) The cell viability analysis. (C) Immunofluorescence (IF) assays of Synaptopodin (green) and DAPI (blue) images of cultured MPC-5 under high-glucose conditions or treated with aVitD3, si-NC, si-Atg16L1 respectively. (D) Representative immunoblot images of Nephrin, Podocin, Synaptopodin and Desmin. (E–I) Relative expression of proteins levels. Band densities were measured by the ImageJ program. The ratio of protein/actin density was calculated and normalized with the sham controls. Data were presented as mean ± SD. n = 5. ** p

Techniques Used: Transfection, Expressing, Western Blot, Immunofluorescence, Cell Culture

VDR siRNA knocked down VDR reduced the protective effect of aVitD3 on MPC-5 injury Induced by high glucose. MPC-5 cells were transfected with VDR siRNA (si-VDR) or normal control siRNA (si-NC) and subjected to the indicated treatment. (A) Representative image of VDR immunoblot. (B) The MPC-5 cells' viability was determined by the CCK-8 assay. (C) Nephrin, Podocin, Synaptopodin and Desmin expression. Representative images from Western blot results. (D–H) Relative expression of proteins levels. Band densities were measured by the ImageJ program. The ratio of protein/actin density was calculated and normalized with the sham controls. Data were presented as mean ± SD. n = 5. ** p
Figure Legend Snippet: VDR siRNA knocked down VDR reduced the protective effect of aVitD3 on MPC-5 injury Induced by high glucose. MPC-5 cells were transfected with VDR siRNA (si-VDR) or normal control siRNA (si-NC) and subjected to the indicated treatment. (A) Representative image of VDR immunoblot. (B) The MPC-5 cells' viability was determined by the CCK-8 assay. (C) Nephrin, Podocin, Synaptopodin and Desmin expression. Representative images from Western blot results. (D–H) Relative expression of proteins levels. Band densities were measured by the ImageJ program. The ratio of protein/actin density was calculated and normalized with the sham controls. Data were presented as mean ± SD. n = 5. ** p

Techniques Used: Transfection, CCK-8 Assay, Expressing, Western Blot

5) Product Images from "Plectin protects podocytes from adriamycin‐induced apoptosis and F‐actin cytoskeletal disruption through the integrin α6β4/ FAK/p38 MAPK pathway, et al. Plectin protects podocytes from adriamycin‐induced apoptosis and F‐actin cytoskeletal disruption through the integrin α6β4/FAK/p38 MAPK pathway"

Article Title: Plectin protects podocytes from adriamycin‐induced apoptosis and F‐actin cytoskeletal disruption through the integrin α6β4/ FAK/p38 MAPK pathway, et al. Plectin protects podocytes from adriamycin‐induced apoptosis and F‐actin cytoskeletal disruption through the integrin α6β4/FAK/p38 MAPK pathway

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13816

ADR contributed to the development of proteinuria and renal dysfunction by inhibiting plectin expression and activating the integrin α6β4/ FAK /p38 pathway. ADR induced nephropathy was introduced by a single injection of 7.5 mg/kg ADR via the tail vein. All rats were killed at the end of the 4th week after ADR injection. A, Light microscopic examination revealed glomerular atrophy and disappearance as well as renal tubular swelling after ADR treatment. B, TEM examination of the NC group revealed the presence of normal glomerular ultrastructure. TEM examination of the ADR group revealed the presence of diffuse foot process effacement, GBM thickening, slit diaphragm loss and mesangial sclerosis. C‐D, Western blot showed that WT 1 and synaptopodin protein expression levels were decreased and that desmin protein expression levels were increased in the ADR group compared with the NC group. E, Western blot showed that plectin expression was suppressed in the ADR ‐treated group (n = 5) compared with the NC group (n = 5). F‐G, Immunohistochemical analysis showed that plectin expression in glomeruli was decreased in ADR treated kidney tissues (n = 5) compared with normal kidney tissues (n = 5). H‐I, Western blot showed that integrin α6β4, FAK and p38 were activated by ADR treatment. J‐K, Western blot showed that cleaved caspase‐3 and Bax protein expression was increased in the ADR group (n = 5) compared with the NC group (n = 5). ** P
Figure Legend Snippet: ADR contributed to the development of proteinuria and renal dysfunction by inhibiting plectin expression and activating the integrin α6β4/ FAK /p38 pathway. ADR induced nephropathy was introduced by a single injection of 7.5 mg/kg ADR via the tail vein. All rats were killed at the end of the 4th week after ADR injection. A, Light microscopic examination revealed glomerular atrophy and disappearance as well as renal tubular swelling after ADR treatment. B, TEM examination of the NC group revealed the presence of normal glomerular ultrastructure. TEM examination of the ADR group revealed the presence of diffuse foot process effacement, GBM thickening, slit diaphragm loss and mesangial sclerosis. C‐D, Western blot showed that WT 1 and synaptopodin protein expression levels were decreased and that desmin protein expression levels were increased in the ADR group compared with the NC group. E, Western blot showed that plectin expression was suppressed in the ADR ‐treated group (n = 5) compared with the NC group (n = 5). F‐G, Immunohistochemical analysis showed that plectin expression in glomeruli was decreased in ADR treated kidney tissues (n = 5) compared with normal kidney tissues (n = 5). H‐I, Western blot showed that integrin α6β4, FAK and p38 were activated by ADR treatment. J‐K, Western blot showed that cleaved caspase‐3 and Bax protein expression was increased in the ADR group (n = 5) compared with the NC group (n = 5). ** P

Techniques Used: Expressing, Injection, Transmission Electron Microscopy, Western Blot, Immunohistochemistry

Inhibiting FAK or p38 alleviated siPlectin‐induced podocyte injury. For the NC + siPlectin group and NC + Scramble group, podocyte was transiently transfected with siPlectin or scramble RNA at a final concentration of 20 nmol/L for 4 h and then cultured normally for 68 h. For inhibitor studies, podocyte was preincubated with the FAK inhibitor 14 (50 μmol/L), the p38 inhibitor SB 203580 (5 μmol/L) or DMSO vehicle respectively for 1 h before siPlectin transfection and then incubated for an additional 72 h until podocyte collection. A, Western blot showed that siPlectin transfection successfully silenced plectin protein expression in the NC + siPlectin group. Inhibiting FAK in the NC + siPlectin + FAK inhibitor group or p38 in the NC + siPlectin + p38 inhibitor group had no effect on plectin expression. B, Western blot showed that FAK inhibition or p38 inhibition significantly attenuated the abnormalities in WT 1, synaptopodin and desmin expression induced by siPlectin. C, Flow cytometry showed that FAK inhibition or p38 inhibition significantly alleviated siPlectin‐induced apoptosis. D, Immunofluorescence staining showed that FAK inhibition or p38 inhibition reversed siPlectin‐induced F‐actin disruption. E‐F, Western blot showed that integrin α6β4, FAK and p38 phosphorylation levels were elevated in the NC + siPlectin group. FAK inhibition at the Y397 site did not affect siPlectin‐induced integrin α6β4 phosphorylation levels but decreased p38 phosphorylation levels in the NC + siPlectin + FAK inhibitor group compared with the NC + siPlectin + DMSO group. p38 inhibition in the NC + siPlectin + p38 inhibitor group had no impact on integrin α6β4 and FAK phosphorylation levels. Data shown are representative of three independent experiments (n = 3). ** P
Figure Legend Snippet: Inhibiting FAK or p38 alleviated siPlectin‐induced podocyte injury. For the NC + siPlectin group and NC + Scramble group, podocyte was transiently transfected with siPlectin or scramble RNA at a final concentration of 20 nmol/L for 4 h and then cultured normally for 68 h. For inhibitor studies, podocyte was preincubated with the FAK inhibitor 14 (50 μmol/L), the p38 inhibitor SB 203580 (5 μmol/L) or DMSO vehicle respectively for 1 h before siPlectin transfection and then incubated for an additional 72 h until podocyte collection. A, Western blot showed that siPlectin transfection successfully silenced plectin protein expression in the NC + siPlectin group. Inhibiting FAK in the NC + siPlectin + FAK inhibitor group or p38 in the NC + siPlectin + p38 inhibitor group had no effect on plectin expression. B, Western blot showed that FAK inhibition or p38 inhibition significantly attenuated the abnormalities in WT 1, synaptopodin and desmin expression induced by siPlectin. C, Flow cytometry showed that FAK inhibition or p38 inhibition significantly alleviated siPlectin‐induced apoptosis. D, Immunofluorescence staining showed that FAK inhibition or p38 inhibition reversed siPlectin‐induced F‐actin disruption. E‐F, Western blot showed that integrin α6β4, FAK and p38 phosphorylation levels were elevated in the NC + siPlectin group. FAK inhibition at the Y397 site did not affect siPlectin‐induced integrin α6β4 phosphorylation levels but decreased p38 phosphorylation levels in the NC + siPlectin + FAK inhibitor group compared with the NC + siPlectin + DMSO group. p38 inhibition in the NC + siPlectin + p38 inhibitor group had no impact on integrin α6β4 and FAK phosphorylation levels. Data shown are representative of three independent experiments (n = 3). ** P

Techniques Used: Transfection, Concentration Assay, Cell Culture, Incubation, Western Blot, Expressing, Inhibition, Flow Cytometry, Cytometry, Immunofluorescence, Staining

Restoring plectin expression prevented ADR ‐induced podocyte injury. For the ADR group, podocyte was treated with 0.5 μg/ mL ADR for 12 h. For the ADR + plectin group or ADR + MOCK group, podocyte was incubated with pEGFP ‐N1‐plectin plasmids or empty vectors for 6 h and then cultured normally for 42 h, 0.5 μg/ mL ADR was added 12 h prior to cell harvest. A‐B, Real‐time PCR and Western blot analysis showed that plectin expression was 2‐3 times of that in control group after transfecting pEGFP ‐N1‐plectin plasmids into podocyte. C‐D, Western blot showed that plectin protein expression levels were significantly increased in the ADR + plectin group compared with the ADR and ADR + Mock groups. E‐F, Flow cytometry analysis showed that podocyte apoptosis was alleviated in the ADR + plectin group compared with the ADR and ADR + Mock groups. G, Immunofluorescence staining showed that restoring plectin expression in the ADR + plectin group ameliorated ADR ‐induced F‐actin filament disruption. H‐I, Western blot showed that WT 1 and synaptopodin protein expression levels were increased and that desmin protein expression levels were decreased in the ADR + plectin group compared with the ADR and ADR + Mock groups. J‐K, Western blot showed that integrin α6β4, FAK and p38 phosphorylation levels were higher in the ADR group than in the NC group. Restoring plectin expression in the ADR + plectin group suppressed integrin α6β4, FAK and p38 phosphorylation but had no effect on total integrin α6β4, FAK and p38 expression levels. Data shown are representative of three independent experiments (n = 3). ** P
Figure Legend Snippet: Restoring plectin expression prevented ADR ‐induced podocyte injury. For the ADR group, podocyte was treated with 0.5 μg/ mL ADR for 12 h. For the ADR + plectin group or ADR + MOCK group, podocyte was incubated with pEGFP ‐N1‐plectin plasmids or empty vectors for 6 h and then cultured normally for 42 h, 0.5 μg/ mL ADR was added 12 h prior to cell harvest. A‐B, Real‐time PCR and Western blot analysis showed that plectin expression was 2‐3 times of that in control group after transfecting pEGFP ‐N1‐plectin plasmids into podocyte. C‐D, Western blot showed that plectin protein expression levels were significantly increased in the ADR + plectin group compared with the ADR and ADR + Mock groups. E‐F, Flow cytometry analysis showed that podocyte apoptosis was alleviated in the ADR + plectin group compared with the ADR and ADR + Mock groups. G, Immunofluorescence staining showed that restoring plectin expression in the ADR + plectin group ameliorated ADR ‐induced F‐actin filament disruption. H‐I, Western blot showed that WT 1 and synaptopodin protein expression levels were increased and that desmin protein expression levels were decreased in the ADR + plectin group compared with the ADR and ADR + Mock groups. J‐K, Western blot showed that integrin α6β4, FAK and p38 phosphorylation levels were higher in the ADR group than in the NC group. Restoring plectin expression in the ADR + plectin group suppressed integrin α6β4, FAK and p38 phosphorylation but had no effect on total integrin α6β4, FAK and p38 expression levels. Data shown are representative of three independent experiments (n = 3). ** P

Techniques Used: Expressing, Incubation, Cell Culture, Real-time Polymerase Chain Reaction, Western Blot, Flow Cytometry, Cytometry, Immunofluorescence, Staining

Plectin suppression produced similar effects as ADR ‐induced podocyte injury by facilitating integrin α6β4‐mediated FAK and p38 activation. For the ADR group, podocyte was treated with 0.5 μg/ mL ADR for 12 h. For the NC + siPlectin group and NC + Scramble group, podocyte was transiently transfected with siPlectin or scrambled RNA at a final concentration of 20 nmol/L for 4 h and then cultured normally for 68 h. A‐B, Western blot showed that plectin protein expression was significantly decreased in the NC + siPlectin group compared with the NC + Scramble groups. Mutating the Y1494 residue of integrin α6β4 in the NC + siPlectin + β4 mutant group had no effect on plectin protein expression. C‐D, Flow cytometry demonstrated increased podocyte apoptosis in the NC + siPlectin group compared with the NC + Scramble group. Mutating integrin α6β4 alleviated siPlectin transfection‐induced apoptosis. E, Immunofluorescence staining demonstrated the presence of significant F‐actin disruption in the NC + siPlectin group compared with the NC + Scramble group. Mutating integrin α6β4 reversed siPlectin transfection‐induced F‐actin disruption. F‐G, Western blot showed that WT 1 and synaptopodin expression levels were significantly decreased and that desmin expression levels were significantly increased in the NC + siPlectin group compared with the NC + Scramble group. These abnormalities were partially reversed by integrin α6β4 mutation in NC + siPlectin + β4 mutant group. H‐I, Western blot showed that siPlectin transfection activated integrin α6β4, FAK and p38 phosphorylation, whereas mutating integrin α6β4 abolished the effects of siPlectin. Data shown are representative of three independent experiments (n = 3). ** P
Figure Legend Snippet: Plectin suppression produced similar effects as ADR ‐induced podocyte injury by facilitating integrin α6β4‐mediated FAK and p38 activation. For the ADR group, podocyte was treated with 0.5 μg/ mL ADR for 12 h. For the NC + siPlectin group and NC + Scramble group, podocyte was transiently transfected with siPlectin or scrambled RNA at a final concentration of 20 nmol/L for 4 h and then cultured normally for 68 h. A‐B, Western blot showed that plectin protein expression was significantly decreased in the NC + siPlectin group compared with the NC + Scramble groups. Mutating the Y1494 residue of integrin α6β4 in the NC + siPlectin + β4 mutant group had no effect on plectin protein expression. C‐D, Flow cytometry demonstrated increased podocyte apoptosis in the NC + siPlectin group compared with the NC + Scramble group. Mutating integrin α6β4 alleviated siPlectin transfection‐induced apoptosis. E, Immunofluorescence staining demonstrated the presence of significant F‐actin disruption in the NC + siPlectin group compared with the NC + Scramble group. Mutating integrin α6β4 reversed siPlectin transfection‐induced F‐actin disruption. F‐G, Western blot showed that WT 1 and synaptopodin expression levels were significantly decreased and that desmin expression levels were significantly increased in the NC + siPlectin group compared with the NC + Scramble group. These abnormalities were partially reversed by integrin α6β4 mutation in NC + siPlectin + β4 mutant group. H‐I, Western blot showed that siPlectin transfection activated integrin α6β4, FAK and p38 phosphorylation, whereas mutating integrin α6β4 abolished the effects of siPlectin. Data shown are representative of three independent experiments (n = 3). ** P

Techniques Used: Produced, Activation Assay, Transfection, Concentration Assay, Cell Culture, Western Blot, Expressing, Mutagenesis, Flow Cytometry, Cytometry, Immunofluorescence, Staining

6) Product Images from "Targeted Proteomics of Isolated Glomeruli from the Kidneys of Diabetic Rats: Sorbin and SH3 Domain Containing 2 Is a Novel Protein Associated with Diabetic Nephropathy"

Article Title: Targeted Proteomics of Isolated Glomeruli from the Kidneys of Diabetic Rats: Sorbin and SH3 Domain Containing 2 Is a Novel Protein Associated with Diabetic Nephropathy

Journal: Experimental Diabetes Research

doi: 10.1155/2011/979354

Immunofluorescence for SORBS2: red (a), synaptopodin: green (b), and merge SORBS2 and synaptopodin: yellow (c) in OLETF rats at 38 weeks of age. SORBS2 was expressed as a capillary pattern in glomeruli from OLETF rats at 38 weeks of age. Scale bar = 20 μ m.
Figure Legend Snippet: Immunofluorescence for SORBS2: red (a), synaptopodin: green (b), and merge SORBS2 and synaptopodin: yellow (c) in OLETF rats at 38 weeks of age. SORBS2 was expressed as a capillary pattern in glomeruli from OLETF rats at 38 weeks of age. Scale bar = 20 μ m.

Techniques Used: Immunofluorescence

7) Product Images from "HDAC6‐mediated α‐tubulin deacetylation suppresses autophagy and enhances motility of podocytes in diabetic nephropathy, et al. HDAC6‐mediated α‐tubulin deacetylation suppresses autophagy and enhances motility of podocytes in diabetic nephropathy"

Article Title: HDAC6‐mediated α‐tubulin deacetylation suppresses autophagy and enhances motility of podocytes in diabetic nephropathy, et al. HDAC6‐mediated α‐tubulin deacetylation suppresses autophagy and enhances motility of podocytes in diabetic nephropathy

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.15772

Selective inhibition of HDAC6 ameliorated renal injury in db/db mice. The activity of HDAC6 in the kidneys of mice treated with different stimuli (A), n = 5, 5 independent experiments. ACR was tested at the indicated time points(B), n = 6, 6 mice for each group. And the serum creatinine of mice treated with different stimuli (C), n = 5, 5 mice for each group. Representative immunohistochemical staining (D) and quantification (E) of WT1 in the glomerulus of mice at 21 wks old, n = 3, 3 mice for each group and 5 glomeruli for each mouse. Immunofluorescent staining (F) and the quantification of synaptopodin (G), n = 5, 5 mice for each group and 5 glomeruli for each mouse. ACR, albumin creatinine ratio; BKS, C57BL/KsJ; DMSO, dimethyl sulfoxide; HDAC6, histone deacetylase 6
Figure Legend Snippet: Selective inhibition of HDAC6 ameliorated renal injury in db/db mice. The activity of HDAC6 in the kidneys of mice treated with different stimuli (A), n = 5, 5 independent experiments. ACR was tested at the indicated time points(B), n = 6, 6 mice for each group. And the serum creatinine of mice treated with different stimuli (C), n = 5, 5 mice for each group. Representative immunohistochemical staining (D) and quantification (E) of WT1 in the glomerulus of mice at 21 wks old, n = 3, 3 mice for each group and 5 glomeruli for each mouse. Immunofluorescent staining (F) and the quantification of synaptopodin (G), n = 5, 5 mice for each group and 5 glomeruli for each mouse. ACR, albumin creatinine ratio; BKS, C57BL/KsJ; DMSO, dimethyl sulfoxide; HDAC6, histone deacetylase 6

Techniques Used: Inhibition, Mouse Assay, Activity Assay, Immunohistochemistry, Staining, Histone Deacetylase Assay

HDAC6 reduced ac‐α‐tubulin and disrupted podocyte architectural integrity by restraining autophagy. HDAC6 (red) co‐localized with the α‐tubulin (green) as representative immunofluorescent staining shown (A), n = 3, 3 independent experiments. Immunoprecipitation assay of HDAC6 and α‐tubulin (B), n = 3, 3 independent experiments. Inhibition of HDAC6 selectively by tubacin restored the levels of synaptopodin (green) and ac‐α‐tubulin (red) in AGE‐treated podocytes as representative immunofluorescent staining shown (C). The expression and skeletal structure of podocytes disrupted by AGE were partially restored by tubacin (C), n = 3, 3 independent experiments. Overexpression of HDAC6 reduced ac‐α‐tubulin and LC3‐II accumulation. Inhibition of HDAC6 reversed the expression of ac‐α‐tubulin and LC3‐II as immunofluorescence shown (D) and summarized data (E and F), n = 4, 4 independent experiments. Representative Western blot analysis (G) and statistical graphic (H) of tubacin increased HDAC6‐induced ac‐α‐tubulin levels at Lys40 but not at Lys112 or Lys352, n = 3, 3 independent experiments. AGE, advanced glycation end products; CON, control; HDAC6, histone deacetylase 6; IP, immunoprecipitation; MFI, mean fluorescence intensity; pc‐HADC6, pcDNA3.1‐HDAC6; si‐HDAC6, siRNA of HDAC6
Figure Legend Snippet: HDAC6 reduced ac‐α‐tubulin and disrupted podocyte architectural integrity by restraining autophagy. HDAC6 (red) co‐localized with the α‐tubulin (green) as representative immunofluorescent staining shown (A), n = 3, 3 independent experiments. Immunoprecipitation assay of HDAC6 and α‐tubulin (B), n = 3, 3 independent experiments. Inhibition of HDAC6 selectively by tubacin restored the levels of synaptopodin (green) and ac‐α‐tubulin (red) in AGE‐treated podocytes as representative immunofluorescent staining shown (C). The expression and skeletal structure of podocytes disrupted by AGE were partially restored by tubacin (C), n = 3, 3 independent experiments. Overexpression of HDAC6 reduced ac‐α‐tubulin and LC3‐II accumulation. Inhibition of HDAC6 reversed the expression of ac‐α‐tubulin and LC3‐II as immunofluorescence shown (D) and summarized data (E and F), n = 4, 4 independent experiments. Representative Western blot analysis (G) and statistical graphic (H) of tubacin increased HDAC6‐induced ac‐α‐tubulin levels at Lys40 but not at Lys112 or Lys352, n = 3, 3 independent experiments. AGE, advanced glycation end products; CON, control; HDAC6, histone deacetylase 6; IP, immunoprecipitation; MFI, mean fluorescence intensity; pc‐HADC6, pcDNA3.1‐HDAC6; si‐HDAC6, siRNA of HDAC6

Techniques Used: Staining, Immunoprecipitation, Inhibition, Expressing, Over Expression, Immunofluorescence, Western Blot, Histone Deacetylase Assay, Fluorescence

HDAC6 interrupted autophagosome formation and turnover at the same time. Inhibition of HDAC6 selectively by tubacin or siRNA restored the levels of synaptopodin (green) and LC3‐II (red) in AGE‐treated podocytes as representative immunofluorescent staining shown (A), n = 3, 3 independent experiments. Overexpression of HDAC6 changed CQ‐induced LC3‐II accumulation observed by Western blotting with densitometric analysis (B‐C), n = 3, 3 independent experiments. Representative fluorescence of autophagosomes (yellow) and autolysosomes (red) (D) and the quantification of autophagosomes (E), autolysosomes (F) in podocytes treated with si‐HDAC6, tubacin or pc‐HDAC6, 3 independent experiments and 3‐4 cells for each group. AGE, advanced glycation end products; BSA, bovine serum albumin; CON, control; CQ, chloroquine; DMSO, dimethyl sulfoxide; HDAC6, histone deacetylase 6; si‐HDAC6, pc‐HADC6, pcDNA3.1‐HDAC6; si‐HDAC6, siRNA of HDAC6
Figure Legend Snippet: HDAC6 interrupted autophagosome formation and turnover at the same time. Inhibition of HDAC6 selectively by tubacin or siRNA restored the levels of synaptopodin (green) and LC3‐II (red) in AGE‐treated podocytes as representative immunofluorescent staining shown (A), n = 3, 3 independent experiments. Overexpression of HDAC6 changed CQ‐induced LC3‐II accumulation observed by Western blotting with densitometric analysis (B‐C), n = 3, 3 independent experiments. Representative fluorescence of autophagosomes (yellow) and autolysosomes (red) (D) and the quantification of autophagosomes (E), autolysosomes (F) in podocytes treated with si‐HDAC6, tubacin or pc‐HDAC6, 3 independent experiments and 3‐4 cells for each group. AGE, advanced glycation end products; BSA, bovine serum albumin; CON, control; CQ, chloroquine; DMSO, dimethyl sulfoxide; HDAC6, histone deacetylase 6; si‐HDAC6, pc‐HADC6, pcDNA3.1‐HDAC6; si‐HDAC6, siRNA of HDAC6

Techniques Used: Inhibition, Staining, Over Expression, Western Blot, Fluorescence, Histone Deacetylase Assay

8) Product Images from "FAK contributes to proteinuria in hypercholesterolaemic rats and modulates podocyte F‐actin re‐organization via activating p38 in response to ox‐ LDL"

Article Title: FAK contributes to proteinuria in hypercholesterolaemic rats and modulates podocyte F‐actin re‐organization via activating p38 in response to ox‐ LDL

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13001

Alterations of injury markers and synaptopodin expression in cultured podocytes by immunofluorescence. Immunofluorescence suggested that under normal conditions, mmp9 was weakly stained within the cell but scarcely secreted, and vimentin was moderately expressed in the podocyte cytoplasm; promoted expression and secretion of mmp9 that was seen at the inter‐surface of the cells and enhanced staining of vimentin was seen in podocytes after ox‐ LDL treatment for 24 hrs. Forced staining of vimentin and mmp9 was markedly reduced by FAK sh RNA or pre‐treatment of SB 203580. Furthermore, we showed that synaptopodin expression were up‐modulated by ox‐ LDL treatment for 24 hrs, compared with podocytes under normal culture medium, which were partially reinstated by FAK gene knockdown or p38 activation abrogation, magnification 400×.
Figure Legend Snippet: Alterations of injury markers and synaptopodin expression in cultured podocytes by immunofluorescence. Immunofluorescence suggested that under normal conditions, mmp9 was weakly stained within the cell but scarcely secreted, and vimentin was moderately expressed in the podocyte cytoplasm; promoted expression and secretion of mmp9 that was seen at the inter‐surface of the cells and enhanced staining of vimentin was seen in podocytes after ox‐ LDL treatment for 24 hrs. Forced staining of vimentin and mmp9 was markedly reduced by FAK sh RNA or pre‐treatment of SB 203580. Furthermore, we showed that synaptopodin expression were up‐modulated by ox‐ LDL treatment for 24 hrs, compared with podocytes under normal culture medium, which were partially reinstated by FAK gene knockdown or p38 activation abrogation, magnification 400×.

Techniques Used: Expressing, Cell Culture, Immunofluorescence, Staining, Activation Assay

9) Product Images from "Expression of uPAR in Urinary Podocytes of Patients with Fabry Disease"

Article Title: Expression of uPAR in Urinary Podocytes of Patients with Fabry Disease

Journal: International Journal of Nephrology

doi: 10.1155/2017/1287289

Expression of uPAR in urinary podocytes of patients with Fabry disease. (a) Synaptopodin negative cells (arrowhead). (b) uPAR negative cells (arrowhead). (c) Synaptopodin positive cells (arrowhead). (d) uPAR positive cells (white arrowhead). (e) Merge indicating the colocalization between synaptopodin and uPAR in Fabry podocytes (arrowhead). Magnification: ×200.
Figure Legend Snippet: Expression of uPAR in urinary podocytes of patients with Fabry disease. (a) Synaptopodin negative cells (arrowhead). (b) uPAR negative cells (arrowhead). (c) Synaptopodin positive cells (arrowhead). (d) uPAR positive cells (white arrowhead). (e) Merge indicating the colocalization between synaptopodin and uPAR in Fabry podocytes (arrowhead). Magnification: ×200.

Techniques Used: Expressing

10) Product Images from "Impact of klotho on the expression of SRGAP2a in podocytes in diabetic nephropathy"

Article Title: Impact of klotho on the expression of SRGAP2a in podocytes in diabetic nephropathy

Journal: BMC Nephrology

doi: 10.1186/s12882-022-02765-z

The HE staining A and Nephrin, Synaptopodin and SRGAP2a immunochemistry B of the kidneys from the modelled DN and DN plus klotho rats. Quantitative analysis of the average optical density of Nephrin C , Synaptopodin D and SRGAP2a E by immunohistochemistry. Bars = 200 μm. All data were mean ± SD, ( n = 6); * p
Figure Legend Snippet: The HE staining A and Nephrin, Synaptopodin and SRGAP2a immunochemistry B of the kidneys from the modelled DN and DN plus klotho rats. Quantitative analysis of the average optical density of Nephrin C , Synaptopodin D and SRGAP2a E by immunohistochemistry. Bars = 200 μm. All data were mean ± SD, ( n = 6); * p

Techniques Used: Staining, Immunohistochemistry

The immunofluorescence staining to label synaptopodin A and nephrin B of the cultured differentiated rat podocytes
Figure Legend Snippet: The immunofluorescence staining to label synaptopodin A and nephrin B of the cultured differentiated rat podocytes

Techniques Used: Immunofluorescence, Staining, Cell Culture

11) Product Images from "A Non-woven Path: Electrospun Poly(lactic acid) Scaffolds for Kidney Tissue Engineering"

Article Title: A Non-woven Path: Electrospun Poly(lactic acid) Scaffolds for Kidney Tissue Engineering

Journal: Tissue Engineering and Regenerative Medicine

doi: 10.1007/s13770-017-0107-5

Fluorescence images showing DAPI and IHC, used to show the presence of key functional marker of several cell types: A – D aquaporin-2, aquaporin-1 indicate the presence of tubular cells, von Willebrand factor indicates glomerular endothelial cells and synaptopodin indicated the glomerular epithelia, scale bar is 100 μm
Figure Legend Snippet: Fluorescence images showing DAPI and IHC, used to show the presence of key functional marker of several cell types: A – D aquaporin-2, aquaporin-1 indicate the presence of tubular cells, von Willebrand factor indicates glomerular endothelial cells and synaptopodin indicated the glomerular epithelia, scale bar is 100 μm

Techniques Used: Fluorescence, Immunohistochemistry, Functional Assay, Marker

12) Product Images from "Early decrease in the podocalyxin to synaptopodin ratio in urinary Fabry podocytes"

Article Title: Early decrease in the podocalyxin to synaptopodin ratio in urinary Fabry podocytes

Journal: Clinical Kidney Journal

doi: 10.1093/ckj/sfy053

( A–C ) Control podocyte. (A) Synaptopodin +; (B) podocalyxin +; (C) merged. ( D–F ) A cluster of Fabry podocytes (colocalization). (D) Synaptopodin +; (E) podocalyxin +; (F) merged. Fabry podocytes (no colocalization). ( G–I ) Fabry podocytes no colocalization: (G) Synaptopodin +; (H) podocalyxin. (I) Merging negative. Double indirect immunofluorescence. Magnification ×400.
Figure Legend Snippet: ( A–C ) Control podocyte. (A) Synaptopodin +; (B) podocalyxin +; (C) merged. ( D–F ) A cluster of Fabry podocytes (colocalization). (D) Synaptopodin +; (E) podocalyxin +; (F) merged. Fabry podocytes (no colocalization). ( G–I ) Fabry podocytes no colocalization: (G) Synaptopodin +; (H) podocalyxin. (I) Merging negative. Double indirect immunofluorescence. Magnification ×400.

Techniques Used: Immunofluorescence

13) Product Images from "Importance of neonatal immunoglobulin transfer for hippocampal development and behaviour in the newborn pig"

Article Title: Importance of neonatal immunoglobulin transfer for hippocampal development and behaviour in the newborn pig

Journal: PLoS ONE

doi: 10.1371/journal.pone.0180002

A) The left hippocampus of the piglet after dissection. Scale bar– 1.5 cm. B) Immunostaining of the subiculum of piglets. Synaptopodin- positive punctae (red) and synaptophysin- positive punctae (green). Scale bar– 100 μm. C) The density of stained regions for the synaptic proteins, synaptophysin (SPhys) and synaptopodin (SPod), in the hippocampus of piglets as analysed with immunohistochemistry. D)The colocalisation coefficients M1 and M2 of synaptophysin-positive and synaptopodin-positive puncta in the hippocampus of piglets as analysed with immunohistochemistry. Unsuckled newborn piglets (NB, n = 6) and newborn piglets fed with either an infant formula (IF, n = 6), bovine colostrum (BC, n = 6), an infant formula + i.v. infusion of sow serum (IF+IGLD, n = 6), an infant formula + i.v. infusion of porcine immunoglobulins (IF+IGHD, n = 6), or swine colostrum (SC, n = 6). Data are presented as mean±SD. Small letters given with result bars describe significant differences when p
Figure Legend Snippet: A) The left hippocampus of the piglet after dissection. Scale bar– 1.5 cm. B) Immunostaining of the subiculum of piglets. Synaptopodin- positive punctae (red) and synaptophysin- positive punctae (green). Scale bar– 100 μm. C) The density of stained regions for the synaptic proteins, synaptophysin (SPhys) and synaptopodin (SPod), in the hippocampus of piglets as analysed with immunohistochemistry. D)The colocalisation coefficients M1 and M2 of synaptophysin-positive and synaptopodin-positive puncta in the hippocampus of piglets as analysed with immunohistochemistry. Unsuckled newborn piglets (NB, n = 6) and newborn piglets fed with either an infant formula (IF, n = 6), bovine colostrum (BC, n = 6), an infant formula + i.v. infusion of sow serum (IF+IGLD, n = 6), an infant formula + i.v. infusion of porcine immunoglobulins (IF+IGHD, n = 6), or swine colostrum (SC, n = 6). Data are presented as mean±SD. Small letters given with result bars describe significant differences when p

Techniques Used: Dissection, Immunostaining, Staining, Immunohistochemistry

14) Product Images from "Curcumin attenuates angiotensin II‐induced podocyte injury and apoptosis by inhibiting endoplasmic reticulum stress"

Article Title: Curcumin attenuates angiotensin II‐induced podocyte injury and apoptosis by inhibiting endoplasmic reticulum stress

Journal: FEBS Open Bio

doi: 10.1002/2211-5463.12946

Curcumin attenuated Ang II‐induced podocyte injury in vitro . (A, B) Western blotting analysis of nephrin, podocin, and synaptopodin. Curcumin dose‐dependently reversed the decrease in the expression of nephrin, podocin, and synaptopodin induced by Ang II. (C, B) Podocin was stained using immunofluorescence, and the nuclei were counterstained using DAPI (×400). Scale bar = 50 μm. Ang II‐induced decrease in podocin was dose‐dependently attenuated by curcumin. Data are expressed as the mean ± standard deviation ( n = 3). Data were analyzed by one‐way ANOVA with Bonferroni's test for multiple comparisons (B, D). * P
Figure Legend Snippet: Curcumin attenuated Ang II‐induced podocyte injury in vitro . (A, B) Western blotting analysis of nephrin, podocin, and synaptopodin. Curcumin dose‐dependently reversed the decrease in the expression of nephrin, podocin, and synaptopodin induced by Ang II. (C, B) Podocin was stained using immunofluorescence, and the nuclei were counterstained using DAPI (×400). Scale bar = 50 μm. Ang II‐induced decrease in podocin was dose‐dependently attenuated by curcumin. Data are expressed as the mean ± standard deviation ( n = 3). Data were analyzed by one‐way ANOVA with Bonferroni's test for multiple comparisons (B, D). * P

Techniques Used: In Vitro, Western Blot, Expressing, Staining, Immunofluorescence, Standard Deviation

Curcumin decreased the Ang II‐induced podocyte injury and apoptosis by attenuating ER stress. (A, B) Western blotting analysis of ER stress‐related proteins. Tunicamycin reactivated ER stress, which was suppressed by curcumin. (C, D) Western blotting analysis of podocyte‐specific proteins. Compared with the Ang II+Cur group, the protein levels of nephrin, podocin, and synaptopodin were reduced in the Ang II+Cur+Tun group. (E, F) Western blotting analysis of apoptosis‐related proteins. Compared with the Ang II+Cur group, the protein levels of Bax, Bcl‐2, and caspase‐3 were increased in the Ang II+Cur+Tun group. Data are expressed as the mean ± standard deviation ( n = 3). Data were analyzed by one‐way ANOVA with Bonferroni's test for multiple comparisons (B, D, F). * P
Figure Legend Snippet: Curcumin decreased the Ang II‐induced podocyte injury and apoptosis by attenuating ER stress. (A, B) Western blotting analysis of ER stress‐related proteins. Tunicamycin reactivated ER stress, which was suppressed by curcumin. (C, D) Western blotting analysis of podocyte‐specific proteins. Compared with the Ang II+Cur group, the protein levels of nephrin, podocin, and synaptopodin were reduced in the Ang II+Cur+Tun group. (E, F) Western blotting analysis of apoptosis‐related proteins. Compared with the Ang II+Cur group, the protein levels of Bax, Bcl‐2, and caspase‐3 were increased in the Ang II+Cur+Tun group. Data are expressed as the mean ± standard deviation ( n = 3). Data were analyzed by one‐way ANOVA with Bonferroni's test for multiple comparisons (B, D, F). * P

Techniques Used: Western Blot, Standard Deviation

Effect of curcumin on podocyte viability and effect of Ang II on podocyte‐specific proteins and apoptosis. (A) Cell viability was determined using a CCK‐8 assay. Twenty micromolar curcumin slightly reduced the viability of podocytes. (B, C) The levels of nephrin, podocin, and synaptopodin were detected using western blotting. Ang II dose‐dependently reduced the levels of nephrin and podocin. (D, E) The levels of Bax, Bcl‐2, and caspase‐3 were detected using western blotting. Ang II dose‐dependently increased the expression of the Bax, Bcl‐2, and caspase‐3. (F, G) The effect of Ang II on cell apoptosis was detected using TUNEL staining. Scale bar = 50 μm. From 10 −8 to 10 −5 mol·L −1 , TUNEL‐positive cells were dose‐dependently increased. Data are expressed as the mean ± standard deviation ( n = 3). Data were analyzed by one‐way ANOVA with Bonferroni's test for multiple comparisons (A, C, E, G). * P
Figure Legend Snippet: Effect of curcumin on podocyte viability and effect of Ang II on podocyte‐specific proteins and apoptosis. (A) Cell viability was determined using a CCK‐8 assay. Twenty micromolar curcumin slightly reduced the viability of podocytes. (B, C) The levels of nephrin, podocin, and synaptopodin were detected using western blotting. Ang II dose‐dependently reduced the levels of nephrin and podocin. (D, E) The levels of Bax, Bcl‐2, and caspase‐3 were detected using western blotting. Ang II dose‐dependently increased the expression of the Bax, Bcl‐2, and caspase‐3. (F, G) The effect of Ang II on cell apoptosis was detected using TUNEL staining. Scale bar = 50 μm. From 10 −8 to 10 −5 mol·L −1 , TUNEL‐positive cells were dose‐dependently increased. Data are expressed as the mean ± standard deviation ( n = 3). Data were analyzed by one‐way ANOVA with Bonferroni's test for multiple comparisons (A, C, E, G). * P

Techniques Used: CCK-8 Assay, Western Blot, Expressing, TUNEL Assay, Staining, Standard Deviation

15) Product Images from "Rtn1a-Mediated Endoplasmic Reticulum Stress in Podocyte Injury and Diabetic Nephropathy"

Article Title: Rtn1a-Mediated Endoplasmic Reticulum Stress in Podocyte Injury and Diabetic Nephropathy

Journal: Scientific Reports

doi: 10.1038/s41598-017-00305-6

RTN1A expression in podocytes was highly associated with ER stress and podocyte injury in the glomeruli of diabetic mice. ( A ) Immunofluorescent staining (magnification ×400) illustrates RTN1A (green) and synaptopodin (red) co-staining in kidney sections. ( B ) Gene expressien of podocyte markers by real-time PCR analysis of glomeruli from mice in different groups ( C ) Gene expression of RTN1A and ER stress markers by real-time PCR analysis of glomeruli from mice in different groups. Values are expressed as means ± SEM. *P
Figure Legend Snippet: RTN1A expression in podocytes was highly associated with ER stress and podocyte injury in the glomeruli of diabetic mice. ( A ) Immunofluorescent staining (magnification ×400) illustrates RTN1A (green) and synaptopodin (red) co-staining in kidney sections. ( B ) Gene expressien of podocyte markers by real-time PCR analysis of glomeruli from mice in different groups ( C ) Gene expression of RTN1A and ER stress markers by real-time PCR analysis of glomeruli from mice in different groups. Values are expressed as means ± SEM. *P

Techniques Used: Expressing, Mouse Assay, Staining, Real-time Polymerase Chain Reaction

16) Product Images from "In IgA Nephropathy, Glomerulosclerosis Is Associated with Increased Urinary CD80 Excretion and Urokinase-Type Plasminogen Activator Receptor-Positive Podocyturia"

Article Title: In IgA Nephropathy, Glomerulosclerosis Is Associated with Increased Urinary CD80 Excretion and Urokinase-Type Plasminogen Activator Receptor-Positive Podocyturia

Journal: Nephron Extra

doi: 10.1159/000473888

The expression of uPAR in urinary podocytes of patients with IgAN. a Synaptopodin-negative cells (white arrow). b uPAR-negative cells (white arrow). c Synaptopodin-positive cells (white arrowhead). d uPAR-positive cells (white arrowhead). e Merged cells indicating the colocalization between synaptopodin and uPAR in IgAN podocytes. a , b ×20. c–e ×40.
Figure Legend Snippet: The expression of uPAR in urinary podocytes of patients with IgAN. a Synaptopodin-negative cells (white arrow). b uPAR-negative cells (white arrow). c Synaptopodin-positive cells (white arrowhead). d uPAR-positive cells (white arrowhead). e Merged cells indicating the colocalization between synaptopodin and uPAR in IgAN podocytes. a , b ×20. c–e ×40.

Techniques Used: Expressing

17) Product Images from "SIRT3-KLF15 signaling ameliorates kidney injury induced by hypertension"

Article Title: SIRT3-KLF15 signaling ameliorates kidney injury induced by hypertension

Journal: Oncotarget

doi: 10.18632/oncotarget.17165

SIRT3 decreases the expression of fibrosis factors in podocytes (A) Morphological changes in the podocyte foot process by electron microscopy and quantification of foot process width. Bars=0.5μm (n=6). (B) Immunofluorescence of synaptopodin (green) and WT-1(red). DAPI stained nucleus in blue. Bars=5μm (C-F) Representative Western blot analysis and quantification of SIRT3, fibronectin and collagen type IV in MPC-5 podocytes. The data are presented as the means ± SEM of three independent experiments. *P
Figure Legend Snippet: SIRT3 decreases the expression of fibrosis factors in podocytes (A) Morphological changes in the podocyte foot process by electron microscopy and quantification of foot process width. Bars=0.5μm (n=6). (B) Immunofluorescence of synaptopodin (green) and WT-1(red). DAPI stained nucleus in blue. Bars=5μm (C-F) Representative Western blot analysis and quantification of SIRT3, fibronectin and collagen type IV in MPC-5 podocytes. The data are presented as the means ± SEM of three independent experiments. *P

Techniques Used: Expressing, Electron Microscopy, Immunofluorescence, Staining, Western Blot

18) Product Images from "Epigenetic regulation of TXNIP-mediated oxidative stress and NLRP3 inflammasome activation contributes to SAHH inhibition-aggravated diabetic nephropathy"

Article Title: Epigenetic regulation of TXNIP-mediated oxidative stress and NLRP3 inflammasome activation contributes to SAHH inhibition-aggravated diabetic nephropathy

Journal: Redox Biology

doi: 10.1016/j.redox.2021.102033

Schematic shows that SAHH inhibition aggravates diabetic nephropathy via epigenetic regulation of TXNIP-mediated NLRP3 inflammasome activation.
Figure Legend Snippet: Schematic shows that SAHH inhibition aggravates diabetic nephropathy via epigenetic regulation of TXNIP-mediated NLRP3 inflammasome activation.

Techniques Used: Inhibition, Activation Assay

Knockdown of SAHH increases oxidative stress and inflammation and diabetic nephropathy . (A) The basic characteristics and plasma methionine metabolites levels of SAHH -/- and wild type mice, (B–C) Representative images and quantitation of SAHH immunofluorescence staining, PAS staining, TEM examination, WT1, F-actin, and Masson staining, (D) The levels of caspase-1 activity and IL-1β production, urine albumin and creatinine, and urinary levels of 8-OHdG was measured by commercial kits. (E) Representative images and quantitation of F-actin staining and ROS levels in podocytes treated with SAHH shRNA. (F) Protein expression of SAHH, EZH2, EGR1, TXNIP, and NLRP3 was assayed by Western blot in vitro and in vivo . Values are mean ± SEM; n = 3 for in vitro , 6–8 for in vivo assays, * P
Figure Legend Snippet: Knockdown of SAHH increases oxidative stress and inflammation and diabetic nephropathy . (A) The basic characteristics and plasma methionine metabolites levels of SAHH -/- and wild type mice, (B–C) Representative images and quantitation of SAHH immunofluorescence staining, PAS staining, TEM examination, WT1, F-actin, and Masson staining, (D) The levels of caspase-1 activity and IL-1β production, urine albumin and creatinine, and urinary levels of 8-OHdG was measured by commercial kits. (E) Representative images and quantitation of F-actin staining and ROS levels in podocytes treated with SAHH shRNA. (F) Protein expression of SAHH, EZH2, EGR1, TXNIP, and NLRP3 was assayed by Western blot in vitro and in vivo . Values are mean ± SEM; n = 3 for in vitro , 6–8 for in vivo assays, * P

Techniques Used: Mouse Assay, Quantitation Assay, Immunofluorescence, Staining, Transmission Electron Microscopy, Activity Assay, shRNA, Expressing, Western Blot, In Vitro, In Vivo

TXNIP mediated SAHH inhibition-induced NLRP3 inflammasome activation and diabetic nephropathy . (A) Urinary levels of 8-OHdG were measured by an ELISA kit. (B) Caspase-1 activity and IL-1β production in kidney tissues was measured by commercial kits. (C) Urine albumin and creatinine was measured using commercial kits. (D) Immunohistochemistry staining and quantitation analyses of NLRP3 in kidney tissues. Scale bar, 20 μm. (E) Glomerular morphological changes were detected using PAS staining. Scale bar, 20 μm. (F) Representative podocyte ultrastructure changes and quantitation of podocyte abnormalities (%) by TEM examination. Scale bar, 2 μm. (G) Representative immunofluorescence images and quantitation of WT1+ podocytes in glomeruli. Scale bar, 20 μm. Values are mean ± SEM; n = 6–8 for in vivo assays, * P
Figure Legend Snippet: TXNIP mediated SAHH inhibition-induced NLRP3 inflammasome activation and diabetic nephropathy . (A) Urinary levels of 8-OHdG were measured by an ELISA kit. (B) Caspase-1 activity and IL-1β production in kidney tissues was measured by commercial kits. (C) Urine albumin and creatinine was measured using commercial kits. (D) Immunohistochemistry staining and quantitation analyses of NLRP3 in kidney tissues. Scale bar, 20 μm. (E) Glomerular morphological changes were detected using PAS staining. Scale bar, 20 μm. (F) Representative podocyte ultrastructure changes and quantitation of podocyte abnormalities (%) by TEM examination. Scale bar, 2 μm. (G) Representative immunofluorescence images and quantitation of WT1+ podocytes in glomeruli. Scale bar, 20 μm. Values are mean ± SEM; n = 6–8 for in vivo assays, * P

Techniques Used: Inhibition, Activation Assay, Enzyme-linked Immunosorbent Assay, Activity Assay, Immunohistochemistry, Staining, Quantitation Assay, Transmission Electron Microscopy, Immunofluorescence, In Vivo

Knockdown of EGR1 alleviates SAHH inhibition-increased inflammation and diabetic nephropathy . (A) The basic characteristics of C57BL/6 mice injected with ADA in the presence or absence of tail vein injection of EGR1 shRNA, (B) Representative images and quantitation of PAS staining, TEM examination, WT1, F-actin, and Masson staining, (C) The levels of caspase-1 activity and IL-1β production in kidney tissues was measured by commercial kits. (D) Urine albumin and creatinine was measured using commercial kits. (E) Urinary levels of 8-OHdG were measured by an ELISA kit. (F) Protein expression of EGR1, TXNIP, and NLRP3 was assayed by Western blot. Values are mean ± SEM; n = 6–8, * P
Figure Legend Snippet: Knockdown of EGR1 alleviates SAHH inhibition-increased inflammation and diabetic nephropathy . (A) The basic characteristics of C57BL/6 mice injected with ADA in the presence or absence of tail vein injection of EGR1 shRNA, (B) Representative images and quantitation of PAS staining, TEM examination, WT1, F-actin, and Masson staining, (C) The levels of caspase-1 activity and IL-1β production in kidney tissues was measured by commercial kits. (D) Urine albumin and creatinine was measured using commercial kits. (E) Urinary levels of 8-OHdG were measured by an ELISA kit. (F) Protein expression of EGR1, TXNIP, and NLRP3 was assayed by Western blot. Values are mean ± SEM; n = 6–8, * P

Techniques Used: Inhibition, Mouse Assay, Injection, shRNA, Quantitation Assay, Staining, Transmission Electron Microscopy, Activity Assay, Enzyme-linked Immunosorbent Assay, Expressing, Western Blot

SAHH inhibition increases high glucose-induced podocyte injury and aggravates STZ-induced diabetic nephropathy . (A) Podocytes were incubated with HG (20 mM) or ADA (20 μmol/L) for 24 h. F-actin was stained with rhodamine–phalloidin and examined by confocal laser scanning microscopy. Scale bar, 50 μm. (B) The protein expression of Desmin and Synaptopodin were assayed by Western blot in podocytes. Values are presented as mean ± SEM; n = 3, * P
Figure Legend Snippet: SAHH inhibition increases high glucose-induced podocyte injury and aggravates STZ-induced diabetic nephropathy . (A) Podocytes were incubated with HG (20 mM) or ADA (20 μmol/L) for 24 h. F-actin was stained with rhodamine–phalloidin and examined by confocal laser scanning microscopy. Scale bar, 50 μm. (B) The protein expression of Desmin and Synaptopodin were assayed by Western blot in podocytes. Values are presented as mean ± SEM; n = 3, * P

Techniques Used: Inhibition, Incubation, Staining, Confocal Laser Scanning Microscopy, Expressing, Western Blot

SAHH inhibition increases high glucose-induced NLRP3 inflammasome activation in vitro and in vivo . (A) The protein expression of NLRP3 was assayed by Western blot in kidney tissues and podocytes. (B) Representative immunohistochemistry staining images and quantitation of NLRP3 expression in kidney tissues sections. Scale bar, 20 μm. (C) The mRNA levels of NLRP3 were measured by qRT-PCR in vivo . (D) IL-1β production and caspase-1 activity in supernatant of podocytes and kidney tissues was measured by ELISA and commercial kits. (E) The protein expression of NLRP3 was assayed by Western blot in podocytes incubated with ADA (20 μmol/L) in the presence or absence of NLRP3 siRNA for 48 h. (F) The protein expression of densmin and synaptopodin were assayed by Western blot in podocytes incubated with ADA (20 μmol/L) in the presence or absence of NLRP3 siRNA or caspase-1 inhibitor (Z-YVAD) for 48 h. (G) F-actin was stained with rhodamine–phalloidin and examined by confocal laser scanning microscopy. Scale bar, 50 μm. Values are presented as mean ± SEM; n = 3, for in vitro assays and n = 6–8 for in vivo assays, * P
Figure Legend Snippet: SAHH inhibition increases high glucose-induced NLRP3 inflammasome activation in vitro and in vivo . (A) The protein expression of NLRP3 was assayed by Western blot in kidney tissues and podocytes. (B) Representative immunohistochemistry staining images and quantitation of NLRP3 expression in kidney tissues sections. Scale bar, 20 μm. (C) The mRNA levels of NLRP3 were measured by qRT-PCR in vivo . (D) IL-1β production and caspase-1 activity in supernatant of podocytes and kidney tissues was measured by ELISA and commercial kits. (E) The protein expression of NLRP3 was assayed by Western blot in podocytes incubated with ADA (20 μmol/L) in the presence or absence of NLRP3 siRNA for 48 h. (F) The protein expression of densmin and synaptopodin were assayed by Western blot in podocytes incubated with ADA (20 μmol/L) in the presence or absence of NLRP3 siRNA or caspase-1 inhibitor (Z-YVAD) for 48 h. (G) F-actin was stained with rhodamine–phalloidin and examined by confocal laser scanning microscopy. Scale bar, 50 μm. Values are presented as mean ± SEM; n = 3, for in vitro assays and n = 6–8 for in vivo assays, * P

Techniques Used: Inhibition, Activation Assay, In Vitro, In Vivo, Expressing, Western Blot, Immunohistochemistry, Staining, Quantitation Assay, Quantitative RT-PCR, Activity Assay, Enzyme-linked Immunosorbent Assay, Incubation, Confocal Laser Scanning Microscopy

SAHH inhibition induced TXNIP expression and increased oxidative stress in vivo and in vitro . (A) Protein expression of TXNIP was assayed by Western blot in vivo and in vitro . (B) Immunohistochemistry staining and quantitation analyses of TXNIP expression in kidney tissues. Scale bar, 20 μm. (C) The mRNA levels of TXNIP were measured by quantitative RT-PCR. (D) Intracellular ROS production was measured by DCF staining and examined using a fluorescence microscope. Scale bar, 50 μm. (E) Urinary levels of oxidative stress marker 8-hydroxy-2′-deoxyguanosine (8-OHdG) were measured by an ELISA kit according to the manufacturer's protocol. (F) Protein expression of TXNIP was assayed by Western blot in podocytes incubated with TXNIP siRNA transfection. (G) Intracellular ROS production was measured by DCF staining and examined using a fluorescence microscope. Scale bar, 50 μm. (H) Caspase-1 activity and IL-1β production in supernatant was measured by commercial kits. (I) The protein expression of NLRP3 was assayed by Western blot in podocytes. Values are mean ± SEM; n = 3 for in vitro assays and n = 6–8 for in vivo assays, * P
Figure Legend Snippet: SAHH inhibition induced TXNIP expression and increased oxidative stress in vivo and in vitro . (A) Protein expression of TXNIP was assayed by Western blot in vivo and in vitro . (B) Immunohistochemistry staining and quantitation analyses of TXNIP expression in kidney tissues. Scale bar, 20 μm. (C) The mRNA levels of TXNIP were measured by quantitative RT-PCR. (D) Intracellular ROS production was measured by DCF staining and examined using a fluorescence microscope. Scale bar, 50 μm. (E) Urinary levels of oxidative stress marker 8-hydroxy-2′-deoxyguanosine (8-OHdG) were measured by an ELISA kit according to the manufacturer's protocol. (F) Protein expression of TXNIP was assayed by Western blot in podocytes incubated with TXNIP siRNA transfection. (G) Intracellular ROS production was measured by DCF staining and examined using a fluorescence microscope. Scale bar, 50 μm. (H) Caspase-1 activity and IL-1β production in supernatant was measured by commercial kits. (I) The protein expression of NLRP3 was assayed by Western blot in podocytes. Values are mean ± SEM; n = 3 for in vitro assays and n = 6–8 for in vivo assays, * P

Techniques Used: Inhibition, Expressing, In Vivo, In Vitro, Western Blot, Immunohistochemistry, Staining, Quantitation Assay, Quantitative RT-PCR, Fluorescence, Microscopy, Marker, Enzyme-linked Immunosorbent Assay, Incubation, Transfection, Activity Assay

Knockout of NLRP3 attenuates SAHH inhibition-aggravated diabetic nephropathy . (A – B) Urine albumin and creatinine was measured using commercial kits. (C) IL-1β production and caspase-1 activity in kidney tissues was measured by commercial kits. (D) Glomerular morphological changes and quantitation were detected using PAS staining. Scale bar, 20 μm. (E) Representative podocyte ultrastructure changes and quantitation of podocyte abnormalities (%) by TEM examination. Scale bar, 2 μm. (F) Representative immunofluorescence images and quantitation of WT1+ podocytes in glomeruli. Scale bar, 20 μm. Results are mean ± SEM; n = 6–8, * P
Figure Legend Snippet: Knockout of NLRP3 attenuates SAHH inhibition-aggravated diabetic nephropathy . (A – B) Urine albumin and creatinine was measured using commercial kits. (C) IL-1β production and caspase-1 activity in kidney tissues was measured by commercial kits. (D) Glomerular morphological changes and quantitation were detected using PAS staining. Scale bar, 20 μm. (E) Representative podocyte ultrastructure changes and quantitation of podocyte abnormalities (%) by TEM examination. Scale bar, 2 μm. (F) Representative immunofluorescence images and quantitation of WT1+ podocytes in glomeruli. Scale bar, 20 μm. Results are mean ± SEM; n = 6–8, * P

Techniques Used: Knock-Out, Inhibition, Activity Assay, Quantitation Assay, Staining, Transmission Electron Microscopy, Immunofluorescence

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    Abcam anti synaptopodin antibody
    Glucose promoted podocyte proliferation in a marked time- and dose-dependent manner. (A) Podocytes were cultured at 37°C for 12, 24 and 48 h. The <t>synaptopodin</t> expression was detected using immunofluorescence assay. The cells were visualized under fluorescence microscopy. Blue and red fluorescence represents the nucleus and synaptopodin, respectively. (B) MTT assay was performed to measure the proliferation of podocytes treated with PBS and glucose at 0, 5, 10, 20, 40, 60, 80 and100 mM for 6, 12, 24 and 48 h. OD, optical density; A, absorbance.
    Anti Synaptopodin Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Abcam mouse monoclonal anti synaptopodin primary antibody
    Letrozole and Aβ 1–42 reduce synaptic proteins. (a) Representative 3D reconstructions of dendritic segments from sister cultures that were treated with either control, Aβ 1–42 (1 μ M), and letrozole (1 μ m) or Aβ 1–42 + letrozole (1 μ m) for 24 or 72 hours and immunostained for synaptophysin (white) and <t>synaptopodin</t> (red). Scale bar, 2 μ m. (b) Quantification of the densities of synaptopodin-positive puncta following treatments. There is a significant decrease in synaptopodin puncta after 24 and 72 hours of Aβ 1–42 , letrozole or Aβ 1–42 + letrozole treatments compared to control conditions. After 72 hours, the number of synaptopodin puncta was significantly lower in letrozole and Aβ 1–42 + letrozole-treated cultures compared to Aβ 1–42 alone. When synaptopodin puncta densities were compared between 24- and 72-hour treated cultures there was a significant decrease only in letrozole and Aβ 1–42 + letrozole-treated cultures after 72 hours. 24 hours: control, n = total dendritic segment lengths of 1041 μ m from 12 cells in 4 cultures; Aβ 1–42 , n = 633 μ m of dendrite from 8 cells in 4 cultures; letrozole, n = 952 μ m of dendrite from 10 cells in 4 cultures; Aβ 1–42 + letrozole, n = 1007 μ m of dendrite from 10 cells in 4 cultures. 72 hours: control, n = total dendritic segment lengths of 559 μ m from 10 cells in 3 cultures; Aβ 1–42 , n = 472 μ m of dendrite from 9 cells in 4 cultures; letrozole, n = 838 μ m of dendrite from 9 cells in 4 cultures; Aβ 1–42 + letrozole, n = 750 μ m of dendrite from 8 cells in 4 cultures. There is a significant decrease in synaptophysin puncta after 24 and 72 hours of Aβ 1–42 , letrozole, or Aβ 1–42 + letrozole treatments compared to control conditions. After 72 hours, the number of synaptophysin puncta was significantly lower in letrozole and Aβ 1–42 + letrozole-treated cultures compared to Aβ 1–42 alone When synaptophysin puncta densities were compared between 24- and 72-hour treated cultures there was a significant decrease in Aβ 1–42 , letrozole, and Aβ 1–42 + letrozole-treated cultures after 72 hours. 24 hours: control, n = total dendritic segment lengths of 1041 μ m from 12 cells in 4 cultures; Aβ 1–42 , n = 633 μ m of dendrite from 8 cells in 4 cultures; letrozole, n = 952 μ m of dendrite from 10 cells in 4 cultures; Aβ 1–42 + letrozole, n = 1007 μ m of dendrite from 10 cells in 4 cultures. 72 hours: control, n = total dendritic segment lengths of 559 μ m from 10 cells in 3 cultures; Aβ 1–42 , n = 472 μ m of dendrite from 9 cells in 4 cultures; letrozole, n = 838 μ m of dendrite from 9 cells in 4 cultures; Aβ 1–42 + letrozole, n = 750 μ m of dendrite from 8 cells in 4 cultures.
    Mouse Monoclonal Anti Synaptopodin Primary Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam synaptopodin antibodies
    Effects of quercetin on HG-induced podocyte injury through the EGFR pathway. (A , B , G , H) Distribution and expression of <t>synaptopodin</t> and nephrin in podocyte through immunofluorescence. (C , D , I , J) Statistical analysis of synaptopodin, nephrin expression. (E , K) Expression of synaptopodin through western blotting. (F , L) Statistical analysis of synaptopodin protein expression. Cells were starved for 24 h and treated with normal glucose, high glucose, DMSO, quercetin, AG1478 or Q40 + AG1478 for 24 h. Data were expressed as mean ± SEM, n = 3. ## p
    Synaptopodin Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Abcam anti synpo
    Two-step immunoblot analysis of selected proteins. a Representative immunoblots from the pooled lysates showing the protein levels of Control, DLB, PDD and the combined ‘Dementias’ group, with GAPDH used as the loading control. b Bar chart of immunoreactivities (mean ± SEM in arbitrary units) for comparing protein expression levels (with mean control values set at 1.0). Dotted lines were drawn at ± 1.3-fold to indicate the threshold of deregulation as determined from the iTRAQ experiment. The data shows upward trends for GSTP1, PLP1 and downward trends for <t>SYNPO</t> and VIM while <t>NCAM</t> did not exhibit any change between different groups. c Representative immunoblots of selected proteins using individual subjects. Control (C), PDD (P) and DLB (D) subjects selected randomly from each group for different proteins. GAPDH was used as the loading control. d Bar chart of normalized immuno-reactivities (mean ± SEM in arbitrary units) of the proteins of interest was calculated from all subjects (21 Controls, 19 DLB, 21 PDD) selected for the iTRAQ experiment. Significant difference (one-way ANOVA followed by post-hoc Bonferroni tests) * p
    Anti Synpo, supplied by Abcam, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Glucose promoted podocyte proliferation in a marked time- and dose-dependent manner. (A) Podocytes were cultured at 37°C for 12, 24 and 48 h. The synaptopodin expression was detected using immunofluorescence assay. The cells were visualized under fluorescence microscopy. Blue and red fluorescence represents the nucleus and synaptopodin, respectively. (B) MTT assay was performed to measure the proliferation of podocytes treated with PBS and glucose at 0, 5, 10, 20, 40, 60, 80 and100 mM for 6, 12, 24 and 48 h. OD, optical density; A, absorbance.

    Journal: Experimental and Therapeutic Medicine

    Article Title: Silence of IGFBP7 suppresses apoptosis and epithelial mesenchymal transformation of high glucose induced-podocytes

    doi: 10.3892/etm.2018.6298

    Figure Lengend Snippet: Glucose promoted podocyte proliferation in a marked time- and dose-dependent manner. (A) Podocytes were cultured at 37°C for 12, 24 and 48 h. The synaptopodin expression was detected using immunofluorescence assay. The cells were visualized under fluorescence microscopy. Blue and red fluorescence represents the nucleus and synaptopodin, respectively. (B) MTT assay was performed to measure the proliferation of podocytes treated with PBS and glucose at 0, 5, 10, 20, 40, 60, 80 and100 mM for 6, 12, 24 and 48 h. OD, optical density; A, absorbance.

    Article Snippet: The anti-synaptopodin antibody (1:600; cat. no. ab220345; Abcam) was used to incubate with the cells overnight at 4°C.

    Techniques: Cell Culture, Expressing, Immunofluorescence, Fluorescence, Microscopy, MTT Assay

    Letrozole and Aβ 1–42 reduce synaptic proteins. (a) Representative 3D reconstructions of dendritic segments from sister cultures that were treated with either control, Aβ 1–42 (1 μ M), and letrozole (1 μ m) or Aβ 1–42 + letrozole (1 μ m) for 24 or 72 hours and immunostained for synaptophysin (white) and synaptopodin (red). Scale bar, 2 μ m. (b) Quantification of the densities of synaptopodin-positive puncta following treatments. There is a significant decrease in synaptopodin puncta after 24 and 72 hours of Aβ 1–42 , letrozole or Aβ 1–42 + letrozole treatments compared to control conditions. After 72 hours, the number of synaptopodin puncta was significantly lower in letrozole and Aβ 1–42 + letrozole-treated cultures compared to Aβ 1–42 alone. When synaptopodin puncta densities were compared between 24- and 72-hour treated cultures there was a significant decrease only in letrozole and Aβ 1–42 + letrozole-treated cultures after 72 hours. 24 hours: control, n = total dendritic segment lengths of 1041 μ m from 12 cells in 4 cultures; Aβ 1–42 , n = 633 μ m of dendrite from 8 cells in 4 cultures; letrozole, n = 952 μ m of dendrite from 10 cells in 4 cultures; Aβ 1–42 + letrozole, n = 1007 μ m of dendrite from 10 cells in 4 cultures. 72 hours: control, n = total dendritic segment lengths of 559 μ m from 10 cells in 3 cultures; Aβ 1–42 , n = 472 μ m of dendrite from 9 cells in 4 cultures; letrozole, n = 838 μ m of dendrite from 9 cells in 4 cultures; Aβ 1–42 + letrozole, n = 750 μ m of dendrite from 8 cells in 4 cultures. There is a significant decrease in synaptophysin puncta after 24 and 72 hours of Aβ 1–42 , letrozole, or Aβ 1–42 + letrozole treatments compared to control conditions. After 72 hours, the number of synaptophysin puncta was significantly lower in letrozole and Aβ 1–42 + letrozole-treated cultures compared to Aβ 1–42 alone When synaptophysin puncta densities were compared between 24- and 72-hour treated cultures there was a significant decrease in Aβ 1–42 , letrozole, and Aβ 1–42 + letrozole-treated cultures after 72 hours. 24 hours: control, n = total dendritic segment lengths of 1041 μ m from 12 cells in 4 cultures; Aβ 1–42 , n = 633 μ m of dendrite from 8 cells in 4 cultures; letrozole, n = 952 μ m of dendrite from 10 cells in 4 cultures; Aβ 1–42 + letrozole, n = 1007 μ m of dendrite from 10 cells in 4 cultures. 72 hours: control, n = total dendritic segment lengths of 559 μ m from 10 cells in 3 cultures; Aβ 1–42 , n = 472 μ m of dendrite from 9 cells in 4 cultures; letrozole, n = 838 μ m of dendrite from 9 cells in 4 cultures; Aβ 1–42 + letrozole, n = 750 μ m of dendrite from 8 cells in 4 cultures.

    Journal: Journal of Aging Research

    Article Title: Letrozole Potentiates Mitochondrial and Dendritic Spine Impairments Induced by β Amyloid

    doi: 10.1155/2013/538979

    Figure Lengend Snippet: Letrozole and Aβ 1–42 reduce synaptic proteins. (a) Representative 3D reconstructions of dendritic segments from sister cultures that were treated with either control, Aβ 1–42 (1 μ M), and letrozole (1 μ m) or Aβ 1–42 + letrozole (1 μ m) for 24 or 72 hours and immunostained for synaptophysin (white) and synaptopodin (red). Scale bar, 2 μ m. (b) Quantification of the densities of synaptopodin-positive puncta following treatments. There is a significant decrease in synaptopodin puncta after 24 and 72 hours of Aβ 1–42 , letrozole or Aβ 1–42 + letrozole treatments compared to control conditions. After 72 hours, the number of synaptopodin puncta was significantly lower in letrozole and Aβ 1–42 + letrozole-treated cultures compared to Aβ 1–42 alone. When synaptopodin puncta densities were compared between 24- and 72-hour treated cultures there was a significant decrease only in letrozole and Aβ 1–42 + letrozole-treated cultures after 72 hours. 24 hours: control, n = total dendritic segment lengths of 1041 μ m from 12 cells in 4 cultures; Aβ 1–42 , n = 633 μ m of dendrite from 8 cells in 4 cultures; letrozole, n = 952 μ m of dendrite from 10 cells in 4 cultures; Aβ 1–42 + letrozole, n = 1007 μ m of dendrite from 10 cells in 4 cultures. 72 hours: control, n = total dendritic segment lengths of 559 μ m from 10 cells in 3 cultures; Aβ 1–42 , n = 472 μ m of dendrite from 9 cells in 4 cultures; letrozole, n = 838 μ m of dendrite from 9 cells in 4 cultures; Aβ 1–42 + letrozole, n = 750 μ m of dendrite from 8 cells in 4 cultures. There is a significant decrease in synaptophysin puncta after 24 and 72 hours of Aβ 1–42 , letrozole, or Aβ 1–42 + letrozole treatments compared to control conditions. After 72 hours, the number of synaptophysin puncta was significantly lower in letrozole and Aβ 1–42 + letrozole-treated cultures compared to Aβ 1–42 alone When synaptophysin puncta densities were compared between 24- and 72-hour treated cultures there was a significant decrease in Aβ 1–42 , letrozole, and Aβ 1–42 + letrozole-treated cultures after 72 hours. 24 hours: control, n = total dendritic segment lengths of 1041 μ m from 12 cells in 4 cultures; Aβ 1–42 , n = 633 μ m of dendrite from 8 cells in 4 cultures; letrozole, n = 952 μ m of dendrite from 10 cells in 4 cultures; Aβ 1–42 + letrozole, n = 1007 μ m of dendrite from 10 cells in 4 cultures. 72 hours: control, n = total dendritic segment lengths of 559 μ m from 10 cells in 3 cultures; Aβ 1–42 , n = 472 μ m of dendrite from 9 cells in 4 cultures; letrozole, n = 838 μ m of dendrite from 9 cells in 4 cultures; Aβ 1–42 + letrozole, n = 750 μ m of dendrite from 8 cells in 4 cultures.

    Article Snippet: Rabbit monoclonal anti-synaptophysin primary antibody was used at 1 : 400 dilution (Zymed, CA, USA) and mouse monoclonal anti-synaptopodin primary antibody was used at 1 : 400 dilution (Abcam, MA, USA), as well.

    Techniques:

    Effects of quercetin on HG-induced podocyte injury through the EGFR pathway. (A , B , G , H) Distribution and expression of synaptopodin and nephrin in podocyte through immunofluorescence. (C , D , I , J) Statistical analysis of synaptopodin, nephrin expression. (E , K) Expression of synaptopodin through western blotting. (F , L) Statistical analysis of synaptopodin protein expression. Cells were starved for 24 h and treated with normal glucose, high glucose, DMSO, quercetin, AG1478 or Q40 + AG1478 for 24 h. Data were expressed as mean ± SEM, n = 3. ## p

    Journal: Frontiers in Pharmacology

    Article Title: Quercetin Attenuates Podocyte Apoptosis of Diabetic Nephropathy Through Targeting EGFR Signaling

    doi: 10.3389/fphar.2021.792777

    Figure Lengend Snippet: Effects of quercetin on HG-induced podocyte injury through the EGFR pathway. (A , B , G , H) Distribution and expression of synaptopodin and nephrin in podocyte through immunofluorescence. (C , D , I , J) Statistical analysis of synaptopodin, nephrin expression. (E , K) Expression of synaptopodin through western blotting. (F , L) Statistical analysis of synaptopodin protein expression. Cells were starved for 24 h and treated with normal glucose, high glucose, DMSO, quercetin, AG1478 or Q40 + AG1478 for 24 h. Data were expressed as mean ± SEM, n = 3. ## p

    Article Snippet: ERK1/2, p-ERK1/2, Bcl2, Bax and synaptopodin antibodies were purchased from Abcam (Cambridge, United Kingdom). β-actin antibody was purchased from Santa Cruz Biotechnology (Santa Cruz, CA, United States).

    Techniques: Expressing, Immunofluorescence, Western Blot

    Two-step immunoblot analysis of selected proteins. a Representative immunoblots from the pooled lysates showing the protein levels of Control, DLB, PDD and the combined ‘Dementias’ group, with GAPDH used as the loading control. b Bar chart of immunoreactivities (mean ± SEM in arbitrary units) for comparing protein expression levels (with mean control values set at 1.0). Dotted lines were drawn at ± 1.3-fold to indicate the threshold of deregulation as determined from the iTRAQ experiment. The data shows upward trends for GSTP1, PLP1 and downward trends for SYNPO and VIM while NCAM did not exhibit any change between different groups. c Representative immunoblots of selected proteins using individual subjects. Control (C), PDD (P) and DLB (D) subjects selected randomly from each group for different proteins. GAPDH was used as the loading control. d Bar chart of normalized immuno-reactivities (mean ± SEM in arbitrary units) of the proteins of interest was calculated from all subjects (21 Controls, 19 DLB, 21 PDD) selected for the iTRAQ experiment. Significant difference (one-way ANOVA followed by post-hoc Bonferroni tests) * p

    Journal: Molecular Brain

    Article Title: An iTRAQ-based proteomic analysis reveals dysregulation of neocortical synaptopodin in Lewy body dementias

    doi: 10.1186/s13041-017-0316-9

    Figure Lengend Snippet: Two-step immunoblot analysis of selected proteins. a Representative immunoblots from the pooled lysates showing the protein levels of Control, DLB, PDD and the combined ‘Dementias’ group, with GAPDH used as the loading control. b Bar chart of immunoreactivities (mean ± SEM in arbitrary units) for comparing protein expression levels (with mean control values set at 1.0). Dotted lines were drawn at ± 1.3-fold to indicate the threshold of deregulation as determined from the iTRAQ experiment. The data shows upward trends for GSTP1, PLP1 and downward trends for SYNPO and VIM while NCAM did not exhibit any change between different groups. c Representative immunoblots of selected proteins using individual subjects. Control (C), PDD (P) and DLB (D) subjects selected randomly from each group for different proteins. GAPDH was used as the loading control. d Bar chart of normalized immuno-reactivities (mean ± SEM in arbitrary units) of the proteins of interest was calculated from all subjects (21 Controls, 19 DLB, 21 PDD) selected for the iTRAQ experiment. Significant difference (one-way ANOVA followed by post-hoc Bonferroni tests) * p

    Article Snippet: Immunoblotting Immunoblotting was performed after 10% or 12% SDS-PAGE by probing with primary antibodies at the indicated dilutions: anti-GAPDH (1: 1000, mouse monoclonal; Milipore, Billerica, MA, USA), anti-COL6A3 (1:200, mouse monoclonal; Santa Cruz Biotech, Santa Cruz, CA, USA), anti-GSTP1 (1:1000, rabbit polyclonal; Abcam, Cambridge, UK), anti-FLNA (1:1000; rabbit polyclonal; Cell Signaling Technology, Danvers, MA, USA), anti-NCAM (1:10,000, rabbit polyclonal; Santa Cruz Biotech), anti-PLP1 (1:1000, rabbit polyclonal; Abcam), anti-SYNPO (1:500, rabbit polyclonal; Abcam), anti-VIM (1:1000, rabbit polyclonal; Genscript, Piscataway, NJ, USA).

    Techniques: Western Blot, Expressing