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Human Protein Atlas prmt5 protein expression
DNA and RNA nucleotide sequences
Prmt5 Protein Expression, supplied by Human Protein Atlas, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "PRMT5 promotes epithelial‐mesenchymal transition via EGFR‐β‐catenin axis in pancreatic cancer cells"

Article Title: PRMT5 promotes epithelial‐mesenchymal transition via EGFR‐β‐catenin axis in pancreatic cancer cells

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.14894

DNA and RNA nucleotide sequences
Figure Legend Snippet: DNA and RNA nucleotide sequences

Techniques Used:

PRMT5 is profiled in pancreatic cancers and different pancreatic cancer cells. A, PRMT5 protein expression in pancreatic cancer tissues and normal pancreatic tissues was analysed through the human protein atlas ( http://www.proteinatlas.org ). Magnification, ×4; bars, 500 μm. Magnification, ×40; bars, 100 μm. B, Analysis of PRMT5 mRNA levels in 39 pairs of pancreatic cancer and non‐tumour tissues in Badea pancreas database. N = 39 for non‐tumour group, and N = 39 for tumour group. *** P < .001. C, Analysis of the TCGA database indicates that PRMT5 expression is correlated with patient’ overall survival. N = 32 for PRMT5‐low group, and N = 50 for PRMT5‐high group. P = .0345 was determined by log‐rank test. D, Analysis of the TCGA database indicates PRMT5 correlates with clinicopathological features. The results are presented by heat map (left panel) and box plot (right panel). N = 139 for pancreas adenocarcinoma ductal type group, N = 23 for pancreas adenocarcinoma other subtype group, and N = 4 for pancreas colloid (mucinous non‐cystic) carcinoma group. P = .0707 (E) Analysis of the TCGA database indicates PRMT5 is associated with stage in pancreatic cancer. The results are presented by heat map (left panel) and box plot (right panel). N = 20 for stage I group, N = 147 for stage II + III + IV group. * P < .05
Figure Legend Snippet: PRMT5 is profiled in pancreatic cancers and different pancreatic cancer cells. A, PRMT5 protein expression in pancreatic cancer tissues and normal pancreatic tissues was analysed through the human protein atlas ( http://www.proteinatlas.org ). Magnification, ×4; bars, 500 μm. Magnification, ×40; bars, 100 μm. B, Analysis of PRMT5 mRNA levels in 39 pairs of pancreatic cancer and non‐tumour tissues in Badea pancreas database. N = 39 for non‐tumour group, and N = 39 for tumour group. *** P < .001. C, Analysis of the TCGA database indicates that PRMT5 expression is correlated with patient’ overall survival. N = 32 for PRMT5‐low group, and N = 50 for PRMT5‐high group. P = .0345 was determined by log‐rank test. D, Analysis of the TCGA database indicates PRMT5 correlates with clinicopathological features. The results are presented by heat map (left panel) and box plot (right panel). N = 139 for pancreas adenocarcinoma ductal type group, N = 23 for pancreas adenocarcinoma other subtype group, and N = 4 for pancreas colloid (mucinous non‐cystic) carcinoma group. P = .0707 (E) Analysis of the TCGA database indicates PRMT5 is associated with stage in pancreatic cancer. The results are presented by heat map (left panel) and box plot (right panel). N = 20 for stage I group, N = 147 for stage II + III + IV group. * P < .05

Techniques Used: Expressing

PRMT5 promotes cell proliferation in pancreatic cancer cells and tumorigenesis. A‐B, CCK‐8 assay showed that PRMT5 knockdown inhibited PaTu8988 and SW1990 cell growth rate (Student's t test:* P < .05). C‐D, Clone formation assays in PaTu8988 and SW1990 cells. PRMT5 knockdown inhibited cell clone formation (Student's t test:* P < .05). The number of clones with at least 50 cells per colony and strong, high dense staining was counted. The rates of colony formation were 48.33% and 17.67% in sh‐EGFP and sh‐PRMT5 PaTu8988 cells, and 35.67% and 10.67% in sh‐EGFP and sh‐PRMT5 SW1990 cells, respectively. E‐F, PaTu8988 cells with PRMT5 down‐regulation were injected (2.0 × 10 6 cells/site) subcutaneously into a mice, and the tumour volume was measured weekly (n = 5 mice). * P < .05. G‐H, CCK‐8 assay showed that ectopic PRMT5 re‐expression in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells promoted cell proliferation rate (Student's t test: * P < .05). I‐J, Clone formation assays in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. Ectopic PRMT5 re‐expression in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells promoted cell clone formation (Student's t test: *** P < .001). The rates of number of colonies (defined as ≥50 cells) were 25.33% and 56.67% in PaTu8988 cells, 18.67% and 58.33% in SW1990 cells, respectively. K‐L, SW1990 cells with PRMT5 up‐regulation were injected (2.0 × 10 6 cells/site) subcutaneously into a mice, and the tumour volume was measured weekly (n = 5 mice), * P < .05
Figure Legend Snippet: PRMT5 promotes cell proliferation in pancreatic cancer cells and tumorigenesis. A‐B, CCK‐8 assay showed that PRMT5 knockdown inhibited PaTu8988 and SW1990 cell growth rate (Student's t test:* P < .05). C‐D, Clone formation assays in PaTu8988 and SW1990 cells. PRMT5 knockdown inhibited cell clone formation (Student's t test:* P < .05). The number of clones with at least 50 cells per colony and strong, high dense staining was counted. The rates of colony formation were 48.33% and 17.67% in sh‐EGFP and sh‐PRMT5 PaTu8988 cells, and 35.67% and 10.67% in sh‐EGFP and sh‐PRMT5 SW1990 cells, respectively. E‐F, PaTu8988 cells with PRMT5 down‐regulation were injected (2.0 × 10 6 cells/site) subcutaneously into a mice, and the tumour volume was measured weekly (n = 5 mice). * P < .05. G‐H, CCK‐8 assay showed that ectopic PRMT5 re‐expression in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells promoted cell proliferation rate (Student's t test: * P < .05). I‐J, Clone formation assays in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. Ectopic PRMT5 re‐expression in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells promoted cell clone formation (Student's t test: *** P < .001). The rates of number of colonies (defined as ≥50 cells) were 25.33% and 56.67% in PaTu8988 cells, 18.67% and 58.33% in SW1990 cells, respectively. K‐L, SW1990 cells with PRMT5 up‐regulation were injected (2.0 × 10 6 cells/site) subcutaneously into a mice, and the tumour volume was measured weekly (n = 5 mice), * P < .05

Techniques Used: CCK-8 Assay, Knockdown, Clone Assay, Staining, Injection, Expressing, Infection

PRMT5 promotes cell migration and invasion in pancreatic cancer cells. A‐B, The migration changes were measured by transwell assay in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells (Student's t test: ** P < .01, *** P < .001). C‐D, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the migration changes were measured by transwell assay (Student's t test: ** P < .01). E‐F, The invasion changes were measured by transwell assay in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells (Student's t test: *** P < .001). The number of cells passing through the reconstituted basement membrane was 363.13 ± 26.25 and 152.54 ± 9.13 in sh‐EGFP and sh‐PRMT5 PaTu8988 cells, and 204.38 ± 18.38 and 89.54 ± 6.75 in sh‐EGFP and sh‐PRMT5 SW1990 cells, respectively. G‐H, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the invasion changes were measured by transwell assay (Student's t test: ** P < .01). Numbers of cells passing through the reconstituted basement membrane were 212.33 ± 12.54 and 403.13 ± 35.42 in PaTu8988 cells, 132.04 ± 8.29 and 212.21 ± 16.46 in SW1990 cells, respectively. I‐J, The protein levels of MMP2 and MMP9 were measured by Western blot
Figure Legend Snippet: PRMT5 promotes cell migration and invasion in pancreatic cancer cells. A‐B, The migration changes were measured by transwell assay in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells (Student's t test: ** P < .01, *** P < .001). C‐D, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the migration changes were measured by transwell assay (Student's t test: ** P < .01). E‐F, The invasion changes were measured by transwell assay in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells (Student's t test: *** P < .001). The number of cells passing through the reconstituted basement membrane was 363.13 ± 26.25 and 152.54 ± 9.13 in sh‐EGFP and sh‐PRMT5 PaTu8988 cells, and 204.38 ± 18.38 and 89.54 ± 6.75 in sh‐EGFP and sh‐PRMT5 SW1990 cells, respectively. G‐H, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the invasion changes were measured by transwell assay (Student's t test: ** P < .01). Numbers of cells passing through the reconstituted basement membrane were 212.33 ± 12.54 and 403.13 ± 35.42 in PaTu8988 cells, 132.04 ± 8.29 and 212.21 ± 16.46 in SW1990 cells, respectively. I‐J, The protein levels of MMP2 and MMP9 were measured by Western blot

Techniques Used: Migration, Transwell Assay, Infection, Transfection, Plasmid Preparation, Membrane, Western Blot

PRMT5 promotes EMT in pancreatic cancer cells. A, The protein levels of E‐cadherin, collagen I, β‐catenin and Vimentin were measured by Western blot in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. B, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the protein levels of E‐cadherin, collagen I, β‐catenin and Vimentin were measured by Western blot. C‐D, Vimentin, β‐catenin and Collagen I mRNA levels were reduced while E‐cadherin mRNA level was increased in shPRMT5‐PaTu8988 and SW1990 cells. * P < .05, ** P < .01, *** P < .001. E‐F, Vimentin, β‐catenin and Collagen I mRNA levels were increased while E‐cadherin mRNA level was reduced in sh‐PRMT5 PaTu8988 and SW1990 cells transfected with pHA‐PRMT5 plasmid. * P < .05, ** P < .01, *** P < .001
Figure Legend Snippet: PRMT5 promotes EMT in pancreatic cancer cells. A, The protein levels of E‐cadherin, collagen I, β‐catenin and Vimentin were measured by Western blot in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. B, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the protein levels of E‐cadherin, collagen I, β‐catenin and Vimentin were measured by Western blot. C‐D, Vimentin, β‐catenin and Collagen I mRNA levels were reduced while E‐cadherin mRNA level was increased in shPRMT5‐PaTu8988 and SW1990 cells. * P < .05, ** P < .01, *** P < .001. E‐F, Vimentin, β‐catenin and Collagen I mRNA levels were increased while E‐cadherin mRNA level was reduced in sh‐PRMT5 PaTu8988 and SW1990 cells transfected with pHA‐PRMT5 plasmid. * P < .05, ** P < .01, *** P < .001

Techniques Used: Western Blot, Infection, Transfection, Plasmid Preparation

PRMT5 activates EGFR/AKT/β‐catenin signalling in pancreatic cancer cells. A, Wnt/β‐catenin and EGFR signalling relative proteins were detected by Western blot in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. B, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, EGFR/AKT/β‐catenin signalling relative proteins were detected by Western blot. C, Pancreatic cancer cells were treated with EGFR inhibitor at 0, 10 μmol/L for 3 d. The expression of EGFR, p‐EGFR (Y1068) and PRMT5 was determined by Western blotting. D, The quantification of EGFR and p‐EGFR is shown. ** P < .01, *** P < .001. E, Wnt/β‐catenin and EGFR signalling relative proteins were detected by Western blot in PaTu8988 and SW1990 pHA‐PRMT5 stable infected cells treated with Erlotinib (10 μmol/L) for 3 d
Figure Legend Snippet: PRMT5 activates EGFR/AKT/β‐catenin signalling in pancreatic cancer cells. A, Wnt/β‐catenin and EGFR signalling relative proteins were detected by Western blot in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. B, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, EGFR/AKT/β‐catenin signalling relative proteins were detected by Western blot. C, Pancreatic cancer cells were treated with EGFR inhibitor at 0, 10 μmol/L for 3 d. The expression of EGFR, p‐EGFR (Y1068) and PRMT5 was determined by Western blotting. D, The quantification of EGFR and p‐EGFR is shown. ** P < .01, *** P < .001. E, Wnt/β‐catenin and EGFR signalling relative proteins were detected by Western blot in PaTu8988 and SW1990 pHA‐PRMT5 stable infected cells treated with Erlotinib (10 μmol/L) for 3 d

Techniques Used: Western Blot, Infection, Transfection, Plasmid Preparation, Expressing



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DNA and RNA nucleotide sequences
Prmt5 Protein Expression, supplied by Human Protein Atlas, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
prmt5 protein expression - by Bioz Stars, 2026-03
90/100 stars
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DNA and RNA nucleotide sequences

Journal: Journal of Cellular and Molecular Medicine

Article Title: PRMT5 promotes epithelial‐mesenchymal transition via EGFR‐β‐catenin axis in pancreatic cancer cells

doi: 10.1111/jcmm.14894

Figure Lengend Snippet: DNA and RNA nucleotide sequences

Article Snippet: To confirm the clinical relevance of PRMT5 expression, we first analysed the PRMT5 protein expression in clinical specimens from the human protein atlas ( http://www.proteinatlas.org ).

Techniques:

PRMT5 is profiled in pancreatic cancers and different pancreatic cancer cells. A, PRMT5 protein expression in pancreatic cancer tissues and normal pancreatic tissues was analysed through the human protein atlas ( http://www.proteinatlas.org ). Magnification, ×4; bars, 500 μm. Magnification, ×40; bars, 100 μm. B, Analysis of PRMT5 mRNA levels in 39 pairs of pancreatic cancer and non‐tumour tissues in Badea pancreas database. N = 39 for non‐tumour group, and N = 39 for tumour group. *** P < .001. C, Analysis of the TCGA database indicates that PRMT5 expression is correlated with patient’ overall survival. N = 32 for PRMT5‐low group, and N = 50 for PRMT5‐high group. P = .0345 was determined by log‐rank test. D, Analysis of the TCGA database indicates PRMT5 correlates with clinicopathological features. The results are presented by heat map (left panel) and box plot (right panel). N = 139 for pancreas adenocarcinoma ductal type group, N = 23 for pancreas adenocarcinoma other subtype group, and N = 4 for pancreas colloid (mucinous non‐cystic) carcinoma group. P = .0707 (E) Analysis of the TCGA database indicates PRMT5 is associated with stage in pancreatic cancer. The results are presented by heat map (left panel) and box plot (right panel). N = 20 for stage I group, N = 147 for stage II + III + IV group. * P < .05

Journal: Journal of Cellular and Molecular Medicine

Article Title: PRMT5 promotes epithelial‐mesenchymal transition via EGFR‐β‐catenin axis in pancreatic cancer cells

doi: 10.1111/jcmm.14894

Figure Lengend Snippet: PRMT5 is profiled in pancreatic cancers and different pancreatic cancer cells. A, PRMT5 protein expression in pancreatic cancer tissues and normal pancreatic tissues was analysed through the human protein atlas ( http://www.proteinatlas.org ). Magnification, ×4; bars, 500 μm. Magnification, ×40; bars, 100 μm. B, Analysis of PRMT5 mRNA levels in 39 pairs of pancreatic cancer and non‐tumour tissues in Badea pancreas database. N = 39 for non‐tumour group, and N = 39 for tumour group. *** P < .001. C, Analysis of the TCGA database indicates that PRMT5 expression is correlated with patient’ overall survival. N = 32 for PRMT5‐low group, and N = 50 for PRMT5‐high group. P = .0345 was determined by log‐rank test. D, Analysis of the TCGA database indicates PRMT5 correlates with clinicopathological features. The results are presented by heat map (left panel) and box plot (right panel). N = 139 for pancreas adenocarcinoma ductal type group, N = 23 for pancreas adenocarcinoma other subtype group, and N = 4 for pancreas colloid (mucinous non‐cystic) carcinoma group. P = .0707 (E) Analysis of the TCGA database indicates PRMT5 is associated with stage in pancreatic cancer. The results are presented by heat map (left panel) and box plot (right panel). N = 20 for stage I group, N = 147 for stage II + III + IV group. * P < .05

Article Snippet: To confirm the clinical relevance of PRMT5 expression, we first analysed the PRMT5 protein expression in clinical specimens from the human protein atlas ( http://www.proteinatlas.org ).

Techniques: Expressing

PRMT5 promotes cell proliferation in pancreatic cancer cells and tumorigenesis. A‐B, CCK‐8 assay showed that PRMT5 knockdown inhibited PaTu8988 and SW1990 cell growth rate (Student's t test:* P < .05). C‐D, Clone formation assays in PaTu8988 and SW1990 cells. PRMT5 knockdown inhibited cell clone formation (Student's t test:* P < .05). The number of clones with at least 50 cells per colony and strong, high dense staining was counted. The rates of colony formation were 48.33% and 17.67% in sh‐EGFP and sh‐PRMT5 PaTu8988 cells, and 35.67% and 10.67% in sh‐EGFP and sh‐PRMT5 SW1990 cells, respectively. E‐F, PaTu8988 cells with PRMT5 down‐regulation were injected (2.0 × 10 6 cells/site) subcutaneously into a mice, and the tumour volume was measured weekly (n = 5 mice). * P < .05. G‐H, CCK‐8 assay showed that ectopic PRMT5 re‐expression in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells promoted cell proliferation rate (Student's t test: * P < .05). I‐J, Clone formation assays in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. Ectopic PRMT5 re‐expression in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells promoted cell clone formation (Student's t test: *** P < .001). The rates of number of colonies (defined as ≥50 cells) were 25.33% and 56.67% in PaTu8988 cells, 18.67% and 58.33% in SW1990 cells, respectively. K‐L, SW1990 cells with PRMT5 up‐regulation were injected (2.0 × 10 6 cells/site) subcutaneously into a mice, and the tumour volume was measured weekly (n = 5 mice), * P < .05

Journal: Journal of Cellular and Molecular Medicine

Article Title: PRMT5 promotes epithelial‐mesenchymal transition via EGFR‐β‐catenin axis in pancreatic cancer cells

doi: 10.1111/jcmm.14894

Figure Lengend Snippet: PRMT5 promotes cell proliferation in pancreatic cancer cells and tumorigenesis. A‐B, CCK‐8 assay showed that PRMT5 knockdown inhibited PaTu8988 and SW1990 cell growth rate (Student's t test:* P < .05). C‐D, Clone formation assays in PaTu8988 and SW1990 cells. PRMT5 knockdown inhibited cell clone formation (Student's t test:* P < .05). The number of clones with at least 50 cells per colony and strong, high dense staining was counted. The rates of colony formation were 48.33% and 17.67% in sh‐EGFP and sh‐PRMT5 PaTu8988 cells, and 35.67% and 10.67% in sh‐EGFP and sh‐PRMT5 SW1990 cells, respectively. E‐F, PaTu8988 cells with PRMT5 down‐regulation were injected (2.0 × 10 6 cells/site) subcutaneously into a mice, and the tumour volume was measured weekly (n = 5 mice). * P < .05. G‐H, CCK‐8 assay showed that ectopic PRMT5 re‐expression in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells promoted cell proliferation rate (Student's t test: * P < .05). I‐J, Clone formation assays in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. Ectopic PRMT5 re‐expression in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells promoted cell clone formation (Student's t test: *** P < .001). The rates of number of colonies (defined as ≥50 cells) were 25.33% and 56.67% in PaTu8988 cells, 18.67% and 58.33% in SW1990 cells, respectively. K‐L, SW1990 cells with PRMT5 up‐regulation were injected (2.0 × 10 6 cells/site) subcutaneously into a mice, and the tumour volume was measured weekly (n = 5 mice), * P < .05

Article Snippet: To confirm the clinical relevance of PRMT5 expression, we first analysed the PRMT5 protein expression in clinical specimens from the human protein atlas ( http://www.proteinatlas.org ).

Techniques: CCK-8 Assay, Knockdown, Clone Assay, Staining, Injection, Expressing, Infection

PRMT5 promotes cell migration and invasion in pancreatic cancer cells. A‐B, The migration changes were measured by transwell assay in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells (Student's t test: ** P < .01, *** P < .001). C‐D, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the migration changes were measured by transwell assay (Student's t test: ** P < .01). E‐F, The invasion changes were measured by transwell assay in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells (Student's t test: *** P < .001). The number of cells passing through the reconstituted basement membrane was 363.13 ± 26.25 and 152.54 ± 9.13 in sh‐EGFP and sh‐PRMT5 PaTu8988 cells, and 204.38 ± 18.38 and 89.54 ± 6.75 in sh‐EGFP and sh‐PRMT5 SW1990 cells, respectively. G‐H, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the invasion changes were measured by transwell assay (Student's t test: ** P < .01). Numbers of cells passing through the reconstituted basement membrane were 212.33 ± 12.54 and 403.13 ± 35.42 in PaTu8988 cells, 132.04 ± 8.29 and 212.21 ± 16.46 in SW1990 cells, respectively. I‐J, The protein levels of MMP2 and MMP9 were measured by Western blot

Journal: Journal of Cellular and Molecular Medicine

Article Title: PRMT5 promotes epithelial‐mesenchymal transition via EGFR‐β‐catenin axis in pancreatic cancer cells

doi: 10.1111/jcmm.14894

Figure Lengend Snippet: PRMT5 promotes cell migration and invasion in pancreatic cancer cells. A‐B, The migration changes were measured by transwell assay in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells (Student's t test: ** P < .01, *** P < .001). C‐D, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the migration changes were measured by transwell assay (Student's t test: ** P < .01). E‐F, The invasion changes were measured by transwell assay in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells (Student's t test: *** P < .001). The number of cells passing through the reconstituted basement membrane was 363.13 ± 26.25 and 152.54 ± 9.13 in sh‐EGFP and sh‐PRMT5 PaTu8988 cells, and 204.38 ± 18.38 and 89.54 ± 6.75 in sh‐EGFP and sh‐PRMT5 SW1990 cells, respectively. G‐H, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the invasion changes were measured by transwell assay (Student's t test: ** P < .01). Numbers of cells passing through the reconstituted basement membrane were 212.33 ± 12.54 and 403.13 ± 35.42 in PaTu8988 cells, 132.04 ± 8.29 and 212.21 ± 16.46 in SW1990 cells, respectively. I‐J, The protein levels of MMP2 and MMP9 were measured by Western blot

Article Snippet: To confirm the clinical relevance of PRMT5 expression, we first analysed the PRMT5 protein expression in clinical specimens from the human protein atlas ( http://www.proteinatlas.org ).

Techniques: Migration, Transwell Assay, Infection, Transfection, Plasmid Preparation, Membrane, Western Blot

PRMT5 promotes EMT in pancreatic cancer cells. A, The protein levels of E‐cadherin, collagen I, β‐catenin and Vimentin were measured by Western blot in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. B, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the protein levels of E‐cadherin, collagen I, β‐catenin and Vimentin were measured by Western blot. C‐D, Vimentin, β‐catenin and Collagen I mRNA levels were reduced while E‐cadherin mRNA level was increased in shPRMT5‐PaTu8988 and SW1990 cells. * P < .05, ** P < .01, *** P < .001. E‐F, Vimentin, β‐catenin and Collagen I mRNA levels were increased while E‐cadherin mRNA level was reduced in sh‐PRMT5 PaTu8988 and SW1990 cells transfected with pHA‐PRMT5 plasmid. * P < .05, ** P < .01, *** P < .001

Journal: Journal of Cellular and Molecular Medicine

Article Title: PRMT5 promotes epithelial‐mesenchymal transition via EGFR‐β‐catenin axis in pancreatic cancer cells

doi: 10.1111/jcmm.14894

Figure Lengend Snippet: PRMT5 promotes EMT in pancreatic cancer cells. A, The protein levels of E‐cadherin, collagen I, β‐catenin and Vimentin were measured by Western blot in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. B, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, the protein levels of E‐cadherin, collagen I, β‐catenin and Vimentin were measured by Western blot. C‐D, Vimentin, β‐catenin and Collagen I mRNA levels were reduced while E‐cadherin mRNA level was increased in shPRMT5‐PaTu8988 and SW1990 cells. * P < .05, ** P < .01, *** P < .001. E‐F, Vimentin, β‐catenin and Collagen I mRNA levels were increased while E‐cadherin mRNA level was reduced in sh‐PRMT5 PaTu8988 and SW1990 cells transfected with pHA‐PRMT5 plasmid. * P < .05, ** P < .01, *** P < .001

Article Snippet: To confirm the clinical relevance of PRMT5 expression, we first analysed the PRMT5 protein expression in clinical specimens from the human protein atlas ( http://www.proteinatlas.org ).

Techniques: Western Blot, Infection, Transfection, Plasmid Preparation

PRMT5 activates EGFR/AKT/β‐catenin signalling in pancreatic cancer cells. A, Wnt/β‐catenin and EGFR signalling relative proteins were detected by Western blot in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. B, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, EGFR/AKT/β‐catenin signalling relative proteins were detected by Western blot. C, Pancreatic cancer cells were treated with EGFR inhibitor at 0, 10 μmol/L for 3 d. The expression of EGFR, p‐EGFR (Y1068) and PRMT5 was determined by Western blotting. D, The quantification of EGFR and p‐EGFR is shown. ** P < .01, *** P < .001. E, Wnt/β‐catenin and EGFR signalling relative proteins were detected by Western blot in PaTu8988 and SW1990 pHA‐PRMT5 stable infected cells treated with Erlotinib (10 μmol/L) for 3 d

Journal: Journal of Cellular and Molecular Medicine

Article Title: PRMT5 promotes epithelial‐mesenchymal transition via EGFR‐β‐catenin axis in pancreatic cancer cells

doi: 10.1111/jcmm.14894

Figure Lengend Snippet: PRMT5 activates EGFR/AKT/β‐catenin signalling in pancreatic cancer cells. A, Wnt/β‐catenin and EGFR signalling relative proteins were detected by Western blot in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells. B, After transfected with pHA‐Venus or pHA‐PRMT5 plasmid in PaTu8988 and SW1990 sh‐PRMT5 stable infected cells, EGFR/AKT/β‐catenin signalling relative proteins were detected by Western blot. C, Pancreatic cancer cells were treated with EGFR inhibitor at 0, 10 μmol/L for 3 d. The expression of EGFR, p‐EGFR (Y1068) and PRMT5 was determined by Western blotting. D, The quantification of EGFR and p‐EGFR is shown. ** P < .01, *** P < .001. E, Wnt/β‐catenin and EGFR signalling relative proteins were detected by Western blot in PaTu8988 and SW1990 pHA‐PRMT5 stable infected cells treated with Erlotinib (10 μmol/L) for 3 d

Article Snippet: To confirm the clinical relevance of PRMT5 expression, we first analysed the PRMT5 protein expression in clinical specimens from the human protein atlas ( http://www.proteinatlas.org ).

Techniques: Western Blot, Infection, Transfection, Plasmid Preparation, Expressing