Review

polyclonal rabbit anti-human integrin alphav (Millipore)

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Millipore polyclonal rabbit anti-human integrin alphav
Polyclonal Rabbit Anti Human Integrin Alphav, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/polyclonal rabbit anti-human integrin alphav/product/Millipore
Average 90 stars, based on 1 article reviews

polyclonal rabbit anti-human integrin alphav - by Bioz Stars, 2026-03

90/100 stars

Images

Image Search Results

a The graph displays the −log10-transformed RRA scores of genes enriched following infection with two SAFV-3 strains in HeLaN-∆SLC cells, analyzed using the MAGeCK software. The X -axis represents data from the screen using the SAFV-3 JPN08-356 strain, whereas the Y -axis shows results from the screen using the SAFV-3 JPN08-404 strain. The dotted line indicates the significance threshold of RRA = 0.01. Genes that met the criterion of RRA < 0.01 in both screens are highlighted in blue. The size of each dot reflects the combined enrichment across both screens, with larger dots indicating a greater sum of −log10 (RRA scores) from both experiments. b Expression of human integrin αV and integrin β8 in HeLaN-WT, HeLaN-∆AV, HeLaN-∆SLC∆AV, HeLaN-∆B8, and HeLaN-∆SLC∆B8 cells. The cells were stained with anti-integrin αV or anti-integrin αVβ8 antibodies and analyzed by flow cytometry. c HeLaN-WT, HeLaN-∆AV, HeLaN-∆B8, HeLaN-∆SLC∆AV, and HeLaN-∆SLC∆B8 cells were infected with tenfold serial dilutions of SAFV-3 and viable cells were stained with crystal violet to assess infection levels. Images are representative of two independent experiments. d Multi-step growth kinetics of SAFV-3 in HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-WT cells. The cells were infected with SAFV-3 and incubated for up to 5 days. Data are presented as mean viral titers with s.d. ( n = 3). Statistical significance was determined using the two-sided Welch’s t -test. **, P < 0.01, *, P < 0.05, n.s. not significant. The dotted line indicates the limit of detection. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a The graph displays the −log10-transformed RRA scores of genes enriched following infection with two SAFV-3 strains in HeLaN-∆SLC cells, analyzed using the MAGeCK software. The X -axis represents data from the screen using the SAFV-3 JPN08-356 strain, whereas the Y -axis shows results from the screen using the SAFV-3 JPN08-404 strain. The dotted line indicates the significance threshold of RRA = 0.01. Genes that met the criterion of RRA < 0.01 in both screens are highlighted in blue. The size of each dot reflects the combined enrichment across both screens, with larger dots indicating a greater sum of −log10 (RRA scores) from both experiments. b Expression of human integrin αV and integrin β8 in HeLaN-WT, HeLaN-∆AV, HeLaN-∆SLC∆AV, HeLaN-∆B8, and HeLaN-∆SLC∆B8 cells. The cells were stained with anti-integrin αV or anti-integrin αVβ8 antibodies and analyzed by flow cytometry. c HeLaN-WT, HeLaN-∆AV, HeLaN-∆B8, HeLaN-∆SLC∆AV, and HeLaN-∆SLC∆B8 cells were infected with tenfold serial dilutions of SAFV-3 and viable cells were stained with crystal violet to assess infection levels. Images are representative of two independent experiments. d Multi-step growth kinetics of SAFV-3 in HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-WT cells. The cells were infected with SAFV-3 and incubated for up to 5 days. Data are presented as mean viral titers with s.d. ( n = 3). Statistical significance was determined using the two-sided Welch’s t -test. **, P < 0.01, *, P < 0.05, n.s. not significant. The dotted line indicates the limit of detection. Source data are provided as a Source Data file.

Article Snippet: To detect of endogenous hamster integrin αV and β8, rabbit anti-human integrin αV polyclonal antibody (27096-1-AP, Proteintech) and rabbit anti-mouse integrin β8 (D1V7M) monoclonal antibody (88300, Cell Signaling Technology) were used, respectively.

Techniques: Transformation Assay, Infection, Software, Expressing, Staining, Flow Cytometry, Incubation

a Western blot analysis of integrin αV (left panel) and integrin β8 (right panel) expression in BHK-21 cells. BHK-21 cells that were lentivirally transduced with either human integrin αV (BHK + human AV) or hamster integrin β8 (BHK + hamster B8) were used as positive controls. The anti-integrin αV antibody cross-reacted with both human and hamster integrin αV. Actin served as the loading control. b Expression of HS, integrin αV, and β8 in BHK-21 derivatives. BHK-21 cells were stained with anti-HS antibody (upper left panel). BHK-21 cells stably expressing human integrin αV and/or β8 (BHK + human AV, BHK + human B8, BHK + human AVB8), as well as the control cells, were stained with anti-integrin αV or anti-integrin αVβ8 antibodies. The cells were analyzed by flow cytometry. c Susceptibility analysis using SAF/UnaG in BHK-21 cells expressing human integrin αV and/or β8. UnaG-positive cells (green, upper panel) and Hoechst-stained nuclei (blue, lower panel) were imaged at 16 h post-infection. Scale bar, 200 μm. The percentage of infected cells was determined by examining at least 1000 cells. Data are representative of two independent experiments. d One-step growth kinetics of SAFV-3 in BHK + human AV, BHK + human B8, BHK + human AVB8, and control cells. The cells were infected with SAFV-3 and incubated for up to 24 h. The dotted line indicates the limit of detection. e Western blot analysis of exogenous integrin β8 expression in BHK-21 cells lentivirally transduced with either mouse or hamster integrin β8. The anti-integrin β8 antibody cross-reacted with both mouse and hamster integrin β8. Actin served as the loading control. f Susceptibility analysis using SAF/UnaG in mouse and hamster integrin β8 expressing BHK-21 cells. UnaG-positive cells (green, upper panel) and Hoechst-stained nuclei (blue, lower panel) were captured at 16 h post-infection. Scale bar, 200 μm. Images are representative of two independent experiments. Data in ( c and d ) represent means with s.d. ( n = 3). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test ( c ) and the two-sided Welch’s t -test ( d ). **, P < 0.01, *, P < 0.05, n.s. not significant. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Western blot analysis of integrin αV (left panel) and integrin β8 (right panel) expression in BHK-21 cells. BHK-21 cells that were lentivirally transduced with either human integrin αV (BHK + human AV) or hamster integrin β8 (BHK + hamster B8) were used as positive controls. The anti-integrin αV antibody cross-reacted with both human and hamster integrin αV. Actin served as the loading control. b Expression of HS, integrin αV, and β8 in BHK-21 derivatives. BHK-21 cells were stained with anti-HS antibody (upper left panel). BHK-21 cells stably expressing human integrin αV and/or β8 (BHK + human AV, BHK + human B8, BHK + human AVB8), as well as the control cells, were stained with anti-integrin αV or anti-integrin αVβ8 antibodies. The cells were analyzed by flow cytometry. c Susceptibility analysis using SAF/UnaG in BHK-21 cells expressing human integrin αV and/or β8. UnaG-positive cells (green, upper panel) and Hoechst-stained nuclei (blue, lower panel) were imaged at 16 h post-infection. Scale bar, 200 μm. The percentage of infected cells was determined by examining at least 1000 cells. Data are representative of two independent experiments. d One-step growth kinetics of SAFV-3 in BHK + human AV, BHK + human B8, BHK + human AVB8, and control cells. The cells were infected with SAFV-3 and incubated for up to 24 h. The dotted line indicates the limit of detection. e Western blot analysis of exogenous integrin β8 expression in BHK-21 cells lentivirally transduced with either mouse or hamster integrin β8. The anti-integrin β8 antibody cross-reacted with both mouse and hamster integrin β8. Actin served as the loading control. f Susceptibility analysis using SAF/UnaG in mouse and hamster integrin β8 expressing BHK-21 cells. UnaG-positive cells (green, upper panel) and Hoechst-stained nuclei (blue, lower panel) were captured at 16 h post-infection. Scale bar, 200 μm. Images are representative of two independent experiments. Data in ( c and d ) represent means with s.d. ( n = 3). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test ( c ) and the two-sided Welch’s t -test ( d ). **, P < 0.01, *, P < 0.05, n.s. not significant. Source data are provided as a Source Data file.

Techniques: Western Blot, Expressing, Transduction, Control, Staining, Stable Transfection, Flow Cytometry, Infection, Incubation, Comparison

a Expression of human integrin β subunits (β1, β3, β5, and β6) on the surface of BHK-21 derivatives. BHK-21 cells lentivirally transduced with the respective integrin β subunits were stained with the indicated antibodies and analyzed using flow cytometry. b Susceptibility analysis using SAF/UnaG in human integrin αV and the indicated β subunit expressing BHK-21 cells. UnaG-positive cells (green, upper panel) and nuclei stained with Hoechst (blue, lower panel) were imaged at 16 h post-infection. Scale bar, 200 μm. Images are representative of two independent experiments.

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Expression of human integrin β subunits (β1, β3, β5, and β6) on the surface of BHK-21 derivatives. BHK-21 cells lentivirally transduced with the respective integrin β subunits were stained with the indicated antibodies and analyzed using flow cytometry. b Susceptibility analysis using SAF/UnaG in human integrin αV and the indicated β subunit expressing BHK-21 cells. UnaG-positive cells (green, upper panel) and nuclei stained with Hoechst (blue, lower panel) were imaged at 16 h post-infection. Scale bar, 200 μm. Images are representative of two independent experiments.

Techniques: Expressing, Transduction, Staining, Flow Cytometry, Infection

a Pull-down assay of SAFV-3 using heparin (left panel) and integrin αVβ8 (right panel). Heparin and Fc chimera of extracellular domains of integrin αVβ8, αVβ3, or the signal sequence (ss) of integrin αV (negative control) were prepared as complexes with magnetic beads. These complexes were incubated with SAFV-3, followed by western blot analysis of the bound virus using anti-SAFV-3 antiserum (left and right upper panels). The bottom right panel shows an image of the integrin-Fc complex on magnetic beads used for pulldown, detected using an anti-mouse IgG antibody. b Cell surface attachment assay for SAFV-3. HeLaN-WT, HeLaN-∆SLC, HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-∆SLC + human AVB8 were incubated with SAFV-3, followed by RT-qPCR analysis of the bound virus. c Expression of human integrin β8 in HeLaN-∆SLC and HeLaN-∆SLC + human AVB8 cells. To compare the expression levels of integrin αVβ8 on the cell surface, HeLaN-∆SLC and HeLaN-∆SLC + human AVB8 cells were stained with anti-integrin αVβ8 antibodies and analyzed by flow cytometry. d , e Inhibition of SAFV-3 attachment to the cell surface by soluble heparin ( d ) or recombinant integrin αVβ8 ( e ). HeLaN-WT cells ( d ) or HeLaN-∆SLC + human AVB8 cells ( e ) were incubated with SAFV-3 pretreated with 1 or 10 μg of soluble heparin or recombinant integrin αVβ8, respectively. Recombinant integrin αVβ3 was the negative control. After incubation at 4 °C for 2 h, bound virus was analyzed using RT-qPCR. f HeLaN-WT, HeLaN-∆SLC, HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-∆SLC + human AVB8 cells were infected with tenfold serial dilutions of SAFV-3, and viable cells were stained with crystal violet to assess infection levels. All data are representative of two independent experiments. Data in ( b , d , and e ) represent means with s.d. ( n = 3). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test. **, P < 0.01, n.s. not significant. Asterisks directly placed on bars indicate statistically significant differences compared to WT or untreated samples, while asterisks placed on the lines connecting bars denote statistically significant differences between those bars. Source data are provided as a Source Data file. Ag antigen, Fc fragment crystallizable region.

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Pull-down assay of SAFV-3 using heparin (left panel) and integrin αVβ8 (right panel). Heparin and Fc chimera of extracellular domains of integrin αVβ8, αVβ3, or the signal sequence (ss) of integrin αV (negative control) were prepared as complexes with magnetic beads. These complexes were incubated with SAFV-3, followed by western blot analysis of the bound virus using anti-SAFV-3 antiserum (left and right upper panels). The bottom right panel shows an image of the integrin-Fc complex on magnetic beads used for pulldown, detected using an anti-mouse IgG antibody. b Cell surface attachment assay for SAFV-3. HeLaN-WT, HeLaN-∆SLC, HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-∆SLC + human AVB8 were incubated with SAFV-3, followed by RT-qPCR analysis of the bound virus. c Expression of human integrin β8 in HeLaN-∆SLC and HeLaN-∆SLC + human AVB8 cells. To compare the expression levels of integrin αVβ8 on the cell surface, HeLaN-∆SLC and HeLaN-∆SLC + human AVB8 cells were stained with anti-integrin αVβ8 antibodies and analyzed by flow cytometry. d , e Inhibition of SAFV-3 attachment to the cell surface by soluble heparin ( d ) or recombinant integrin αVβ8 ( e ). HeLaN-WT cells ( d ) or HeLaN-∆SLC + human AVB8 cells ( e ) were incubated with SAFV-3 pretreated with 1 or 10 μg of soluble heparin or recombinant integrin αVβ8, respectively. Recombinant integrin αVβ3 was the negative control. After incubation at 4 °C for 2 h, bound virus was analyzed using RT-qPCR. f HeLaN-WT, HeLaN-∆SLC, HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-∆SLC + human AVB8 cells were infected with tenfold serial dilutions of SAFV-3, and viable cells were stained with crystal violet to assess infection levels. All data are representative of two independent experiments. Data in ( b , d , and e ) represent means with s.d. ( n = 3). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test. **, P < 0.01, n.s. not significant. Asterisks directly placed on bars indicate statistically significant differences compared to WT or untreated samples, while asterisks placed on the lines connecting bars denote statistically significant differences between those bars. Source data are provided as a Source Data file. Ag antigen, Fc fragment crystallizable region.

Techniques: Pull Down Assay, Sequencing, Negative Control, Magnetic Beads, Incubation, Western Blot, Virus, Quantitative RT-PCR, Expressing, Staining, Flow Cytometry, Inhibition, Recombinant, Infection, Comparison

a Expression of HS and human integrin β8 in BHK-WT, BHK-∆SLC, BHK + human AVB8, BHK-∆SLC + human AVB8, and revertant cells expressing human SLC35B2 (BHK-∆SLC + human AVB8 + SLC). The cells were stained with anti-HS or anti-integrin αVβ8 antibodies and analyzed by flow cytometry. b Cell surface attachment assay for SAFV-3. BHK-WT and BHK-∆SLC cells were incubated with SAFV-3 at 4 °C for 2 h. Viral binding to HS was assessed by RT-qPCR quantification of cell-bound virus ( n = 3). c Susceptibility analysis using SAF/UnaG in BHK + human AVB8, BHK-∆SLC + human AVB8, and BHK-∆SLC + human AVB8 + SLC cells. The cells used in this experiment were sorted to equalize the surface expression levels of integrin αVβ8 between BHK + human AVB8 and BHK-∆SLC + human AVB8 cells. UnaG-positive cells (green) and nuclei stained with Hoechst (blue) were imaged at 16 h post-infection. The percentage of infected cells was determined by examining at least 800 cells/well ( n = 4). Scale bar, 200 μm. d Cell surface attachment assay for SAFV-3 in BHK + human AVB8, BHK-∆SLC + human AVB8, and BHK-∆SLC + human AVB8 + SLC cells ( n = 3). Bar graphs in ( b– d ) are presented as means with s.d. Statistical significance was determined using the two-sided Welch’s t -test ( b ) and a one-way ANOVA with Dunnett’s multiple comparison test ( c , d ). **, P < 0.01, *, P < 0.05. All data are representative of two independent experiments. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Expression of HS and human integrin β8 in BHK-WT, BHK-∆SLC, BHK + human AVB8, BHK-∆SLC + human AVB8, and revertant cells expressing human SLC35B2 (BHK-∆SLC + human AVB8 + SLC). The cells were stained with anti-HS or anti-integrin αVβ8 antibodies and analyzed by flow cytometry. b Cell surface attachment assay for SAFV-3. BHK-WT and BHK-∆SLC cells were incubated with SAFV-3 at 4 °C for 2 h. Viral binding to HS was assessed by RT-qPCR quantification of cell-bound virus ( n = 3). c Susceptibility analysis using SAF/UnaG in BHK + human AVB8, BHK-∆SLC + human AVB8, and BHK-∆SLC + human AVB8 + SLC cells. The cells used in this experiment were sorted to equalize the surface expression levels of integrin αVβ8 between BHK + human AVB8 and BHK-∆SLC + human AVB8 cells. UnaG-positive cells (green) and nuclei stained with Hoechst (blue) were imaged at 16 h post-infection. The percentage of infected cells was determined by examining at least 800 cells/well ( n = 4). Scale bar, 200 μm. d Cell surface attachment assay for SAFV-3 in BHK + human AVB8, BHK-∆SLC + human AVB8, and BHK-∆SLC + human AVB8 + SLC cells ( n = 3). Bar graphs in ( b– d ) are presented as means with s.d. Statistical significance was determined using the two-sided Welch’s t -test ( b ) and a one-way ANOVA with Dunnett’s multiple comparison test ( c , d ). **, P < 0.01, *, P < 0.05. All data are representative of two independent experiments. Source data are provided as a Source Data file.

Techniques: Expressing, Staining, Flow Cytometry, Incubation, Binding Assay, Quantitative RT-PCR, Virus, Infection, Comparison

a Viral infection analysis using integrin β8 mutants. BHK-21 cells expressing the human integrin β8 mutants (∆SDL, Y172N, and I208R) were inoculated with SAFV-3. After 2 days, virus titers were determined using the TCID 50 assay. Human integrin β3 was the negative control. The dotted line indicates the limit of detection. The right panel shows the results of western blot analysis of integrin β8 mutants and integrin β3 expression in BHK-21 cells. b Alignment of the amino acid sequences of puff A on VP2 of SAFV-3 (left panel) and CD loop I on VP1 of SAFV-2 (right panel). RGD-like sequences are highlighted. c Infection blocking assay using RGD peptide. Left panel: HeLaN-∆SLC cells were pretreated with 10 or 100 μg of GRGDS, GRADS, or GRAES peptide at 4 °C for 30 min and then incubated with SAFV-3/UnaG virus for an additional 60 min. Right panel: HeLaN-∆SLC cells were pretreated with 10 or 100 μg of GRGDS, GRLDS, or GRAES peptide for 30 min and then incubated with SAFV-2/UnaG virus for an additional 60 min. GRGDS and GRAES peptides were positive and negative controls, respectively. The number of UnaG-positive cells at 14 h post-infection was counted using ImageJ software. d Schematic illustration of mutagenesis in RGD-like sequence. The mutated amino acid residues are highlighted. e HeLaN-∆SLC∆B8, HeLaN-∆SLC, and HeLaN-∆SLC + human AVB8 cells were infected with tenfold serial dilutions of mutant viruses carrying mutations in the RGD-like sequences, and viable cells were stained with crystal violet. Primary progeny virus produced from BHK cells transfected with infectious RNA (P-0 virus) was used. Bar graphs in ( a and c ) represent means with s.d. ( n = 3 in ( a ); n = 9 peptide-free and n = 3 peptide-added samples in ( c )). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test. **, P < 0.01, n.s. not significant. Statistical comparisons in ( c ) were made between peptide-free and peptide-added samples. All data are representative of two independent experiments. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Viral infection analysis using integrin β8 mutants. BHK-21 cells expressing the human integrin β8 mutants (∆SDL, Y172N, and I208R) were inoculated with SAFV-3. After 2 days, virus titers were determined using the TCID 50 assay. Human integrin β3 was the negative control. The dotted line indicates the limit of detection. The right panel shows the results of western blot analysis of integrin β8 mutants and integrin β3 expression in BHK-21 cells. b Alignment of the amino acid sequences of puff A on VP2 of SAFV-3 (left panel) and CD loop I on VP1 of SAFV-2 (right panel). RGD-like sequences are highlighted. c Infection blocking assay using RGD peptide. Left panel: HeLaN-∆SLC cells were pretreated with 10 or 100 μg of GRGDS, GRADS, or GRAES peptide at 4 °C for 30 min and then incubated with SAFV-3/UnaG virus for an additional 60 min. Right panel: HeLaN-∆SLC cells were pretreated with 10 or 100 μg of GRGDS, GRLDS, or GRAES peptide for 30 min and then incubated with SAFV-2/UnaG virus for an additional 60 min. GRGDS and GRAES peptides were positive and negative controls, respectively. The number of UnaG-positive cells at 14 h post-infection was counted using ImageJ software. d Schematic illustration of mutagenesis in RGD-like sequence. The mutated amino acid residues are highlighted. e HeLaN-∆SLC∆B8, HeLaN-∆SLC, and HeLaN-∆SLC + human AVB8 cells were infected with tenfold serial dilutions of mutant viruses carrying mutations in the RGD-like sequences, and viable cells were stained with crystal violet. Primary progeny virus produced from BHK cells transfected with infectious RNA (P-0 virus) was used. Bar graphs in ( a and c ) represent means with s.d. ( n = 3 in ( a ); n = 9 peptide-free and n = 3 peptide-added samples in ( c )). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test. **, P < 0.01, n.s. not significant. Statistical comparisons in ( c ) were made between peptide-free and peptide-added samples. All data are representative of two independent experiments. Source data are provided as a Source Data file.

Techniques: Infection, Expressing, Virus, Negative Control, Western Blot, Blocking Assay, Incubation, Software, Mutagenesis, Sequencing, Staining, Produced, Transfection, Comparison

Sulfated GAGs and integrin αVβ8 function as interconnected dual receptors for SAFV infection in HeLa-N cells. SAFV can directly bind to either sulfated GAGs or integrin αVβ8, while a portion of viruses bound to sulfated GAGs subsequently interact with integrin αVβ8. In addition, the data suggest the existence of a downstream molecule (factor X) required for an unspecified step in the viral entry process following sulfated GAGs binding.

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: Sulfated GAGs and integrin αVβ8 function as interconnected dual receptors for SAFV infection in HeLa-N cells. SAFV can directly bind to either sulfated GAGs or integrin αVβ8, while a portion of viruses bound to sulfated GAGs subsequently interact with integrin αVβ8. In addition, the data suggest the existence of a downstream molecule (factor X) required for an unspecified step in the viral entry process following sulfated GAGs binding.

Techniques: Infection, Binding Assay

YAP1 regulates Wnt5A-induced integrin av and Smad2/3 activation. SKOV-3, OVCAR-3, and CAOV-4 cells were transfected with siRNA Scrambled (Scr) or Wnt5A. ( A ) Integrin αv expression level was assessed by immunoblotting in multicellular aggregates (MCAs) OvCa cells (upper panel) and quantifying bands from three experiments in the lower panel. ( B ) The cells were pre-treated with VP (5 μM) 1 h or treated with rhWnt5A (600 ng/mL) for 14 h alone or VP-pretreated + rhWnt5A then expression levels of integrin αv was determined in MCAs OvCa cells (Left panel), and quantification of bands (right panel). ( C ） The Wnt5A overexpressing OVCAR-3 (C3/OVCAR-3) and SKOV-3 clones (C9/SKOV-3) were treated with CWHM-12 (10 μM) for 24 h. Immunoblot of TGFβ1, pSmad2/3, YAP1 determined in MCAs OvCa cells (Left panel) and quantification of bands (right panels). The lower panel shows the quantification of bands from three independent experiments. GAPDH levels were used as an internal control, and results are expressed as mean ± SD. (D) The immunolocalization of pSmad2/3 and YAP-1 in CWHM-12-treated cells compared to control. Original magnification, ×400. *: p < 0.05, **: p < 0.01 and ***: p < 0.001 compared to untreated control cells (Ctrl) or Scr.

Journal: Cells

Article Title: Wnt5A and TGFβ1 Converges through YAP1 Activity and Integrin Alpha v Up-Regulation Promoting Epithelial to Mesenchymal Transition in Ovarian Cancer Cells and Mesothelial Cell Activation

doi: 10.3390/cells11020237

Figure Lengend Snippet: YAP1 regulates Wnt5A-induced integrin av and Smad2/3 activation. SKOV-3, OVCAR-3, and CAOV-4 cells were transfected with siRNA Scrambled (Scr) or Wnt5A. ( A ) Integrin αv expression level was assessed by immunoblotting in multicellular aggregates (MCAs) OvCa cells (upper panel) and quantifying bands from three experiments in the lower panel. ( B ) The cells were pre-treated with VP (5 μM) 1 h or treated with rhWnt5A (600 ng/mL) for 14 h alone or VP-pretreated + rhWnt5A then expression levels of integrin αv was determined in MCAs OvCa cells (Left panel), and quantification of bands (right panel). ( C ） The Wnt5A overexpressing OVCAR-3 (C3/OVCAR-3) and SKOV-3 clones (C9/SKOV-3) were treated with CWHM-12 (10 μM) for 24 h. Immunoblot of TGFβ1, pSmad2/3, YAP1 determined in MCAs OvCa cells (Left panel) and quantification of bands (right panels). The lower panel shows the quantification of bands from three independent experiments. GAPDH levels were used as an internal control, and results are expressed as mean ± SD. (D) The immunolocalization of pSmad2/3 and YAP-1 in CWHM-12-treated cells compared to control. Original magnification, ×400. *: p < 0.05, **: p < 0.01 and ***: p < 0.001 compared to untreated control cells (Ctrl) or Scr.

Article Snippet: The following antibodies were used in this study: mouse monoclonal anti-human pSmad2/3 and mouse monoclonal anti-human Smad2/3 were purchased from (Santa Cruz Biotechnology Inc. Heidelberg, Germany), rabbit polyclonal anti-human TGFβ1, rabbit polyclonal anti-human YAP1, and rabbit polyclonal anti-human integrin αv (Biorbyt Ltd., Cambridge, UK); mouse monoclonal anti-human Wnt5A and rabbit polyclonal anti-human GAPDH rabbit polyclonal anti-human α-SMA (Abcam, Boston, MA, USA).

Techniques: Activation Assay, Transfection, Expressing, Western Blot, Clone Assay, Control

Model of Wnt5A involvement in EMT and mesothelial activation and clearance. Wnt5A derived from ovarian cancer cells through cytoskeletal rearrangement could directly or indirectly cause YAP1 phosphorylation, which translocates into the nucleus and induces TGFβ1, integrin αv, Wnt5A, and other EMT markers in this drawing. Integrin αv, in turn, may activate extracellular latent-TGFβ1 and play a pivotal role in the EMT process. In addition, YAP1 may cause retention of Smad2/3 in the nucleus, thereby prolonging their biological activity.

Journal: Cells

doi: 10.3390/cells11020237

Figure Lengend Snippet: Model of Wnt5A involvement in EMT and mesothelial activation and clearance. Wnt5A derived from ovarian cancer cells through cytoskeletal rearrangement could directly or indirectly cause YAP1 phosphorylation, which translocates into the nucleus and induces TGFβ1, integrin αv, Wnt5A, and other EMT markers in this drawing. Integrin αv, in turn, may activate extracellular latent-TGFβ1 and play a pivotal role in the EMT process. In addition, YAP1 may cause retention of Smad2/3 in the nucleus, thereby prolonging their biological activity.

Techniques: Activation Assay, Derivative Assay, Phospho-proteomics, Activity Assay

Review

Structured Review

Images

Similar Products

Image Search Results