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Proteintech rabbit anti integrin alpha v polyclonal antibody

Immunohistochemistry for periostin receptor subunits in nasal mucosae of control (left panels) and Japanese cedar pollen (JCP)-challenged mice (right panels). Male ICR mice were sensitized by i.p . injections of JCP (0.1 mg in 50 µL PBS) with 2 mg Imuject Alum on days 0, 7, and 14. On days 21–24, animals were intranasally challenged with JCP (1 mg in 20 µL PBS, 10 µL/nostril) or its vehicle (PBS: control) under the conscious state every 24 h. Twenty-four hours after the last JCP challenge (day 25), the nasal tissues were isolated and subjected to immunohistochemical examinations with <t>anti-integrin</t> <t>alpha</t> <t>v</t> (Itgav: 1:300 dilution; upper panels ), anti-integrin beta 3 (Itgb3: 1:300 dilution; middle panels ), and anti-integrin beta 5 (Itgb5: 1:400 dilution; lower panels ) antibodies in paraffin-embedded sections (4 µm thickness). Scale bars: 50 µm.

Rabbit Anti Integrin Alpha V Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+integrin+alpha+v+polyclonal+antibody/ITGAV+Antibody/pmc12898203-151-5-14
Average 93 stars, based on 38 article reviews

rabbit anti integrin alpha v polyclonal antibody - by Bioz Stars, 2026-09

93/100 stars

Images

1) Product Images from "Role of Periostin in the Development of Nasal Hyperresponsiveness in Mice with Allergic Rhinitis"

Article Title: Role of Periostin in the Development of Nasal Hyperresponsiveness in Mice with Allergic Rhinitis

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms27031151

Figure Legend Snippet: Immunohistochemistry for periostin receptor subunits in nasal mucosae of control (left panels) and Japanese cedar pollen (JCP)-challenged mice (right panels). Male ICR mice were sensitized by i.p . injections of JCP (0.1 mg in 50 µL PBS) with 2 mg Imuject Alum on days 0, 7, and 14. On days 21–24, animals were intranasally challenged with JCP (1 mg in 20 µL PBS, 10 µL/nostril) or its vehicle (PBS: control) under the conscious state every 24 h. Twenty-four hours after the last JCP challenge (day 25), the nasal tissues were isolated and subjected to immunohistochemical examinations with anti-integrin alpha v (Itgav: 1:300 dilution; upper panels ), anti-integrin beta 3 (Itgb3: 1:300 dilution; middle panels ), and anti-integrin beta 5 (Itgb5: 1:400 dilution; lower panels ) antibodies in paraffin-embedded sections (4 µm thickness). Scale bars: 50 µm.

Techniques Used: Immunohistochemistry, Control, Isolation, Immunohistochemical staining

Immunohistochemistry:

Article Title: Role of Periostin in the Development of Nasal Hyperresponsiveness in Mice with Allergic Rhinitis
Article Snippet: The deparaffinized sections were also used for immunohistochemistry using IMMPRESS Horse Anti-Rabbit IgG Plus Polymer Kit (Vector Laboratories, Inc.) according to manufacturer’s instructions as previously described in detail [ , ].The deparaffinized sections were also used for immunohistochemistry using IMMPRESS Horse Anti-Rabbit IgG Plus Polymer Kit (Vector Laboratories, Inc.) according to manufacturer’s instructions as previously described in detail [ , ].. The primary antibodies used were rabbit anti-integrin alpha v polyclonal antibody (27096-1-AP, 1:300 dilution; Proteintech Group, Inc., Rosemont, IL, USA), rabbit anti-integrin beta 3 polyclonal antibody (18309-1-AP, 1:300 dilution; Proteintech Group, Inc.), and rabbit anti-integrin beta 5 polyclonal antibody (28543-1-AP, 1:400 dilution; Proteintech Group, Inc.).

Control:

Isolation:

Immunohistochemical staining:

Image Search Results

Journal: International Journal of Molecular Sciences

Article Title: Role of Periostin in the Development of Nasal Hyperresponsiveness in Mice with Allergic Rhinitis

doi: 10.3390/ijms27031151

Figure Lengend Snippet: Immunohistochemistry for periostin receptor subunits in nasal mucosae of control (left panels) and Japanese cedar pollen (JCP)-challenged mice (right panels). Male ICR mice were sensitized by i.p . injections of JCP (0.1 mg in 50 µL PBS) with 2 mg Imuject Alum on days 0, 7, and 14. On days 21–24, animals were intranasally challenged with JCP (1 mg in 20 µL PBS, 10 µL/nostril) or its vehicle (PBS: control) under the conscious state every 24 h. Twenty-four hours after the last JCP challenge (day 25), the nasal tissues were isolated and subjected to immunohistochemical examinations with anti-integrin alpha v (Itgav: 1:300 dilution; upper panels ), anti-integrin beta 3 (Itgb3: 1:300 dilution; middle panels ), and anti-integrin beta 5 (Itgb5: 1:400 dilution; lower panels ) antibodies in paraffin-embedded sections (4 µm thickness). Scale bars: 50 µm.

Article Snippet: The primary antibodies used were rabbit anti-integrin alpha v polyclonal antibody (27096-1-AP, 1:300 dilution; Proteintech Group, Inc., Rosemont, IL, USA), rabbit anti-integrin beta 3 polyclonal antibody (18309-1-AP, 1:300 dilution; Proteintech Group, Inc.), and rabbit anti-integrin beta 5 polyclonal antibody (28543-1-AP, 1:400 dilution; Proteintech Group, Inc.).

Techniques: Immunohistochemistry, Control, Isolation, Immunohistochemical staining

Western blotting of integrin subunits in PC3 cells and sEVs. (A) sEVs were isolated from the cell culture supernatant of intact PC3 cells or from cells in which an integrin subunit (β1, β4, α2, α6) was knocked out via the CRISPR-Cas9 method. (B) The correlation map of integrin heterodimers and the ECM.

Journal: bioRxiv

Article Title: Extracellular vesicles adhere to cells predominantly through the interaction of CD151-associated integrin heterodimers and GM1 with laminin

doi: 10.1101/2024.04.11.589011

Figure Lengend Snippet: Western blotting of integrin subunits in PC3 cells and sEVs. (A) sEVs were isolated from the cell culture supernatant of intact PC3 cells or from cells in which an integrin subunit (β1, β4, α2, α6) was knocked out via the CRISPR-Cas9 method. (B) The correlation map of integrin heterodimers and the ECM.

Article Snippet: The following primary antibodies were used for western blotting: mouse monoclonal anti-beta actin 15G5A11/E2 (1:5000, Thermo Fisher, Cat# MA1-140), mouse monoclonal anti-CD63 8A12 (1:1000, Cosmo Bio, Cat# SHI-EXO-M02), mouse monoclonal anti-CD81 B11 (1:500, Santa Cruz Biotechnology, Cat# SC166029), rabbit monoclonal anti-CD9 EPR23105-125 (1:1000, Abcam, Cat# ab263019), mouse monoclonal anti-CD151 11G5a (1:250, Abcam, Cat# ab33315), rabbit polyclonal anti-fibronectin (1:1000, Sigma‒Aldrich, Cat# F3648), rabbit monoclonal anti-GAPDH 14C10 (1:2000, Cell Signaling, Cat# 2181S), rabbit monoclonal anti-integrin alpha 2 EPR5788 (1:2500, Abcam, Cat# ab133557), rabbit polyclonal anti-integrin alpha 3 (1:500, Abcam, Cat# ab190731), rabbit polyclonal anti-integrin alpha 5 (1:250, Cell Signaling, Cat# 4705S), rabbit polyclonal anti-integrin alpha 6 (1:500, Cell Signaling, Cat# 3750S), rabbit polyclonal anti-integrin alpha 7 (1:500, Abcam, Cat# ab203254), rabbit polyclonal anti-integrin alpha V (1:500, Abcam, Cat# ab117611), mouse monoclonal anti-CD29 Clone 18 (1:2000, BD Bioscience, Cat# 610467), rabbit polyclonal anti-integrin beta 3 (1:500, Millipore, Cat# AB2984), rabbit polyclonal anti-integrin beta 4 (1:500, Cell Signaling, Cat# 4707S), rabbit polyclonal anti-integrin beta 5 (1:500, Cell Signaling, Cat# 4708S), rabbit polyclonal anti-laminin 1+2 (1:1000, Abcam, Cat# ab7463), mouse monoclonal anti-talin-1 97H6 (1:500, Gene Tex, Cat# GTX38972), rabbit polyclonal anti-phospho-talin (Ser-425), (1:250, ECM Biosciences, Cat# TP4171), and anti-GM3 antibody clone GMR6 (1:1000, Tokyo Chemical Industry, Cat# A2582), along with biotin-conjugated Cholera toxin B subunit (1:500, List Labs, Cat# 112).

Techniques: Western Blot, Isolation, Cell Culture, CRISPR

Integrin α2β1 in sEVs derived from PC3 cells is responsible for the binding of CD63-containing sEVs to collagen type I, and integrins α6β1 and α6β4 are responsible for the binding to laminin. (A, C, E, and G) Single-particle fluorescence images of sEV-CD63Halo7-SF650T on glass coated with fibronectin, collagen type I, and laminin before and after the KO of integrin β1 (A), integrin α2 (C), integrin α6 (E), and integrin β4 (G). (B, D, F, and H) The numbers of sEVs attached to glass coated with these extracellular matrix molecules before and after the KO of integrin β1 (B), integrin α2 (D), integrin α6 (F), and integrin β4 (H). The data are presented as the mean ± SE. * indicates a significant difference (p<0.001) according to Welch’s t-test (two-sided).

Journal: bioRxiv

Article Title: Extracellular vesicles adhere to cells predominantly through the interaction of CD151-associated integrin heterodimers and GM1 with laminin

doi: 10.1101/2024.04.11.589011

Figure Lengend Snippet: Integrin α2β1 in sEVs derived from PC3 cells is responsible for the binding of CD63-containing sEVs to collagen type I, and integrins α6β1 and α6β4 are responsible for the binding to laminin. (A, C, E, and G) Single-particle fluorescence images of sEV-CD63Halo7-SF650T on glass coated with fibronectin, collagen type I, and laminin before and after the KO of integrin β1 (A), integrin α2 (C), integrin α6 (E), and integrin β4 (G). (B, D, F, and H) The numbers of sEVs attached to glass coated with these extracellular matrix molecules before and after the KO of integrin β1 (B), integrin α2 (D), integrin α6 (F), and integrin β4 (H). The data are presented as the mean ± SE. * indicates a significant difference (p<0.001) according to Welch’s t-test (two-sided).

Techniques: Derivative Assay, Binding Assay, Single Particle, Fluorescence

GM1 is responsible for the binding of sEVs to laminin. (A) (top) Schematic diagram of gangliosides and (bottom) chemical structure of GM1. (B) Dot blotting of GM1 and GM3 in PC3 cells and PC3-derived sEVs. (C) Western blot analysis of integrin subunits in B78 cell lines with abundant expression of one type of ganglioside—GM1, GM2, GM3, GD2 or GD2/GD3—and sEVs derived from these cells. (D and E) The numbers of sEVs attached to glass coated with laminin (D) and the numbers normalized to the ratio of integrin α6/CD81 in the sEVs (E). (F and G) The numbers of sEVs attached to glass coated with fibronectin (F) and the numbers normalized to the ratio of integrin α5/CD81 in the sEVs (G). (H) Single-particle fluorescence images of DMPC-liposomes containing GM1, GM2, GM3, GD1a, GD2, or GD3 on glass coated with fibronectin or laminin. (I and J) The numbers of liposomes attached to glass coated with laminin (I) or fibronectin (J). The data are presented as the mean ± SE. * indicates a significant difference (p<0.001) according to Welch’s t-test (two-sided).

Journal: bioRxiv

Article Title: Extracellular vesicles adhere to cells predominantly through the interaction of CD151-associated integrin heterodimers and GM1 with laminin

doi: 10.1101/2024.04.11.589011

Figure Lengend Snippet: GM1 is responsible for the binding of sEVs to laminin. (A) (top) Schematic diagram of gangliosides and (bottom) chemical structure of GM1. (B) Dot blotting of GM1 and GM3 in PC3 cells and PC3-derived sEVs. (C) Western blot analysis of integrin subunits in B78 cell lines with abundant expression of one type of ganglioside—GM1, GM2, GM3, GD2 or GD2/GD3—and sEVs derived from these cells. (D and E) The numbers of sEVs attached to glass coated with laminin (D) and the numbers normalized to the ratio of integrin α6/CD81 in the sEVs (E). (F and G) The numbers of sEVs attached to glass coated with fibronectin (F) and the numbers normalized to the ratio of integrin α5/CD81 in the sEVs (G). (H) Single-particle fluorescence images of DMPC-liposomes containing GM1, GM2, GM3, GD1a, GD2, or GD3 on glass coated with fibronectin or laminin. (I and J) The numbers of liposomes attached to glass coated with laminin (I) or fibronectin (J). The data are presented as the mean ± SE. * indicates a significant difference (p<0.001) according to Welch’s t-test (two-sided).

Techniques: Binding Assay, Derivative Assay, Western Blot, Expressing, Single Particle, Fluorescence, Liposomes

Tumor-derived sEVs bind much more strongly to laminin than to fibronectin. (A) The diameters of sEVs, mEVs, and MVs derived from the 4175-LuT, PC3, BxPC3, HeLa, and SKBR3 cell lines were measured by qNano. (B) Single-particle fluorescence images of sEV-CD63Halo7-SF650T particles derived from the 4175-LuT, PC3, BxPC3, HeLa, and SKBR3 cell lines on glass coated with fibronectin or laminin. (C-E) The numbers of EV-CD63Halo7-SF650T particles (sEVs (C), mEVs (D), and MVs (E)) attached to glass coated with ECM components. The data are presented as the mean ± SE. (F) Western blotting of integrin subunits in sEVs, mEVs, and MVs derived from 4175-LuT, PC3, BxPC3, HeLa, and SKBR3 cells.

Journal: bioRxiv

Article Title: Extracellular vesicles adhere to cells predominantly through the interaction of CD151-associated integrin heterodimers and GM1 with laminin

doi: 10.1101/2024.04.11.589011

Figure Lengend Snippet: Tumor-derived sEVs bind much more strongly to laminin than to fibronectin. (A) The diameters of sEVs, mEVs, and MVs derived from the 4175-LuT, PC3, BxPC3, HeLa, and SKBR3 cell lines were measured by qNano. (B) Single-particle fluorescence images of sEV-CD63Halo7-SF650T particles derived from the 4175-LuT, PC3, BxPC3, HeLa, and SKBR3 cell lines on glass coated with fibronectin or laminin. (C-E) The numbers of EV-CD63Halo7-SF650T particles (sEVs (C), mEVs (D), and MVs (E)) attached to glass coated with ECM components. The data are presented as the mean ± SE. (F) Western blotting of integrin subunits in sEVs, mEVs, and MVs derived from 4175-LuT, PC3, BxPC3, HeLa, and SKBR3 cells.

Techniques: Derivative Assay, Single Particle, Fluorescence, Western Blot

Integrins β1 and α6 in sEVs and the extracellular matrix (ECM) are responsible for the binding of sEVs to cell plasma membranes. (A) Immunofluorescence images of fibronectin, collagen type I, and laminin in human normal embryonic lung fibroblast (MRC-5) cells and human bone marrow stromal (HS-5) cells. (B) The fluorescence intensities of laminin on cells in 1000 μm 2 . The data are presented as the mean ± SE. *p<0.01 by Welch’s t-test (two-sided). (C) Fluorescence images of MRC-5 cells expressing mCherry and sEV-CD63Halo7-SF650T particles (arrowhead) attached to cell membranes after 10, 20, and 30 min of incubation. sEVs isolated from the cell culture supernatant of intact PC3 cells (top panels) and from the cell culture supernatant of integrin β1 KO PC3 cells (bottom panels) bound to MRC-5 cells. (D) Fluorescence images of HS-5 cells and sEV-CD63Halo7-SF650T particles (arrowhead) attached to cell membranes after 30 min of incubation. sEVs were isolated from intact PC3 cells (top panels) and integrin β1 KO PC3 cells (bottom panels). (E) Fluorescence images of MRC-5 cells and the attached sEV-CD63Halo7-SF650T particles derived from intact PC3 cells (top panels) and from integrin α6 KO PC3 cells (bottom panels) after 30 min of incubation. (F-H) Time course of the numbers of intact sEVs and integrin β1-KO sEVs attached to the MRC-5 cell membrane ( n = 8 images) (F) and to the HS-5 cell membrane ( n = 15 images) (G) per 1000 μm 2 . (H) Time course of the numbers of intact sEVs and integrin α6 KO sEVs attached to the MRC-5 cell membrane per 1000 mm 2 ( n = 12 images). The data are presented as the mean ± SE.

Journal: bioRxiv

Article Title: Extracellular vesicles adhere to cells predominantly through the interaction of CD151-associated integrin heterodimers and GM1 with laminin

doi: 10.1101/2024.04.11.589011

Figure Lengend Snippet: Integrins β1 and α6 in sEVs and the extracellular matrix (ECM) are responsible for the binding of sEVs to cell plasma membranes. (A) Immunofluorescence images of fibronectin, collagen type I, and laminin in human normal embryonic lung fibroblast (MRC-5) cells and human bone marrow stromal (HS-5) cells. (B) The fluorescence intensities of laminin on cells in 1000 μm 2 . The data are presented as the mean ± SE. *p<0.01 by Welch’s t-test (two-sided). (C) Fluorescence images of MRC-5 cells expressing mCherry and sEV-CD63Halo7-SF650T particles (arrowhead) attached to cell membranes after 10, 20, and 30 min of incubation. sEVs isolated from the cell culture supernatant of intact PC3 cells (top panels) and from the cell culture supernatant of integrin β1 KO PC3 cells (bottom panels) bound to MRC-5 cells. (D) Fluorescence images of HS-5 cells and sEV-CD63Halo7-SF650T particles (arrowhead) attached to cell membranes after 30 min of incubation. sEVs were isolated from intact PC3 cells (top panels) and integrin β1 KO PC3 cells (bottom panels). (E) Fluorescence images of MRC-5 cells and the attached sEV-CD63Halo7-SF650T particles derived from intact PC3 cells (top panels) and from integrin α6 KO PC3 cells (bottom panels) after 30 min of incubation. (F-H) Time course of the numbers of intact sEVs and integrin β1-KO sEVs attached to the MRC-5 cell membrane ( n = 8 images) (F) and to the HS-5 cell membrane ( n = 15 images) (G) per 1000 μm 2 . (H) Time course of the numbers of intact sEVs and integrin α6 KO sEVs attached to the MRC-5 cell membrane per 1000 mm 2 ( n = 12 images). The data are presented as the mean ± SE.

Techniques: Binding Assay, Immunofluorescence, Fluorescence, Expressing, Incubation, Isolation, Cell Culture, Derivative Assay, Membrane

Talin-1 in sEVs does not regulate the binding affinity of integrins for laminin. (A) Western blot analysis of PC3 cell-derived sEVs after talin-1 KD by siRNA or overexpression of talin-1. (B, C, and D) The fluorescence images (B) and the numbers of PC3-sEVs attached to glass coated with laminin before and after (C) talin-1 KD or (D) overexpression of talin-1. Halo7-integrin β1 in sEVs was labeled with SF650T. (E, F, and G) The fluorescence images (E) and the numbers of CD63-labeled sEVs attached to glass coated with laminin before and after (F) talin-1 KD and (G) overexpression of talin-1. (H) Western blot analysis of the phosphorylation of Ser425 on talin-1 in PC3 cells and sEVs. Roscovitine: an inhibitor of CDK5 that phosphorylates Ser425 of talin-1.

Journal: bioRxiv

Article Title: Extracellular vesicles adhere to cells predominantly through the interaction of CD151-associated integrin heterodimers and GM1 with laminin

doi: 10.1101/2024.04.11.589011

Figure Lengend Snippet: Talin-1 in sEVs does not regulate the binding affinity of integrins for laminin. (A) Western blot analysis of PC3 cell-derived sEVs after talin-1 KD by siRNA or overexpression of talin-1. (B, C, and D) The fluorescence images (B) and the numbers of PC3-sEVs attached to glass coated with laminin before and after (C) talin-1 KD or (D) overexpression of talin-1. Halo7-integrin β1 in sEVs was labeled with SF650T. (E, F, and G) The fluorescence images (E) and the numbers of CD63-labeled sEVs attached to glass coated with laminin before and after (F) talin-1 KD and (G) overexpression of talin-1. (H) Western blot analysis of the phosphorylation of Ser425 on talin-1 in PC3 cells and sEVs. Roscovitine: an inhibitor of CDK5 that phosphorylates Ser425 of talin-1.

Techniques: Binding Assay, Western Blot, Derivative Assay, Over Expression, Fluorescence, Labeling

CD151 and cholesterol regulate the binding affinity of sEVs for laminin. (A) Fluorescence images of sEV-CD63Halo7-SF650T particles bound to laminin (LN) on glass before and after cholesterol depletion by MβCD and the numbers of attached sEVs per image (82 μm×82 μm). (B and C) The numbers of sEV-CD63-Halo7-SF650T particles attached to glass coated with laminin before and after treatment with saponin (B) and the addition of cholesterol by MβCD-cholesterol complex (C). (D) Fluorescence images of an MRC-5-GFP cell and sEV-CD63Halo7-SF650T particles on the MRC-5 cell after 30 min of incubation. (E and F) Time course of the number of sEV-CD63-Halo7-SF650T particles per 1000 μm 2 attached to the MRC-5 cell membrane before and after treatment with MβCD ( n = 16 cells) (E) or the MβCD-cholesterol complex ( n = 8 cells) (F). (G) Western blot analysis of CD151 and integrin subunits in PC3 cells and sEVs after CD151 KD. The amount of cell proteins loaded in one lane was 2.5 times greater than that of the sEVs in the other lane. (H) Images of wild-type (WT) PC3 cells and CD151-knockdown cells on glass coated with ECM components (fibronectin (FN), laminin (LN), or collagen type Ⅰ (COL1)) after 2 h of incubation. The areas of the cells were quantified. (I) Single-particle fluorescence images of sEV-CD63Halo7-SF650T particles bound to laminin (LN) on glass before and after CD151 was knocked down and cholesterol was depleted by MβCD (left). The number of attached sEVs increased (right). (J) The binding affinity ratio of cholesterol-depleted sEVs to intact sEVs was compared with that of CD151 KD sEVs. The data are presented as the mean ± SE. * indicates a significant difference (p<0.01) according to Welch’s t-test (two-sided).

Journal: bioRxiv

Article Title: Extracellular vesicles adhere to cells predominantly through the interaction of CD151-associated integrin heterodimers and GM1 with laminin

doi: 10.1101/2024.04.11.589011

Figure Lengend Snippet: CD151 and cholesterol regulate the binding affinity of sEVs for laminin. (A) Fluorescence images of sEV-CD63Halo7-SF650T particles bound to laminin (LN) on glass before and after cholesterol depletion by MβCD and the numbers of attached sEVs per image (82 μm×82 μm). (B and C) The numbers of sEV-CD63-Halo7-SF650T particles attached to glass coated with laminin before and after treatment with saponin (B) and the addition of cholesterol by MβCD-cholesterol complex (C). (D) Fluorescence images of an MRC-5-GFP cell and sEV-CD63Halo7-SF650T particles on the MRC-5 cell after 30 min of incubation. (E and F) Time course of the number of sEV-CD63-Halo7-SF650T particles per 1000 μm 2 attached to the MRC-5 cell membrane before and after treatment with MβCD ( n = 16 cells) (E) or the MβCD-cholesterol complex ( n = 8 cells) (F). (G) Western blot analysis of CD151 and integrin subunits in PC3 cells and sEVs after CD151 KD. The amount of cell proteins loaded in one lane was 2.5 times greater than that of the sEVs in the other lane. (H) Images of wild-type (WT) PC3 cells and CD151-knockdown cells on glass coated with ECM components (fibronectin (FN), laminin (LN), or collagen type Ⅰ (COL1)) after 2 h of incubation. The areas of the cells were quantified. (I) Single-particle fluorescence images of sEV-CD63Halo7-SF650T particles bound to laminin (LN) on glass before and after CD151 was knocked down and cholesterol was depleted by MβCD (left). The number of attached sEVs increased (right). (J) The binding affinity ratio of cholesterol-depleted sEVs to intact sEVs was compared with that of CD151 KD sEVs. The data are presented as the mean ± SE. * indicates a significant difference (p<0.01) according to Welch’s t-test (two-sided).

Techniques: Binding Assay, Fluorescence, Incubation, Membrane, Western Blot, Single Particle

Schematic model showing the binding of EVs to the recipient cell PM. (A) Integrin heterodimers in EVs, α6β1/α6β4 and α2β1, can bind to laminin and collagen type I, respectively, but integrin heterodimers in EVs, such as α5β1, bind only weakly to fibronectin. (B) Because Ser 425 of talin-1 is hardly phosphorylated in EVs, talin-1 is inactive and is not involved in promoting the ECM-binding activity of integrin heterodimers. (C) CD151 facilitates the binding of integrins α6β1 and α6β4 in sEVs to laminin. CD151 also links these integrins with tetraspanin-enriched membrane microdomains (TEMs) in a cholesterol-dependent manner. A molecule X in TEMs attenuates the binding of integrin heterodimers in EVs to laminin.

Journal: bioRxiv

Article Title: Extracellular vesicles adhere to cells predominantly through the interaction of CD151-associated integrin heterodimers and GM1 with laminin

doi: 10.1101/2024.04.11.589011

Figure Lengend Snippet: Schematic model showing the binding of EVs to the recipient cell PM. (A) Integrin heterodimers in EVs, α6β1/α6β4 and α2β1, can bind to laminin and collagen type I, respectively, but integrin heterodimers in EVs, such as α5β1, bind only weakly to fibronectin. (B) Because Ser 425 of talin-1 is hardly phosphorylated in EVs, talin-1 is inactive and is not involved in promoting the ECM-binding activity of integrin heterodimers. (C) CD151 facilitates the binding of integrins α6β1 and α6β4 in sEVs to laminin. CD151 also links these integrins with tetraspanin-enriched membrane microdomains (TEMs) in a cholesterol-dependent manner. A molecule X in TEMs attenuates the binding of integrin heterodimers in EVs to laminin.

Techniques: Binding Assay, Activity Assay, Membrane

(A) Western blot analysis of expressions of integrin subunits α V , β 1 and β 3 in HEK293(β 1 ) and HEK293(β 3 ) cell lines. (B) Confocal laser scanning microscopic images of HEK293(β 1 ) and HEK293(β 3 ) cells incubated for 30 min at 37°C in the presence of 0.1 μM Cy5-labeled RAFT-c(-RGDfK-) 4 , cRGD, or RAFT-c(-RβADfK) 4 . Nuclei were stained with Hoechst 33342 (blue), and fluorescence signal from Cy5 was pseudocolored red. Original objective: Plan-Neofluar 40x/1.30 Oil ph3.

Journal: Molecular Cancer

Article Title: In vivo optical imaging of integrin α V -β 3 in mice using multivalent or monovalent cRGD targeting vectors

doi: 10.1186/1476-4598-6-41

Figure Lengend Snippet: (A) Western blot analysis of expressions of integrin subunits α V , β 1 and β 3 in HEK293(β 1 ) and HEK293(β 3 ) cell lines. (B) Confocal laser scanning microscopic images of HEK293(β 1 ) and HEK293(β 3 ) cells incubated for 30 min at 37°C in the presence of 0.1 μM Cy5-labeled RAFT-c(-RGDfK-) 4 , cRGD, or RAFT-c(-RβADfK) 4 . Nuclei were stained with Hoechst 33342 (blue), and fluorescence signal from Cy5 was pseudocolored red. Original objective: Plan-Neofluar 40x/1.30 Oil ph3.

Article Snippet: The membranes were then incubated with primary antibody: rabbit anti-human integrin α V polyclonal antibody (1:5000; Chemicon International, Inc., Temecula, CA), rabbit anti-integrin β 1 tail serum (1:1500; kindly provided by Dr C. Albiges-Rizo, Grenoble, France) or mouse anti-human β 3 monoclonal antibody (clone VI-PL2, 1:100; BD Biosciences PharMingen, San Diego, CA).

Techniques: Western Blot, Incubation, Labeling, Staining, Fluorescence

Effect of GLUT4 on glucose concentration in the uterine fluid and endometrial receptivity following GLUT4-siRNA transfection. (A) Uterine fluid was collected on pregnant day 4 using in vivo uterine perfusion and glucose concentration in the uterine fluid was measured by HPLC. The glucose concentration in the GLUT4-siRNA side was obviously higher than that in the control side (4.12 ± 0.57 vs. 2.01 ± 0.29 mM, ∗ P < 0.05 vs. control, n = 12), but was still lower than that in blood (6.7 ± 0.72 mM). (B) Pinopode formation in the luminal epithelium was observed by SEM on pregnant day 4. Arrows indicate pinopodes. Scale bar , 30 μm. (C) Western blotting analysis for leukemia inhibitory factor (LIF) expression on pregnant day 4 following GLUT4-siRNA transfection. Relative density analysis of the LIF protein by Image Lab 3.0 software ( n = 3, normalized by β-actin). (D) Western blotting for integrin ανβ3 expression following GLUT4-siRNA transfection ( n = 3, normalized by β-actin). * P < 0.05 vs. control.

Journal: Frontiers in Physiology

Article Title: GLUT4 in Mouse Endometrial Epithelium: Roles in Embryonic Development and Implantation

doi: 10.3389/fphys.2021.674924

Figure Lengend Snippet: Effect of GLUT4 on glucose concentration in the uterine fluid and endometrial receptivity following GLUT4-siRNA transfection. (A) Uterine fluid was collected on pregnant day 4 using in vivo uterine perfusion and glucose concentration in the uterine fluid was measured by HPLC. The glucose concentration in the GLUT4-siRNA side was obviously higher than that in the control side (4.12 ± 0.57 vs. 2.01 ± 0.29 mM, ∗ P < 0.05 vs. control, n = 12), but was still lower than that in blood (6.7 ± 0.72 mM). (B) Pinopode formation in the luminal epithelium was observed by SEM on pregnant day 4. Arrows indicate pinopodes. Scale bar , 30 μm. (C) Western blotting analysis for leukemia inhibitory factor (LIF) expression on pregnant day 4 following GLUT4-siRNA transfection. Relative density analysis of the LIF protein by Image Lab 3.0 software ( n = 3, normalized by β-actin). (D) Western blotting for integrin ανβ3 expression following GLUT4-siRNA transfection ( n = 3, normalized by β-actin). * P < 0.05 vs. control.

Article Snippet: The membranes were blocked with 5% skim milk at room temperature for 2 h and incubated with rabbit anti-GLUT4 antibodies (1:1,000 dilution; ab33780, Abcam, United States), AMPK (1:600; ab131512, Abcam), p -AMPK (1:600; ab23875, Abcam), rabbit anti-integrin ανβ3 antibody (1:1,000 dilution; bs-1310R, Bioss, China), rabbit anti-LIF antibody (1:1,000 dilution; ab101228, Abcam, United States), and rabbit anti-β-actin (1:2,000 dilution; AF7018, Affinity, China) overnight at 4°C.

Techniques: Concentration Assay, Transfection, In Vivo, Western Blot, Expressing, Software

a Dot plots representing uptake of Alexa 647-labeled iRGD-AgNPs or control AgNPs by mCherry-labeled CAF spheroids. The bar diagram shows the proportion of CAFs that internalized the AgNPs. n = 4 independent experiments. Two-tailed unpaired t test; p = 0.0008. b Dot plots representing iRGD-AgNP uptake by mCherry-labeled CAF spheroids in the presence of anti-NRP-1, αvβ3, or αvβ5 antibodies or control IgG. The bar diagram shows the proportion of CAFs that internalized the AgNPs normalized against IgG. n = 4 (Rabbit IgG and NRP-1), n = 5 (Mouse IgG, αvβ3, and αvβ5) independent experiments. One-way ANOVA; p = 0.4784 (NRP-1 vs. αvβ3), p < 0.0001 (NRP-1 vs. αvβ5 and αvβ3 vs. αvβ5). c Representative confocal images from three independent experiments of GFP-positive hPCF1424 CAFs (green) treated with Alexa 647-labeled iRGD-AgNPs (red) in the presence of mouse IgG (left panels) or an anti-αvβ5 blocking antibody (right panels). The cells were etched to remove the AgNPs bound to the surface and highlight the internalized particles. Pre-etch and post-etch images are shown. Scale bars 100 µm. d Bar diagram showing the % expression of αvβ5 or NRP-1 in hPCF1424 CAFs transiently transfected with non-specific siRNA (NS), two different pools of siRNAs against integrin β5 (ITGb5-1 and -2), or NRP-1 siRNA (siNRP-1), as measured by median fluorescence intensity (left panel). Representative data of three biological replicates. e Bar diagram showing flow cytometric analysis of iRGD-AgNP uptake by the siRNA-treated CAFs in ( d ). The results are shown as the proportion of CAFs that internalized the AgNPs. n = 3 (NRP-1), n = 5 (ITGb5-1 and -2) independent experiments. One-way ANOVA; p < 0.0001 (NS vs. siITGb5-1 and NS vs. siITGb5-2), p = 0.9997 (NS vs. siNRP-1). All error bars, SEM. *** p < 0.001; **** p < 0.0001. Source data provided in Source Data file.

Journal: Nature Communications

Article Title: Tumor-penetrating therapy for β5 integrin-rich pancreas cancer

doi: 10.1038/s41467-021-21858-1

Figure Lengend Snippet: a Dot plots representing uptake of Alexa 647-labeled iRGD-AgNPs or control AgNPs by mCherry-labeled CAF spheroids. The bar diagram shows the proportion of CAFs that internalized the AgNPs. n = 4 independent experiments. Two-tailed unpaired t test; p = 0.0008. b Dot plots representing iRGD-AgNP uptake by mCherry-labeled CAF spheroids in the presence of anti-NRP-1, αvβ3, or αvβ5 antibodies or control IgG. The bar diagram shows the proportion of CAFs that internalized the AgNPs normalized against IgG. n = 4 (Rabbit IgG and NRP-1), n = 5 (Mouse IgG, αvβ3, and αvβ5) independent experiments. One-way ANOVA; p = 0.4784 (NRP-1 vs. αvβ3), p < 0.0001 (NRP-1 vs. αvβ5 and αvβ3 vs. αvβ5). c Representative confocal images from three independent experiments of GFP-positive hPCF1424 CAFs (green) treated with Alexa 647-labeled iRGD-AgNPs (red) in the presence of mouse IgG (left panels) or an anti-αvβ5 blocking antibody (right panels). The cells were etched to remove the AgNPs bound to the surface and highlight the internalized particles. Pre-etch and post-etch images are shown. Scale bars 100 µm. d Bar diagram showing the % expression of αvβ5 or NRP-1 in hPCF1424 CAFs transiently transfected with non-specific siRNA (NS), two different pools of siRNAs against integrin β5 (ITGb5-1 and -2), or NRP-1 siRNA (siNRP-1), as measured by median fluorescence intensity (left panel). Representative data of three biological replicates. e Bar diagram showing flow cytometric analysis of iRGD-AgNP uptake by the siRNA-treated CAFs in ( d ). The results are shown as the proportion of CAFs that internalized the AgNPs. n = 3 (NRP-1), n = 5 (ITGb5-1 and -2) independent experiments. One-way ANOVA; p < 0.0001 (NS vs. siITGb5-1 and NS vs. siITGb5-2), p = 0.9997 (NS vs. siNRP-1). All error bars, SEM. *** p < 0.001; **** p < 0.0001. Source data provided in Source Data file.

Article Snippet: The sections were treated with a rabbit anti-αvβ5 polyclonal antibody (1:200) (Cat. no. bs-1356R, BIOSS, Woburn, MA) or a rabbit polyclonal anti-cleaved caspase 3 antibody (1:250) (Cat. no. 9579S, Cell Signaling) at 4 °C overnight and incubated with ImmPRESS (IHC-P, rabbit, MP-7401) secondary antibody reagent (Vector, Burlingame, CA).

Techniques: Labeling, Two Tailed Test, Blocking Assay, Expressing, Transfection, Fluorescence

a Flow cytometry analysis showing entry of iRGD-AgNP or control AgNP into spheroids made of PC3 tumor cells alone or PC3 cells mixed with mCherry-labeled hPCF1424 CAFs (co-cult). Note that iRGD-AgNPs entered PC3 cells more efficiently in the presence of CAFs. b Quantified results of ( a ). Proportion of cells that internalized the particles are shown. n = 5 independent experiments. Two-tailed unpaired t test; p = 0.00015 (PC3 alone vs co-cult), p = 0.0177 (CAF alone vs. co-cult). c Flow cytometry analysis showing the expression of αvβ5 and αvβ3 integrins and NRP-1 in PC3 and CAF spheroids cultured alone (gray bars) or co-cultured with each other (black bars). n = 6 independent experiments. Two-tailed unpaired Student’s t test; p = 0.000325 (αvβ5: PC3 alone vs. co-cult), p = 0.0247 (αvβ5: CAF alone vs. co-cult), p = 0.0158 (αvβ3: PC3 alone vs. co-cult), p = 0.0132 (αvβ3: CAF alone vs. co-cult), p = 0.947 (NRP-1: PC3 alone vs. co-cult), p = 0.055 (CAF alone vs. co-cult). All error bars, SEM. * p < 0.05; *** p < 0.001. Source data provided in Source Data file.

Journal: Nature Communications

Article Title: Tumor-penetrating therapy for β5 integrin-rich pancreas cancer

doi: 10.1038/s41467-021-21858-1

Figure Lengend Snippet: a Flow cytometry analysis showing entry of iRGD-AgNP or control AgNP into spheroids made of PC3 tumor cells alone or PC3 cells mixed with mCherry-labeled hPCF1424 CAFs (co-cult). Note that iRGD-AgNPs entered PC3 cells more efficiently in the presence of CAFs. b Quantified results of ( a ). Proportion of cells that internalized the particles are shown. n = 5 independent experiments. Two-tailed unpaired t test; p = 0.00015 (PC3 alone vs co-cult), p = 0.0177 (CAF alone vs. co-cult). c Flow cytometry analysis showing the expression of αvβ5 and αvβ3 integrins and NRP-1 in PC3 and CAF spheroids cultured alone (gray bars) or co-cultured with each other (black bars). n = 6 independent experiments. Two-tailed unpaired Student’s t test; p = 0.000325 (αvβ5: PC3 alone vs. co-cult), p = 0.0247 (αvβ5: CAF alone vs. co-cult), p = 0.0158 (αvβ3: PC3 alone vs. co-cult), p = 0.0132 (αvβ3: CAF alone vs. co-cult), p = 0.947 (NRP-1: PC3 alone vs. co-cult), p = 0.055 (CAF alone vs. co-cult). All error bars, SEM. * p < 0.05; *** p < 0.001. Source data provided in Source Data file.

Techniques: Flow Cytometry, Labeling, Two Tailed Test, Expressing, Cell Culture

a Expression of αvβ5 integrin in PC3 cells after 2 days of incubation in normal media (NM) or CM prepared from cultured hPCF1424 CAFs ( n = 9), mPCFAA0779 CAFs ( n = 7), or MIA PaCa-2 human PDAC cells ( n = 4) performed in independent experiments. Fold over NM is shown. One-way ANOVA; p < 0.0001 (NM vs. hPCF1424 CM), p = 0.5085 (NM vs. mPCFAA0779 CM), p = 0.9886 (NM vs. MIA PaCa-2). b Dot plots representing iRGD-AgNP or control AgNP uptake in PC3 cells cultured in NM or CM from hPCF1424 CAFs. c The bar diagrams show the proportion of PC3 (left) or LM-PmC (right) cells that internalized iRGD-AgNPs. The cells were incubated in NM or CM from hPCF1424 CAFs for 2 days prior to study. n = 6 (PC3), n = 3 (LM-P) independent experiments. Two-tailed unpaired Student’s t test; p = 0.0001 (PC3 NM vs. CAF CM), p = 0.0127 (LM-P NM vs. CAF CM). d Expression of actin, αv, and β5 integrin mRNAs normalized against cyclophilin A analyzed by qPCR in PC3 cells incubated with NM or CM from hPCF1424 CAFs. n = 3 independent experiments. Two-tailed unpaired Student’s t test; p = 0.00016 (αv), p < 0.0001 (β5), p = 0.923 (actin). e , f Expression of αvβ5 integrin ( e ) or NRP-1 ( f ) in PC3 cells cultured in normal media (NM) or CM from hPCF1424 CAFs in the presence or absence of exogenous TGF-β, a TGF-β-specific inhibitor LY2157299, or vehicle alone. Mean fluorescence intensity (MFI) assessed by flow cytometry is shown. n = 4 independent experiments. Two-tailed unpaired Student’s t test; p = 0.0008 ( e: NM vs. TGF-β), p = 0.0009 ( e: TGF-β vs. TGF-β + LY2157299), p = 0.7082 ( e: CAF CM vs. CAF CM + DMSO), p = 0.0177 ( e: CAF CM + DMSO vs. CAF CM + LY2157299). No significant differences in ( f ). All error bars, SEM; * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001. Source data provided in Source Data file.

Journal: Nature Communications

Article Title: Tumor-penetrating therapy for β5 integrin-rich pancreas cancer

doi: 10.1038/s41467-021-21858-1

Figure Lengend Snippet: a Expression of αvβ5 integrin in PC3 cells after 2 days of incubation in normal media (NM) or CM prepared from cultured hPCF1424 CAFs ( n = 9), mPCFAA0779 CAFs ( n = 7), or MIA PaCa-2 human PDAC cells ( n = 4) performed in independent experiments. Fold over NM is shown. One-way ANOVA; p < 0.0001 (NM vs. hPCF1424 CM), p = 0.5085 (NM vs. mPCFAA0779 CM), p = 0.9886 (NM vs. MIA PaCa-2). b Dot plots representing iRGD-AgNP or control AgNP uptake in PC3 cells cultured in NM or CM from hPCF1424 CAFs. c The bar diagrams show the proportion of PC3 (left) or LM-PmC (right) cells that internalized iRGD-AgNPs. The cells were incubated in NM or CM from hPCF1424 CAFs for 2 days prior to study. n = 6 (PC3), n = 3 (LM-P) independent experiments. Two-tailed unpaired Student’s t test; p = 0.0001 (PC3 NM vs. CAF CM), p = 0.0127 (LM-P NM vs. CAF CM). d Expression of actin, αv, and β5 integrin mRNAs normalized against cyclophilin A analyzed by qPCR in PC3 cells incubated with NM or CM from hPCF1424 CAFs. n = 3 independent experiments. Two-tailed unpaired Student’s t test; p = 0.00016 (αv), p < 0.0001 (β5), p = 0.923 (actin). e , f Expression of αvβ5 integrin ( e ) or NRP-1 ( f ) in PC3 cells cultured in normal media (NM) or CM from hPCF1424 CAFs in the presence or absence of exogenous TGF-β, a TGF-β-specific inhibitor LY2157299, or vehicle alone. Mean fluorescence intensity (MFI) assessed by flow cytometry is shown. n = 4 independent experiments. Two-tailed unpaired Student’s t test; p = 0.0008 ( e: NM vs. TGF-β), p = 0.0009 ( e: TGF-β vs. TGF-β + LY2157299), p = 0.7082 ( e: CAF CM vs. CAF CM + DMSO), p = 0.0177 ( e: CAF CM + DMSO vs. CAF CM + LY2157299). No significant differences in ( f ). All error bars, SEM; * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001. Source data provided in Source Data file.

Techniques: Expressing, Incubation, Cell Culture, Two Tailed Test, Fluorescence, Flow Cytometry

Review

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1) Product Images from "Role of Periostin in the Development of Nasal Hyperresponsiveness in Mice with Allergic Rhinitis"

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