Journal: Virology Journal

Article Title: Examination of soluble integrin resistant mutants of foot-and-mouth disease virus

doi: 10.1186/1743-422X-10-2

Figure Lengend Snippet: Integrin expression profile. BHK-21, CHO 677, and LFBK cell lysates were examined by Western blot probing with: anti-β 3 integrin (ITGβ3), anti-β 6 integrin (ITGβ6), and anti-RHA. Equivalent loading between lanes was confirmed by probing with anti-tubulin-α. Molecular weight ladder bands are indicated.

Article Snippet: Mouse monoclonal anti-β 3 integrin (ITGβ3) was purchased from Abcam (Cambridge, MA).

Techniques: Expressing, Western Blot, Molecular Weight

Journal: PLoS ONE

Article Title: A Novel Cryptic Binding Motif, LRSKSRSFQVSDEQY, in the C-Terminal Fragment of MMP-3/7-Cleaved Osteopontin as a Novel Ligand for α9β1 Integrin Is Involved in the Anti-Type II Collagen Antibody-Induced Arthritis

doi: 10.1371/journal.pone.0116210

Figure Lengend Snippet: A. Binding of LRS-TDE peptide to B16-BL6 cells in the presence of Mn 2+ ions or EDTA. B16-BL6 cells were plated onto dishes coated with LRS-TDE peptide as described in . B. Binding of LRS-TDE peptide (5 µg/mL) to B16-BL6 cells in the presence of antibodies (10 µg/mL) for various integrins or OPN. C. Surface expression of α9β1 integrin on B16-BL6 cells. Shaded peak represents cells stained with control antibody, and open peak represents cells stained with anti-α9β1 integrin (55A2C). D. Binding of SVVYGLR (5 µg/mL) or LRS-TDE peptide (5 µg/mL) to NIH3T3 cells expressing mouse α9 integrin (α9/NIH) or mouse α4 integrin (α4/NIH). E. Surface expression of CD44 on α4/NIH cells or B16-BL6 cells. Shaded peak represents cells stained with control antibody (rat IgG2a), and open peak represents cells stained with anti-CD44 (KM81). F. Binding of LRS-TDE peptide to B16-BL6 cells in the presence of antibodies (20 µg/mL) for CD44 or control Ig (rat IgG2a).

Article Snippet: Anti-β1 integrin (HMβ1-1) antibody, anti-β3 integrin (2C9.G2) antibody, anti-α1 integrin (Ha31/8) antibody, anti-α2 integrin (HMα2) antibody, anti-α4 integrin (R1-2) antibody, anti-α5 integrin (HMα5) antibody, anti-αv integrin (RMV-7), and anti-αL integrin (M17/4) were obtained from BD Bioscience.

Techniques: Binding Assay, Expressing, Staining

Journal: PLoS ONE

Article Title: A Novel Cryptic Binding Motif, LRSKSRSFQVSDEQY, in the C-Terminal Fragment of MMP-3/7-Cleaved Osteopontin as a Novel Ligand for α9β1 Integrin Is Involved in the Anti-Type II Collagen Antibody-Induced Arthritis

doi: 10.1371/journal.pone.0116210

Figure Lengend Snippet: A. α9/NIH cells were plated onto dishes coated with GRGDS, GDSLAYGLR, or LRS-TDE peptides (10 µg/mL), scratched with the tip of a pipette, and allowed to migrate into wound spaces for 15 h. * P <0.05 versus BSA, one-way ANOVA followed by Student's t test with Bonferroni's correction. Data are presented as means ±SEM from three independent experiments. B. Effect of GRGDS, GDSLAYGLR, or LRS-TDE peptides (10 µg/mL) on α9/NIH cells proliferation assessed by the colorimetric assay (WST-8) for the quantification of cell proliferation. C. α9/NIH cells were incubated with control Ig (Hamster IgG) or anti-α9β1 integrin (55A2C) antibody (10 µg/mL). Cells that had migrated into the scratch area were counted. ** P <0.005 versus control Ig, Student's t test. Data are presented as means ±SEM from three independent experiments.

Article Snippet: Anti-β1 integrin (HMβ1-1) antibody, anti-β3 integrin (2C9.G2) antibody, anti-α1 integrin (Ha31/8) antibody, anti-α2 integrin (HMα2) antibody, anti-α4 integrin (R1-2) antibody, anti-α5 integrin (HMα5) antibody, anti-αv integrin (RMV-7), and anti-αL integrin (M17/4) were obtained from BD Bioscience.

Techniques: Transferring, Colorimetric Assay, Incubation

Journal:

Article Title: Physiological levels of tumstatin, a fragment of collagen IV ?3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via ?V?3 integrin

doi:

Figure Lengend Snippet: A: Proliferation assay in β3 integrin−/− endothelial cells. MLEC were isolated from wild-type (β3+/+) and β3 integrin−/− (β3−/−) mice as previously described (Maeshima et al., 2002). Proliferation was assessed by [3H]-thymidine incorporation. All groups represent triplicate analyses. The results are shown as the mean ± SEM. ** indicates p < 0.01; compared to control cells.

Article Snippet: They were incubated with various primary antibodies, i.e., rat anti-mouse CD31 (Pharmingen), rabbit anti-von Willebrand Factor (vWF) (Dako), rat anti-β1 integrin (Pharmingen), and hamster anti-β3 integrin (Pharmingen) antibodies at room temperature for 2 hr.

Techniques: Proliferation Assay, Isolation

Journal:

Article Title: Physiological levels of tumstatin, a fragment of collagen IV ?3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via ?V?3 integrin

doi:

Figure Lengend Snippet: A: Immunohistochemical staining with anti-β3 integrin (β3) antibody and CD31 or vWF was performed to assess localization of β3 integrin in blood vessels. Anti-CD31 antibody was used for the tumor and skin tissues and anti-vWF antibody was used for the liver tissue. β3 integrin-positive blood vessels (merge) are indicated with arrows. Scale bar: 50 μm.

Article Snippet: They were incubated with various primary antibodies, i.e., rat anti-mouse CD31 (Pharmingen), rabbit anti-von Willebrand Factor (vWF) (Dako), rat anti-β1 integrin (Pharmingen), and hamster anti-β3 integrin (Pharmingen) antibodies at room temperature for 2 hr.

Techniques: Immunohistochemical staining, Staining

Journal:

Article Title: Physiological levels of tumstatin, a fragment of collagen IV ?3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via ?V?3 integrin

doi:

Figure Lengend Snippet: A: Immunohistochemical staining with anti-β3 integrin (β3) antibody and CD31 was performed to assess localization of β3 integrin in the tumor blood vessels with volumes of 0.1, 0.5 and 3.0 cm3 in wild-type mice. β3 integrin-positive blood vessels (merge) are indicated with arrows. Scale bar: 50 μm.

Article Snippet: They were incubated with various primary antibodies, i.e., rat anti-mouse CD31 (Pharmingen), rabbit anti-von Willebrand Factor (vWF) (Dako), rat anti-β1 integrin (Pharmingen), and hamster anti-β3 integrin (Pharmingen) antibodies at room temperature for 2 hr.

Techniques: Immunohistochemical staining, Staining

Journal: PLoS ONE

Article Title: Vascular Smooth Muscle Cells Stimulate Platelets and Facilitate Thrombus Formation through Platelet CLEC-2: Implications in Atherothrombosis

doi: 10.1371/journal.pone.0139357

Figure Lengend Snippet: A) Different concentrations of His-S100A13 were flowed over an immobilized hCLEC-2-rFc2 or a control rFc2-coated surface. The arrows indicate the beginning and the end of perfusion of S100A13. The results from one experiment are shown that is representative of the other three. RU indicates resonance units. B) (i) Platelets spreading on the surface of BSA, collagen, or S100A13 were investigated. (ii) Magnified images of adhered WT platelets on the surfaces coated with BSA or recombinant S100A13. (iii) Quantification of adherent platelets in the images in (i). Adherent platelets were counted. C) Western blotting with anti-S100A13 or anti-β3 integrin antibody. Plt represents platelets. The data are representative of three experiments.

Article Snippet: CASMCs (5 × 10 6 /mL), washed human platelets (1 × 10 /mL), or recombinant His-tagged S100A13 protein (1 μg/mL) were separated by electrophoresis[ ] and western blotted with rabbit monoclonal anti-S100A13 antibody (Epitomics) or anti-β3 integrin antibody (Clone 1, BD Biosciences).

Techniques: Recombinant, Western Blot