◀ Back to ITGA5
ITGA5 — ITGB1
Pathways - manually collected, often from reviews:
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OpenBEL Selventa BEL large corpus:
Complex of ITGA5-ITGB1
→
TNF
(increases)
Evidence: alpha2beta1 is upregulated by VEGF, alphaVbeta3 and alpha5beta1 are not, but instead are induced by bFGF, TNF and other angiogenic cytokines
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OpenBEL Selventa BEL large corpus:
Complex of FN1-ITGA5-ITGB1
→
VEGFA
(increases)
Evidence: The data in Figure 1D suggested that a second aV integ- rin, aVb5, which has been implicated in angiogenesis, may also be activated by VEGF165. Therefore, we sought concento determine if still other integrins implicated in angio- genesis, a5b1, a fibronectin receptor (Bloch et al., 1997), and a2b1, a collagen receptor (Senger et al., 1997), might be activated by VEGF165. In cell migration assays, VEGF165 markedly stimulated HUVEC movement onto effibronectin (see Figure 3A). The migrating cells e...
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OpenBEL Selventa BEL large corpus:
Complex of ITGA5-ITGB1
→
VEGFA
(increases, VEGFA Activity)
Evidence: The data in Figure 1D suggested that a second aV integ- rin, aVb5, which has been implicated in angiogenesis, may also be activated by VEGF165. Therefore, we sought concento determine if still other integrins implicated in angio- genesis, a5b1, a fibronectin receptor (Bloch et al., 1997), and a2b1, a collagen receptor (Senger et al., 1997), might be activated by VEGF165. In cell migration assays, VEGF165 markedly stimulated HUVEC movement onto effibronectin (see Figure 3A). The migrating cells e...
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OpenBEL Selventa BEL large corpus:
Complex of ITGA5-ITGB1
→
VEGFA
(increases, VEGFA Activity)
Evidence: VEGF enhanced cell adhesion, migration, soluble ligand binding, and adenovirus gene transfer mediated by alphavbeta3 and also activated other integrins, alphavbeta5, alpha5beta1, and alpha2beta1, involved in angiogenesis. The major findings of our studies are as follows. First, VEGF165 can activate integrin aVb3, leading to enhanced adhesion of endothelial cells to a variety of ligands.
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OpenBEL Selventa BEL large corpus:
Complex of ITGA5-ITGB1
→
VEGFA
(increases, VEGFA Activity)
Evidence: Fifth, VEGF165 activation is not targeted to a single integrin; b1 integrins, as exemplified by a5b1 and a2b1, also are affected by VEGF165 stimulation. In addition, our data suggest that aVb5 can be activated by the growth factor.
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OpenBEL Selventa BEL large corpus:
Complex of FN1-ITGA5-ITGB1
→
Complex of ITGA5-ITGB1
(directlyIncreases, FN1/ITGA5/ITGB1 Activity)
Evidence: The data in Figure 1D suggested that a second aV integ- rin, aVb5, which has been implicated in angiogenesis, may also be activated by VEGF165. Therefore, we sought concento determine if still other integrins implicated in angio- genesis, a5b1, a fibronectin receptor (Bloch et al., 1997), and a2b1, a collagen receptor (Senger et al., 1997), might be activated by VEGF165. In cell migration assays, VEGF165 markedly stimulated HUVEC movement onto effibronectin (see Figure 3A). The migrating cells e...
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OpenBEL Selventa BEL large corpus:
CDC42
→
Complex of ITGA5-ITGB1
(increases)
Bao et al., Mol Cell Biol 2002*
Evidence: Cell attachment to fibronectin activated Cdc42 within 20 minutes in ECV 304 cells by an integrin-dependent manner. Attachment through ITGA5.ITGB1 to fibronectin activated Cdc42 thereby increasing the proteolysis of CDKN1A. Transient overexpression of N17Cdc42 blocked the reduction of CDKN1A caused by adhesion to fibronectin, indicating that integrin-induced signaling through Cdc42 increases the proteolysis of CDKN1A.
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OpenBEL Selventa BEL large corpus:
EGFR
→
Complex of ITGA5-ITGB1
(increases, ITGA5/ITGB1 Activity, EGFR Activity)
Giancotti et al., Science 1999
Evidence: The receptors for insulin, plateletderived growth factor (PDGF), epidermal growth factor (EGF), and vascular endothelial growth factor (VEGF) are optimally activated by their ligands only under appropriate cell attachment conditions (24-28). Although a systematic analysis has not been conducted, certain integrins appear to be preferentially associated with specific growth factor receptors. Thus, the avb3 integrin can be immunoprecipitated in complexes with the insulin, PDGF, and VEGF receptors (...
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OpenBEL Selventa BEL large corpus:
IL1B
→
Complex of ITGA5-ITGB1
(increases, IL1B Activity)
Evidence: Ligation of alpha 5 beta 1 using activating mAb JBS5 (which acts as agonist similar to FN N-terminal fragment) up-regulates the inflammatory mediators such as NO and PGE2 as well as the cytokines, IL-6 and IL-8. Furthermore, up-regulation of these proinflammatory mediators by alpha 5 beta1 integrin ligation is mediated via induction and autocrine production of IL-1 beta, because type II soluble IL-1 decoy receptor inhibits their production.
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OpenBEL Selventa BEL large corpus:
IL6
→
Complex of ITGA5-ITGB1
(increases, IL6 Activity)
Evidence: Ligation of alpha 5 beta 1 using activating mAb JBS5 (which acts as agonist similar to FN N-terminal fragment) up-regulates the inflammatory mediators such as NO and PGE2 as well as the cytokines, IL-6 and IL-8. Furthermore, up-regulation of these proinflammatory mediators by alpha 5 beta1 integrin ligation is mediated via induction and autocrine production of IL-1 beta, because type II soluble IL-1 decoy receptor inhibits their production.
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OpenBEL Selventa BEL large corpus:
MAPK1
→
Complex of ITGA5-ITGB1
(increases, ITGA5/ITGB1 Activity)
Bao et al., Mol Cell Biol 2002*
Evidence: Cell attachment to fibronectin through ITGA5.ITGB1 activated the phosphorylation of ERK-2 within 60 minutes. ERK-2 activation was detected even in the presence of dn Cdc42 or dn Rac1 after attachment to fibronectin, indicating that these integrin-induced signaling components are still activated by attachment when Cdc42 and Rac1 are blocked.
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OpenBEL Selventa BEL large corpus:
MAPK1
→
Complex of ITGA5-ITGB1
(increases)
Bao et al., Mol Cell Biol 2002*
Evidence: Cell attachment to fibronectin through ITGA5.ITGB1 activated the phosphorylation of ERK-2 within 60 minutes. ERK-2 activation was detected even in the presence of dn Cdc42 or dn Rac1 after attachment to fibronectin, indicating that these integrin-induced signaling components are still activated by attachment when Cdc42 and Rac1 are blocked.
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OpenBEL Selventa BEL large corpus:
MAPK3
→
Complex of ITGA5-ITGB1
(increases, ITGA5/ITGB1 Activity)
Bao et al., Mol Cell Biol 2002*
Evidence: Cell attachment to fibronectin through ITGA5.ITGB1 activated the phosphorylation of ERK-1 within 60 minutes. ERK-1 activation was detected even in the presence of dn Cdc42 or dn Rac1 after attachment to fibronectin, indicating that these integrin-induced signaling components are still activated by attachment when Cdc42 and Rac1 are blocked.
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OpenBEL Selventa BEL large corpus:
PRKCA
→
Complex of ITGA5-ITGB1
(increases, ITGA5/ITGB1 Activity, PRKCA Activity)
Podar et al., J Biol Chem 2002*
Evidence: these data show that activation of PI 3-kinase is an early event in the VEGF-triggered Flt-1 signaling cascade...These results indicate that VEGF-induced PI 3-kinase activation along with b1 integrin binding to fibronectin activate PKCa.
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OpenBEL Selventa BEL large corpus:
PTK2
→
Complex of ITGA5-ITGB1
(increases, ITGA5/ITGB1 Activity)
Bao et al., Mol Cell Biol 2002*
Evidence: Upon attachment to fibronectin, ECV 304 cells transfected with dn Cdc42 or dn Rac1 mutants exhibited the phosphorylated form of FAK. FAK phosphorylated at Tyr397 appeared within 60 minutes and was detected even in the presence of dn Cdc42 or dn Rac1, indicating that these integrin-induced signaling components are still activated by attachment when Cdc42 and Rac1 are blocked.
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OpenBEL Selventa BEL large corpus:
Complex of FN1-ITGA5-ITGB1
→
CXCR4
(increases, FN1/ITGA5/ITGB1 Activity)
Robledo et al., J Biol Chem 2001*
Evidence: Furthermore, the chemokine SDF-1alpha, the ligand of CXCR4, triggered modulation of beta(1) integrin-dependent melanoma cell adhesion to fibronectin.
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OpenBEL Selventa BEL large corpus:
Complex of ITGA5-ITGB1
→
FGF2
(increases)
Evidence: alpha2beta1 is upregulated by VEGF, alphaVbeta3 and alpha5beta1 are not, but instead are induced by bFGF, TNF and other angiogenic cytokines
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OpenBEL Selventa BEL large corpus:
Complex of ITGA5-ITGB1
→
FN1
(directlyIncreases, FN1 Activity)
Giancotti et al., Science 1999
Evidence: The a5b1 integrin, which binds to fibronectin, induces expression of the antiapoptotic protein Bcl-2, protecting cells from apoptosis from stresses such as the lack of growth factors (55). Other integrins, including another fibronectin receptor, avb1, do not provide this survival effect. The avb3 integrin promotes endothelial and melanoma cell survival; this effect correlates with suppression of the p53 pathway and activation of the nuclear factor kappa B transcription factor (56). The activatio...
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KEGG Focal adhesion:
ACTN1/ACTN2/ACTN3/ACTN4
→
Complex of 21 proteins
(protein-protein, binding/association)
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KEGG Focal adhesion:
FLNA/FLNB/FLNC
→
Complex of 21 proteins
(protein-protein, binding/association)
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KEGG Focal adhesion:
TLN1/TLN2
→
Complex of 21 proteins
(protein-protein, binding/association)
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KEGG Focal adhesion:
PXN
→
Complex of 21 proteins
(protein-protein, binding/association)
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KEGG Focal adhesion:
VASP
→
Complex of 21 proteins
(protein-protein, binding/association)
-
KEGG Focal adhesion:
PARVA/PARVB/PARVG
→
Complex of 21 proteins
(protein-protein, binding/association)
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KEGG Focal adhesion:
CHAD/COL11A1/COL11A2/COL1A1/COL1A2/COL2A1/COL3A1/COL4A1/COL4A2/COL4A4/COL4A5/COL4A6/COL5A1/COL5A2/COL5A3/COL6A1/COL6A2/COL6A3/COL6A6/COMP/FN1/IBSP/LAMA1/LAMA2/LAMA3/LAMA4/LAMA5/LAMB1/LAMB2/LAMB3/LAMB4/LAMC1/LAMC2/LAMC3/RELN/SPP1/THBS1/THBS2/THBS3/THBS4/TNC/TNN/TNR/TNXB/VTN/VWF
→
Complex of 21 proteins
(protein-protein, activation)
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KEGG ECM-receptor interaction:
FN1
→
Complex of ITGA5-ITGB1
(protein-protein, activation)
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KEGG Dilated cardiomyopathy:
Complex of 21 proteins
→
ACTB/ACTG1
(protein-protein, binding/association)
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NCI Pathway Database Urokinase-type plasminogen activator (uPA) and uPAR-mediated signaling:
uPA/uPAR/alpha5/beta1 Integrin complex (PLAUR-PLAU-ITGA5-ITGB1)
→
uPA/uPAR/alpha5/beta1 Integrin/Fibronectin complex (PLAUR-FN1-PLAU-ITGA5-ITGB1)
(modification, collaborate)
Simon et al., J Biol Chem 2000, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database Urokinase-type plasminogen activator (uPA) and uPAR-mediated signaling:
uPA/uPAR/alpha5/beta1 Integrin complex (PLAUR-PLAU-ITGA5-ITGB1)
→
Fibronectin complex (FN1)
(modification, collaborate)
Simon et al., J Biol Chem 2000, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database Urokinase-type plasminogen activator (uPA) and uPAR-mediated signaling:
uPA/uPAR/alpha5/beta1 Integrin/Fibronectin complex (PLAUR-FN1-PLAU-ITGA5-ITGB1)
→
Fibronectin complex (FN1)
(modification, collaborate)
Simon et al., J Biol Chem 2000, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database Signaling events mediated by focal adhesion kinase:
Talin (TLN1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, activates)
Michael et al., Mol Biol Cell 2009*, Chen et al., J Biol Chem 1995*
Evidence: assay, physical interaction
-
NCI Pathway Database Signaling events mediated by focal adhesion kinase:
FAK (PTK2)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, activates)
Michael et al., Mol Biol Cell 2009*, Chen et al., J Biol Chem 1995*
Evidence: assay, physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
uPA/uPAR/alpha5/beta1 Integrin complex (PLAUR-PLAU-ITGA5-ITGB1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Monaghan et al., J Biol Chem 2004*, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007, Wei et al., Science 1996
Evidence: physical interaction
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NCI Pathway Database Beta1 integrin cell surface interactions:
uPA/uPAR/alpha5/beta1 Integrin complex (PLAUR-PLAU-ITGA5-ITGB1)
→
uPA/uPAR complex (PLAUR-PLAU)
(modification, collaborate)
Monaghan et al., J Biol Chem 2004*, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007, Wei et al., Science 1996
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
→
uPA/uPAR complex (PLAUR-PLAU)
(modification, collaborate)
Monaghan et al., J Biol Chem 2004*, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007, Wei et al., Science 1996
Evidence: physical interaction
-
NCI Pathway Database Urokinase-type plasminogen activator (uPA) and uPAR-mediated signaling:
uPA/uPAR/alpha5/beta1 Integrin complex (PLAUR-PLAU-ITGA5-ITGB1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Monaghan et al., J Biol Chem 2004*, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007, Wei et al., Science 1996
Evidence: physical interaction
-
NCI Pathway Database Urokinase-type plasminogen activator (uPA) and uPAR-mediated signaling:
uPA/uPAR/alpha5/beta1 Integrin complex (PLAUR-PLAU-ITGA5-ITGB1)
→
uPA/uPAR complex (PLAUR-PLAU)
(modification, collaborate)
Monaghan et al., J Biol Chem 2004*, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007, Wei et al., Science 1996
Evidence: physical interaction
-
NCI Pathway Database Urokinase-type plasminogen activator (uPA) and uPAR-mediated signaling:
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
→
uPA/uPAR complex (PLAUR-PLAU)
(modification, collaborate)
Monaghan et al., J Biol Chem 2004*, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007, Wei et al., Science 1996
Evidence: physical interaction
-
NCI Pathway Database Syndecan-2-mediated signaling events:
Syndecan-2 (SDC2)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(positive regulation of stress fiber assembly, collaborate)
Kusano et al., Exp Cell Res 2000*
Evidence: mutant phenotype, assay, other species
-
NCI Pathway Database Beta1 integrin cell surface interactions:
Fibrinogen complex (FGA-FGG-FGB)
→
alpha5/beta1 Integrin/Fibrinogen complex (ITGA5-ITGB1-FGB-FGA-FGG)
(modification, collaborate)
Podolnikova et al., J Biol Chem 2003, Suehiro et al., J Biol Chem 1997
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
Fibrinogen complex (FGA-FGG-FGB)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Podolnikova et al., J Biol Chem 2003, Suehiro et al., J Biol Chem 1997
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
alpha5/beta1 Integrin/Fibrinogen complex (ITGA5-ITGB1-FGB-FGA-FGG)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Podolnikova et al., J Biol Chem 2003, Suehiro et al., J Biol Chem 1997
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
alpha5/beta1 Integrin/Fibrillin-1 complex (FBN1-ITGA5-ITGB1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Bax et al., J Biol Chem 2003, Jovanovic et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
alpha5/beta1 Integrin/Fibrillin-1 complex (FBN1-ITGA5-ITGB1)
→
Fibrillin-1 (FBN1)
(modification, collaborate)
Bax et al., J Biol Chem 2003, Jovanovic et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
→
Fibrillin-1 (FBN1)
(modification, collaborate)
Bax et al., J Biol Chem 2003, Jovanovic et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
Tie2/Ang1 complex (ANGPT1-TEK)
→
Tie2/Ang1/alpha5/beta1 Integrin complex (ANGPT1-TEK-ITGA5-ITGB1)
(modification, collaborate)
Lee et al., Mol Cancer Res 2006
Evidence: mutant phenotype, physical interaction, other species
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
Tie2/Ang1 complex (ANGPT1-TEK)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Lee et al., Mol Cancer Res 2006
Evidence: mutant phenotype, physical interaction, other species
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
Tie2/Ang1/alpha5/beta1 Integrin complex (ANGPT1-TEK-ITGA5-ITGB1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Lee et al., Mol Cancer Res 2006
Evidence: mutant phenotype, physical interaction, other species
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
Fibronectin complex (FN1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, activates)
Lee et al., Mol Cancer Res 2006
Evidence: mutant phenotype, physical interaction, other species
-
NCI Pathway Database Beta1 integrin cell surface interactions:
Fibronectin complex (FN1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Mould et al., J Biol Chem 2002*, García et al., Biochemistry 2002*, Maschler et al., Oncogene 2005, Peng et al., J Immunol 2005, Takada et al., Nature 1987*, Hemler et al., J Biol Chem 1987, Lange et al., Exp Cell Res 1994, Lange et al., Exp Dermatol 1995, Mould et al., J Biol Chem 1995*, Mould et al., Biochem Soc Trans 1995*
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
Fibronectin complex (FN1)
→
alpha5/beta1 Integrin/Fibronectin complex (ITGA5-ITGB1-FN1)
(modification, collaborate)
Mould et al., J Biol Chem 2002*, García et al., Biochemistry 2002*, Maschler et al., Oncogene 2005, Peng et al., J Immunol 2005, Takada et al., Nature 1987*, Hemler et al., J Biol Chem 1987, Lange et al., Exp Cell Res 1994, Lange et al., Exp Dermatol 1995, Mould et al., J Biol Chem 1995*, Mould et al., Biochem Soc Trans 1995*
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
→
alpha5/beta1 Integrin/Fibronectin complex (ITGA5-ITGB1-FN1)
(modification, collaborate)
Mould et al., J Biol Chem 2002*, García et al., Biochemistry 2002*, Maschler et al., Oncogene 2005, Peng et al., J Immunol 2005, Takada et al., Nature 1987*, Hemler et al., J Biol Chem 1987, Lange et al., Exp Cell Res 1994, Lange et al., Exp Dermatol 1995, Mould et al., J Biol Chem 1995*, Mould et al., Biochem Soc Trans 1995*
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
alpha5/beta1 Integrin/COL18A1 complex (COL18A1-ITGA5-ITGB1)
→
COL18A1 (COL18A1)
(modification, collaborate)
Sudhakar et al., Proc Natl Acad Sci U S A 2003
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
alpha5/beta1 Integrin/COL18A1 complex (COL18A1-ITGA5-ITGB1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Sudhakar et al., Proc Natl Acad Sci U S A 2003
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
COL18A1 (COL18A1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Sudhakar et al., Proc Natl Acad Sci U S A 2003
Evidence: physical interaction
-
NCI Pathway Database Syndecan-4-mediated signaling events:
Fibronectin complex (FN1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, activates)
Woods et al., Arch Biochem Biophys 2000, Tumova et al., J Biol Chem 2000, Mahalingam et al., J Biol Chem 2007, Bass et al., J Cell Biol 2007
Evidence: mutant phenotype, assay
-
NCI Pathway Database Syndecan-4-mediated signaling events:
RAC1/GDP complex (RAC1)
→
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
(modification, collaborate)
Woods et al., Arch Biochem Biophys 2000, Tumova et al., J Biol Chem 2000, Mahalingam et al., J Biol Chem 2007, Bass et al., J Cell Biol 2007
Evidence: mutant phenotype, assay
-
NCI Pathway Database Syndecan-4-mediated signaling events:
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
→
Syndecan-4 (SDC4)
(modification, activates)
Woods et al., Arch Biochem Biophys 2000, Tumova et al., J Biol Chem 2000, Mahalingam et al., J Biol Chem 2007, Bass et al., J Cell Biol 2007
Evidence: mutant phenotype, assay
-
NCI Pathway Database Syndecan-4-mediated signaling events:
alpha5/beta1 Integrin complex (ITGA5-ITGB1)
→
PKC alpha (PRKCA)
(modification, activates)
Woods et al., Arch Biochem Biophys 2000, Tumova et al., J Biol Chem 2000, Mahalingam et al., J Biol Chem 2007, Bass et al., J Cell Biol 2007
Evidence: mutant phenotype, assay
-
NCI Pathway Database Beta1 integrin cell surface interactions:
uPA/uPAR/alpha5/beta1 Integrin complex (PLAUR-PLAU-ITGA5-ITGB1)
→
uPA/uPAR/alpha5/beta1 Integrin/Fibronectin complex (PLAUR-FN1-PLAU-ITGA5-ITGB1)
(modification, collaborate)
Simon et al., J Biol Chem 2000, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
uPA/uPAR/alpha5/beta1 Integrin complex (PLAUR-PLAU-ITGA5-ITGB1)
→
Fibronectin complex (FN1)
(modification, collaborate)
Simon et al., J Biol Chem 2000, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database Beta1 integrin cell surface interactions:
uPA/uPAR/alpha5/beta1 Integrin/Fibronectin complex (PLAUR-FN1-PLAU-ITGA5-ITGB1)
→
Fibronectin complex (FN1)
(modification, collaborate)
Simon et al., J Biol Chem 2000, Wei et al., J Cell Biol 2005, Chaurasia et al., J Biol Chem 2006, Wei et al., J Biol Chem 2007
Evidence: physical interaction
-
NCI Pathway Database VEGFR3 signaling in lymphatic endothelium:
VEGFR3/VEGFD complex (FLT4-FIGF)
→
alpha5/beta1 Integrin/Fibronectin complex (ITGA5-ITGB1-FN1)
(modification, collaborate)
Wang et al., J Biol Chem 2001
Evidence: mutant phenotype, assay
-
NCI Pathway Database VEGFR3 signaling in lymphatic endothelium:
VEGFR3/VEGFD complex (FLT4-FIGF)
→
VEGFR3/VEGFD/Fibronectin/alpha5/beta1 Integrin complex (FIGF-FLT4-FN1-ITGA5-ITGB1)
(modification, collaborate)
Wang et al., J Biol Chem 2001
Evidence: mutant phenotype, assay
-
NCI Pathway Database VEGFR3 signaling in lymphatic endothelium:
alpha5/beta1 Integrin/Fibronectin complex (ITGA5-ITGB1-FN1)
→
VEGFR3/VEGFD/Fibronectin/alpha5/beta1 Integrin complex (FIGF-FLT4-FN1-ITGA5-ITGB1)
(modification, collaborate)
Wang et al., J Biol Chem 2001
Evidence: mutant phenotype, assay
-
NCI Pathway Database VEGFR3 signaling in lymphatic endothelium:
VEGFR3/Fibronectin/alpha5/beta1 Integrin complex (FLT4-FN1-ITGA5-ITGB1)
→
alpha5/beta1 Integrin/Fibronectin complex (ITGA5-ITGB1-FN1)
(modification, collaborate)
Wang et al., J Biol Chem 2001
Evidence: mutant phenotype, assay
-
NCI Pathway Database VEGFR3 signaling in lymphatic endothelium:
VEGFR3/Fibronectin/alpha5/beta1 Integrin complex (FLT4-FN1-ITGA5-ITGB1)
→
VEGFR3 (FLT4)
(modification, collaborate)
Wang et al., J Biol Chem 2001
Evidence: mutant phenotype, assay
-
NCI Pathway Database VEGFR3 signaling in lymphatic endothelium:
alpha5/beta1 Integrin/Fibronectin complex (ITGA5-ITGB1-FN1)
→
VEGFR3 (FLT4)
(modification, collaborate)
Wang et al., J Biol Chem 2001
Evidence: mutant phenotype, assay
-
Reactome Reaction:
ITGA5
→
ITGB1
(direct_complex)
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind_translation Interaction:
ITGB1
—
ITGA5
(coimmunoprecipitation)
Hemler et al., J Biol Chem 1987
-
IRef Biogrid Interaction:
ITGB1
—
ITGA5
(physical association, affinity chromatography technology)
Lobert et al., Dev Cell 2010*
-
IRef Biogrid Interaction:
ITGB1
—
ITGA5
(physical association, affinity chromatography technology)
Rantala et al., Nat Cell Biol 2011*
-
IRef Biogrid Interaction:
ITGB1
—
ITGA5
(physical association, affinity chromatography technology)
Zhang et al., Hepatology 2003*
-
IRef Biogrid Interaction:
ITGB1
—
ITGA5
(colocalization, biochemical)
Havugimana et al., Cell 2012
-
MIPS CORUM ITGA5-ITGB1-FN1-TGM2 complex:
ITGA5-ITGB1-FN1-TGM2 complex complex (FN1-ITGA5-ITGB1-TGM2)
Akimov et al., J Cell Biol 2000
-
MIPS CORUM ITGA5-ITGB1-ADAM15 complex:
ITGA5-ITGB1-ADAM15 complex complex (ADAM15-ITGA5-ITGB1)
Nath et al., J Cell Sci 1999*
-
MIPS CORUM ITGA5-ITGB4 complex:
ITGA5-ITGB4 complex complex (ITGA5-ITGB1)
Hemler et al., J Biol Chem 1987
-
MIPS CORUM ITGA5-ITGB1-FN-1-NOV complex:
ITGA5-ITGB1-FN-1-NOV complex complex (FN1-ITGA5-ITGB1-NOV)
Ellis et al., J Vasc Res 2003*
-
MIPS CORUM ITGA5-ITGB1-CAL4A3 complex:
ITGA5-ITGB1-CAL4A3 complex complex (COL18A1-ITGA5-ITGB1)
Sudhakar et al., Proc Natl Acad Sci U S A 2003
-
MIPS CORUM ITGA5-ITGB1-SPP1 complex:
ITGA5-ITGB1-SPP1 complex complex (ITGA5-ITGB1-SPP1)
Yokosaki et al., Matrix Biol 2005*
-
IRef Corum Interaction:
Complex of ITGA5-ITGB1-FN1-ITGB1-FN1-ITGA5-NOV-NOV
(association, coimmunoprecipitation)
Ellis et al., J Vasc Res 2003*
-
IRef Corum Interaction:
Complex of ITGA5-ITGB1-FN1-TGM2
(association, coimmunoprecipitation)
Akimov et al., J Cell Biol 2000
-
IRef Corum Interaction:
Complex of ITGA5-ITGB1
(association, coimmunoprecipitation)
Lee et al., J Biol Chem 2004*
-
IRef Corum Interaction:
Complex of ITGB1-ITGA5-SPP1
(association, affinity chromatography technology)
Yokosaki et al., Matrix Biol 2005*
-
IRef Corum Interaction:
Complex of ITGB1-ITGA5-ADAM15
(association, affinity chromatography technology)
Nath et al., J Cell Sci 1999*
-
IRef Corum Interaction:
Complex of COL18A1-ITGA5-ITGA5-ITGB1-ITGB1-COL18A1
(association, coimmunoprecipitation)
Sudhakar et al., Proc Natl Acad Sci U S A 2003
-
IRef Corum Interaction:
ITGB1
—
ITGA5
(association, coimmunoprecipitation)
Hemler et al., J Biol Chem 1987
-
IRef Dip Interaction:
ITGB1
—
ITGA5
(physical association, pull down)
Kim et al., Nature 2012*
-
IRef Hprd Interaction:
Complex of 33 proteins
(in vivo)
Zhao et al., J Cell Biol 2001*
-
IRef Hprd Interaction:
Complex of FN1-ITGA5-ITGB1-ITGA5-ITGB1-FN1-ITGB1-ITGA5-FN1
(in vivo)
Trache et al., Biophys J 2005*, Weinacker et al., J Biol Chem 1994
-
IRef Hprd Interaction:
Complex of 19 proteins
(in vivo)
Schütt et al., J Mol Endocrinol 2004*
-
IRef Hprd Interaction:
Complex of ITGB1-ITGA5-ITGA5-ITGA5-ADAM15-ADAM15-ADAM15-ITGB1-ITGB1
(in vivo)
Nath et al., J Cell Sci 1999*
-
IRef Hprd Interaction:
Complex of 19 proteins
(in vivo)
Akimov et al., J Cell Biol 2000
-
IRef Hprd Interaction:
Complex of ITGA5-PPAP2B-ITGB1-ITGB1-PPAP2B-ITGA5-PPAP2B-ITGA5-ITGB1
(in vivo)
Humtsoe et al., Biochem Biophys Res Commun 2005*
-
IRef Hprd Interaction:
ITGB1
—
ITGA5
(in vitro)
Jones et al., Proc Natl Acad Sci U S A 1993*
-
IRef Hprd Interaction:
ITGB1
—
ITGA5
(in vivo)
Jones et al., Proc Natl Acad Sci U S A 1993*
-
IRef Intact Interaction:
Complex of ITGA5-ITGB1-MMP9
(association, anti bait coimmunoprecipitation)
Wang et al., J Biol Chem 2003*
-
IRef Intact Interaction:
Complex of 102 proteins
(association, pull down)
Tang et al., Proteomics 2010
-
IRef Intact Interaction:
Complex of PXN-ITGB1-ITGA5-FN1
(association, cross-linking study)
Humphries et al., Science signaling 2009
-
IRef Intact Interaction:
Complex of ITGA5-ITGB1-SHARPIN
(association, anti bait coimmunoprecipitation)
Rantala et al., Nat Cell Biol 2011*
-
IRef Intact Interaction:
Complex of ITGB1-ITGA5
(physical association, enzyme linked immunosorbent assay)
Humtsoe et al., Biochem Biophys Res Commun 2005*
-
IRef Intact Interaction:
Complex of ITGA5-FN1-ITGB1-ITGA5-ITGB1-FN1
(association, cross-linking study)
Humphries et al., Science signaling 2009
-
IRef Intact Interaction:
Complex of 168 proteins
(association, cross-linking study)
Byron et al., Proteomics 2012
-
IRef Intact Interaction:
Complex of 400 proteins
(association, cross-linking study)
Humphries et al., Science signaling 2009
-
IRef Intact Interaction:
Complex of ITGA5-ITGB1-PPAP2B
(physical association, enzyme linked immunosorbent assay)
Humtsoe et al., Biochem Biophys Res Commun 2005*
-
IRef Intact Interaction:
ITGB1
—
ITGA5
(direct interaction, inferred by curator)
Hermjakob et al., Nucleic Acids Res 2004
-
IRef Ophid Interaction:
ITGB1
—
ITGA5
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Shibayama et al., Blood 1999
:
These data indicate that H-Ras and PLC, but not Raf-1, MAPK kinase, or the MAPK pathway, are involved in the inside-out signaling pathway of IL-3 induced
VLA-4 and
VLA-5 activation in Baf3 cells
Duncan et al., J Cell Sci 2000
(Cataract) :
Overexpression of
PAX6 ( 5a ) in lens fiber cells
results in cataract and upregulation of (
alpha)5(beta)1 integrin expression
Qiang et al., Exp Hematol 2000
:
Activation of
mitogen activated protein kinase through
alpha5/beta1 integrin is required for cell cycle progression of B progenitor cell line, Reh, on human marrow stromal cells
Casey et al., Clin Exp Metastasis 2000
(Ovarian Neoplasms) :
Blocking antibodies against alpha integrin subunits suggest that ovarian carcinoma cell migration toward fibronectin is primarily
mediated by the
alpha5beta1 integrin , type IV collagen by the
alpha2beta1 integrin , and laminin by the alpha6beta1 integrin ... Blocking antibodies against alpha integrin subunits suggest that ovarian carcinoma cell migration toward fibronectin is primarily
mediated by the
alpha5beta1 integrin , type IV collagen by the alpha2beta1 integrin, and laminin by the
alpha6beta1 integrin
Aguirre-Ghiso et al., Mol Biol Cell 2001
:
Activation of
alpha5beta1-integrin by
uPAR generates persistently high level of active ERK necessary for tumor growth in vivo
Lee et al., Biochim Biophys Acta 2002
:
The
alpha5beta1 integrin selectively
enhances epidermal growth factor signaling to the phosphatidylinositol-3-kinase/Akt pathway in intestinal epithelial cells
Zhao et al., J Biol Chem 2002
:
An increase in
apoE synthesis after plating on fibronectin could be observed by 2 h and was
inhibited by blocking antibodies to the
alpha(5)beta(1) integrin receptor for fibronectin
Liu et al., Cancer Cell 2002
(Carcinoma, Hepatocellular...) :
Urokinase
plasminogen activator receptor ( uPAR )
activates alpha5beta1 integrin and ERK signaling, inducing in vivo proliferation of HEp3 human carcinoma
Srinivasan et al., Circ Res 2003
(Diabetes Mellitus, Type 2) :
These data indicate that glucose regulates monocyte : endothelial interactions through stimulation of
IL-8 and ROS production and
activation of the
alpha5beta1 integrin complex on HAECs
Wilson et al., Invest Ophthalmol Vis Sci 2003
:
Fibronectin fragments promote human retinal endothelial cell adhesion and proliferation and
ERK activation through
alpha5beta1 integrin and PI 3-kinase
Aguirre-Ghiso et al., Cancer Res 2003
(Breast Neoplasms...) :
Mechanistic analysis implicated high
uPAR expression and its interaction with and
activation of
alpha5beta1-integrin as determinants of the in vivo growth promoting high ERK/p38 ratio in several cell lines
Loeser et al., J Biol Chem 2003
:
These studies have identified a novel pathway for the MAP kinase regulation of MMP-13 production which involves FN-f stimulation of the
alpha5beta1 integrin and
activation of the nonreceptor tyrosine kinase
PYK2 by PKC, most likely PKCdelta
Wickström et al., J Biol Chem 2003
:
Subsequently, through
alpha5beta1 integrin , heparan sulfate, and lipid raft mediated interactions, endostatin
induced Src dependent activation of p190RhoGAP with concomitant decrease in RhoA activity and disassembly of actin stress fibers and focal adhesions ... Subsequently, through
alpha5beta1 integrin , heparan sulfate, and lipid raft mediated interactions, endostatin
induced Src dependent activation of
p190RhoGAP with concomitant decrease in RhoA activity and disassembly of actin stress fibers and focal adhesions
Chen et al., J Urol 2003
(Carcinoma, Transitional Cell...) :
We tested the hypothesis that BCG initiates
NF-kappa B signaling as a
consequence of cross linking
alpha 5 beta 1 integrin receptors present on the tumor cell surface
Mitra et al., J Environ Pathol Toxicol Oncol 2003
(Melanoma, Experimental...) :
RESULTS : The zymographic analysis showed that ligation of cell surface
alpha5beta1 integrin by alpha5 monoclonal antibody
leads to the expression and activation of
MMP-2 and MMP-7 in B16F10 melanoma cells ... RESULTS : The zymographic analysis showed that ligation of cell surface
alpha5beta1 integrin by alpha5 monoclonal antibody
leads to the expression and activation of MMP-2 and
MMP-7 in B16F10 melanoma cells ... CONCLUSION :
alpha5beta1 integrin induced expression and activation of
MMP-2 and -7 indicates the role of tumor cell surface integrin receptor in the modulation of MMPs and, thereby, the invasive property of tumor cells ... CONCLUSION :
alpha5beta1 integrin induced expression and activation of
MMP-2 and -7 indicates the role of tumor cell surface integrin receptor in the modulation of MMPs and, thereby, the invasive property of tumor cells
Alahari et al., EMBO J 2004
:
Nischarin binding to PAK1 is
enhanced by active Rac, with the three proteins forming a complex, while expression of the
alpha5beta1 integrin also increases the Nischarin/PAK1 association
Disatnik et al., J Cell Sci 2004
:
These results demonstrate a direct biochemical pathway linking
alpha5beta1 integrin signaling to cytoskeletal dynamics and
involving bi-directional translocation of
MARCKS during the dramatic changes in cellular morphology that occur during cell migration and tissue morphogenesis
Garciadiego-Cázares et al., Development 2004
:
In the
presence of
BMP7 , inhibition of
alpha5beta1 integrin function still induced the formation of the ectopic joint between proliferating chondrocytes and hypertrophic chondrocytes
Lowrie et al., Br J Cancer 2004
(Carcinoma...) :
Latent effects of fibronectin,
alpha5beta1 integrin , alphaVbeta5 integrin and the cytoskeleton
regulate pancreatic carcinoma cell
IL-8 secretion
Han et al., Int J Cancer 2005
(Carcinoma, Non-Small-Cell Lung...) :
Overall, these findings suggest that
COX-2 inhibitors
suppress alpha5beta1 integrin expression in NSCLC through effects on integrin alpha5 gene transcription mediated by Erk activation, increased Sp1, decreased AP-1 DNA binding and inactivation of SAPK/JNK signals
Lu et al., Mol Pharmacol 2006
:
Laulimalide inhibited integrin activation ; however, compared with docetaxel, it had a weaker inhibitory effect on the
VEGF induced association of VEGFR-2 with the
alpha5beta1 integrin ... Compared with docetaxel, laulimalide more potently caused a reduction in the constitutive levels ( i.e., in the absence of VEGF ) of phosphorylated
paxillin and more potently
inhibited the association of RhoA with the
alpha5beta1 integrin
Wu et al., J Cancer Res Clin Oncol 2006
(Breast Neoplasms) :
In this study we investigated the
effects of
E-cadherin on cell-matrix adhesion and
alpha5beta1 integrin expression in human breast carcinoma cells
Reyes-Reyes et al., Exp Cell Res 2006
(Adenocarcinoma...) :
Using a model system of cultured Colo 320 human colon adenocarcinoma cells incubated with soluble P-selectin-IgG chimeric protein, we have found that
P-selectin can
stimulate activation of the
alpha(5)beta(1) integrin resulting in a specific increase of adhesion and spreading of these cells on fibronectin substrates ... These results suggest that
P-selectin binding to tumor cells can
activate alpha(5)beta(1) integrin via PI3-K and p38 MAPK signaling pathways leading to increased cell adhesion
Camacho-Leal et al., J Cell Physiol 2007
(MAP Kinase Signaling System) :
Inhibition of PI3-K and ILK, but not
MAPK ,
prevented the
alpha5beta1 integrin activation ... Inhibition of PI3-K and
ILK , but not MAPK,
prevented the
alpha5beta1 integrin activation ... Inhibition of
PI3-K and ILK, but not MAPK,
prevented the
alpha5beta1 integrin activation
Kragtorp et al., Dev Dyn 2007
:
Loss of
integrin alpha5 delayed somite turning and accumulation of
integrin beta1 at somite boundaries, and disrupted the fibronectin matrix surrounding developing somites
Tyagi et al., Mol Cell Biochem 2008
(Cardiovascular Diseases) :
In cultured ECs, Fg binding to intercellular adhesion molecule-1 and to
alpha(5)beta(1) integrin ,
caused phosphorylation of
ERK
Alsaleh et al., Arthritis Rheum 2007
(Arthritis, Rheumatoid) :
BAFF synthesis by rheumatoid synoviocytes is positively
controlled by
alpha5beta1 integrin stimulation and is negatively regulated by tumor necrosis factor alpha and Toll-like receptor ligands ... In contrast, we demonstrated that stimulation of
alpha5beta1 integrin can
induce BAFF synthesis and release per se and that stimulation of this pathway has no inhibitory effect on IFNgamma induced BAFF synthesis
Das et al., Life Sci 2008
(Breast Neoplasms) :
Blocking of
alpha5beta 1 integrin with anti-alpha5 monoclonal antibody
inhibits the fibronectin induced
MMP activation response appreciably
Reyes-Reyes et al., Exp Cell Res 2008
(Adenocarcinoma...) :
We have previously shown that
P-selectin binding to Colo-320 human colon carcinoma cells
induces specific activation of the
alpha(5)beta(1) integrin with a concomitant increase of cell adhesion and spreading on fibronectin substrates in a phosphatidylinositol 3-kinase (PI3-K) and p38 MAPK dependent manner ... We have previously shown that P-selectin binding to Colo-320 human colon carcinoma cells induces specific activation of the
alpha(5)beta(1) integrin with a concomitant increase of cell adhesion and spreading on fibronectin substrates in a phosphatidylinositol 3-kinase (PI3-K) and p38
MAPK dependent manner
Bass et al., J Cell Biol 2008
:
Matrix induced tyrosine phosphorylation of
p190RhoGAP is
stimulated solely by engagement of
alpha(5)beta(1) integrin and is independent of syndecan-4
Valdembri et al., PLoS Biol 2009
:
Neuropilin-1/GIPC1 signaling
regulates alpha5beta1 integrin traffic and function in endothelial cells ...
Neuropilin-1/GIPC1 signaling
regulates alpha5beta1 integrin traffic and function in endothelial cells
Yap et al., Oncogene 2009
(Carcinoma, Squamous Cell...) :
We found that alphavbeta6- and
alpha5beta1-integrin dependent activation of
Rac1 was mediated through Eps8
Tuomi et al., Science signaling 2009
(Lung Neoplasms...) :
Disruption of intercellular adhesions, increased abundance of
alpha(5)beta(1) integrin , and
activation of
protein kinase Cepsilon ( PKCepsilon ) correlate with invasion and unfavorable prognosis in lung cancer
Yang et al., J Biol Chem 2010
(Ion Channel Gating) :
Thus,
BK channel activity is
enhanced by
alpha5beta1 integrin activation, likely through an intracellular signaling pathway involving c-src phosphorylation of the channel alpha-subunit at Tyr-766
Fiedler et al., Haematologica 2012
(Chromosome Deletion...) :
All platelets of patients expressed normal levels of CD41/61, CD49b, and CD49f receptors, while CD42a/b and
CD29 were slightly reduced and the fibronectin receptor
CD49e markedly
reduced
Galiano et al., J Clin Invest 1996
(Skin Ulcer) :
Our results suggest that activation of both the IGF-I receptor and the
alpha5beta1 integrin is
required for
IGF-I to stimulate wound healing
Magro et al., Gen Diagn Pathol 1997
(Dupuytren Contracture) :
These findings suggest that the
alpha5beta1 integrin/fibronectin complex may be
involved in regulating the interactions between myofibroblasts and
ECM in palmar fibromatosis
Xie et al., J Biol Chem 1998
:
Our results suggest that
TNF-alpha may
regulate macrophage differentiation and critical matrix degrading activities of myeloid progenitor cells in an autocrine manner by augmenting surface levels of the
alpha5 beta1 integrin , thus promoting interactions with the extracellular matrix, a key event for maturation and migration of these cells during inflammation
Kagami et al., Biochem Biophys Res Commun 1998
:
Immunoprecipitation using 35S-metabolic labeling, flow cytometry and a 3H-thymidine-uptake analysis demonstrated that
PDGF-BB stimulated the cell mitogenicity and the expression of
alpha5beta1 integrin ( a fibronectin receptor ), but not alpha1beta1 integrin ( a collagen and laminin receptor ) of MCs on plastic, in a dose dependent manner ... Thus, the parallel
up-regulation of MC-mitogenicity and
alpha5beta1 integrin expression by
PDGF-BB suggested that alpha5beta1 integrin is an important ECM receptor involved in the proliferative phenotype of MC
Collo et al., J Cell Sci 1999
:
We have investigated the
effect of wound induced two-dimensional migration, basic fibroblast growth factor (bFGF),
transforming growth factor-beta1 ( TGF-beta1 ) and leukemia inhibitory factor (LIF) on expression of the
alpha5beta1 integrin in endothelial cells ... We have investigated the
effect of wound induced two-dimensional migration,
basic fibroblast growth factor (bFGF) , transforming growth factor-beta1 ( TGF-beta1 ) and leukemia inhibitory factor (LIF) on expression of the
alpha5beta1 integrin in endothelial cells ... We have investigated the
effect of wound induced two-dimensional migration, basic fibroblast growth factor (bFGF), transforming growth factor-beta1 ( TGF-beta1 ) and
leukemia inhibitory factor (LIF) on expression of the
alpha5beta1 integrin in endothelial cells ... We have investigated the
effect of wound induced two-dimensional migration, basic fibroblast growth factor (bFGF),
transforming growth factor-beta1 ( TGF-beta1 ) and leukemia inhibitory factor (LIF) on expression of the
alpha5beta1 integrin in endothelial cells