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J Biol Chem, Vol. 274, Issue 34, 24321-24327, August 20, 1999
From the Departments of Cyr61 and connective tissue growth factor (CTGF),
members of a newly identified family of extracellular matrix-associated signaling molecules, are found to mediate cell adhesion, promote cell
migration and enhance growth factor-induced cell proliferation in
vitro, and induce angiogenesis in vivo. We previously
showed that vascular endothelial cell adhesion and migration to Cyr61 and Fisp12 (mouse CTGF) are mediated through integrin
Activation-dependent Adhesion of Human Platelets to
Cyr61 and Fisp12/Mouse Connective Tissue Growth Factor Is Mediated
through Integrin
IIb
3
,
Pharmacology and
§ Molecular Genetics, University of Illinois,
Chicago, Illinois 60612
v
3. Both Cyr61 and Fisp12/mCTGF are
present in normal blood vessel walls, and it has been demonstrated that
CTGF is overexpressed in advanced atherosclerotic lesions. In the
present study, we examined whether Cyr61 and Fisp12/mCTGF could serve
as substrates for platelet adhesion. Agonist (ADP, thrombin, or
U46619)-stimulated but not resting platelets adhered to both Cyr61 and
Fisp12/mCTGF, and this process was completely inhibited by
prostaglandin I2, which prevents platelet activation. The
specificity of Cyr61- and Fisp12/mCTGF-mediated platelet adhesion was
demonstrated by specific inhibition of this process with polyclonal
anti-Cyr61 and anti-Fisp12/mCTGF antibodies, respectively. The adhesion
of ADP-activated platelets to both proteins was divalent
cation-dependent and was blocked by RGDS, HHLGGAKQAGDV, or
echistatin, but not by RGES. Furthermore, this process was specifically
inhibited by the monoclonal antibody AP-2
(anti-IIb3), but not by LM609
(anti-v3), indicating that the
interaction is mediated through integrin
IIb3. In a solid phase binding assay,
activated IIb3, purified by RGD affinity chromatography, bound to immobilized Cyr61 and Fisp12/mCTGF in a
dose-dependent and RGD-inhibitable manner. In contrast,
unactivated IIb3 failed to bind to either
protein. Collectively, these findings identify Cyr61 and Fisp12/mCTGF
as two novel activation-dependent adhesive ligands for the
integrin IIb3 on human platelets, and implicate a functional role for these proteins in hemostasis and thrombosis.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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X. Tong, D. Xie, J. O'Kelly, C. W. Miller, C. Muller-Tidow, and H. P. Koeffler Cyr61, a Member of CCN Family, Is a Tumor Suppressor in Non-Small Cell Lung Cancer J. Biol. Chem., December 7, 2001; 276(50): 47709 - 47714. [Abstract] [Full Text] [PDF]
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D. Sampath, R. C. Winneker, and Z. Zhang Cyr61, a Member of the CCN Family, Is Required for MCF-7 Cell Proliferation: Regulation by 17{beta}-Estradiol and Overexpression in Human Breast Cancer Endocrinology, June 1, 2001; 142(6): 2540 - 2548. [Abstract] [Full Text] [PDF]
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B. V. Latinkic, F.-E Mo, J. A. Greenspan, N. G. Copeland, D. J. Gilbert, N. A. Jenkins, S. R. Ross, and L. F. Lau Promoter Function of the Angiogenic Inducer Cyr61Gene in Transgenic Mice: Tissue Specificity, Inducibility During Wound Healing, and Role of the Serum Response Element Endocrinology, June 1, 2001; 142(6): 2549 - 2557. [Abstract] [Full Text] [PDF]
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 G. R. Grotendorst, L. F. Lau, and B. Perbal CCN Proteins Are Distinct from, and Should Not Be Considered Members of, the Insulin-Like Growth Factor-Binding Protein Superfamily J. Clin. Endocrinol. Metab., February 1, 2001; 86(2): 944 - 945. [Full Text]
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