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J. Biol. Chem., Vol. 278, Issue 28, 25808-25815, July 11, 2003
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Identification of a Novel Integrin 
M
2 Binding Site in CCN1 (CYR61), a Matricellular Protein Expressed in Healing Wounds and Atherosclerotic Lesions*
From the
Departments of Pharmacology and
¶Molecular Genetics, University of Illinois at
Chicago, College of Medicine, Chicago, Illinois 60612 and
||Joseph J. Jacobs Center for Thrombosis and
Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic
Foundation, Cleveland, Ohio 44195
CCN1 (cysteine-rich 61) and CCN2 (connective tissue growth factor) are
growth factor-inducible immediate-early gene products found in atherosclerotic
lesions, restenosed blood vessels, and healing cutaneous wounds. Both CCN
proteins have been shown to support cell adhesion and induce cell migration
through interaction with integrin receptors. Recently, we have identified
integrin 
M
2 as the major adhesion receptor
mediating monocyte adhesion to CCN1 and CCN2 and have shown that the
MI domain binds specifically to both proteins. In the
present study, we demonstrated that activated monocytes adhered to a synthetic
peptide (CCN1-H2, SSVKKYRPKYCGS) derived from a conserved region within the
CCN1 C-terminal domain, and this process was blocked by the
anti-M monoclonal antibody 2LPM19c. Consistently, a
glutathione S-transferase (GST) fusion protein containing the
MI domain (GST-MI) bound to immobilized
CCN1-H2 as well as to the corresponding H2 sequence in CCN2 (CCN2-H2,
TSVKTYRAKFCGV). By contrast, a scrambled CCN1-H2 peptide and an 18-residue
peptide derived from an adjacent sequence of CCN1-H2 failed to support
monocyte adhesion or MI domain binding. To confirm that the
CCN1-H2 sequence within the CCN1 protein mediates
M2 interaction, we developed an
anti-peptide antibody against CCN1-H2 and showed that it specifically blocked
GST-MI binding to intact CCN1. Collectively, these results
identify the H2 sequence in CCN1 and CCN2 as a novel integrin
M2 binding motif that bears no apparent
homology to any M2 binding sequence
reported to date.
Received for publication, February 12, 2003 , and in revised form, April 10, 2003.
* This work was supported by the National Institutes of Health Grants HL-41793 (to S. C.-T. L), CA-46565 and CA-80080 (to L. F. L.), and HL-63199 (to T. P. U.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Supported by the National Institutes of Health HL-07829 training grant and
by a predoctoral fellowship from the American Heart Association, Midwest
Affiliate.
** An Established Investigator of the American Heart Association.
To whom correspondence should be addressed: Dept. of Pharmacology (M/C 868),
University of Illinois at Chicago, 835 South Wolcott Ave., Chicago, IL 60612.
Tel.: 312-413-5928; Fax: 312-996-1225; E-mail:
sclam{at}uic.edu.
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