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M301534200v1
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Papers In Press, published online ahead of print May 6, 2003
J. Biol. Chem, 10.1074/jbc.M301534200
Submitted on February 12, 2003
Revised on April 10, 2003
Accepted on May 6, 2003

Identification of a novel integrin alpha Mbeta 2 binding site in CCN1 (CYR61), a matricellular protein expressed in healing wounds and atherosclerotic lesions

Joseph M. Schober, Lester F. Lau, Tatiana P. Ugarova, and Stephen C. Lam

Pharmacology Dept., University of Illinois at Chicago, Chicago, IL 60657

Corresponding Author: sclam{at}uic.edu

CCN1 (cysteine-rich 61, CYR61) and CCN2 (connective tissue growth factor, CTGF) 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 alpha Mbeta 2 as the major adhesion receptor mediating monocyte adhesion to CCN1 and CCN2, and have shown that the alpha 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-alpha M monoclonal antibody 2LPM19c. Consistently, a GST fusion protein containing the alpha MI-domain (GST-alpha 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 alpha MI-domain binding. To confirm that the CCN1-H2 sequence within the CCN1 protein mediates alpha Mbeta 2 interaction, we developed an anti-peptide antibody against CCN1-H2 and showed that it specifically blocked GST-alpha MI binding to intact CCN1. Collectively, these results identify the H2 sequence in CCN1 and CCN2 as a novel integrin alpha Mbeta 2 binding motif which bears no apparent homolgy to any alpha Mbeta 2 binding sequence reported to date.


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