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J. Biol. Chem., Vol. 278, Issue 42, 40679-40687, October 17, 2003

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Recognition of the N-terminal Modules of Thrombospondin-1 and Thrombospondin-2 by ₆₁ Integrin^*

Maria J. Calzada , John M. Sipes , Henry C. Krutzsch , Peter D. Yurchenco , Douglas S. Annis ¶, Deane F. Mosher ¶ and David D. Roberts  ||

From the Laboratory of Pathology, NCI, National Institutes of Health, Bethesda, Maryland 20892-1500, the Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, and the ^¶Department of Medicine, University of Wisconsin, Madison, Wisconsin 53706

In addition to its recognition by ₃₁ and ₄₁ integrins, the N-terminal pentraxin module of thrombospondin-1 is a ligand for ₆₁ integrin. ₆₁ integrin mediates adhesion of human microvascular endothelial and HT-1080 fibrosarcoma cells to immobilized thrombospondin-1 and recombinant N-terminal regions of thrombospondin-1 and thrombospondin-2. ₆₁ also mediates chemotaxis of microvascular cells to thrombospondin-1 and thrombospondin-2. Using synthetic peptides, LALERKDHSG was identified as an ₆₁-binding sequence in thrombospondin-1. This peptide inhibited ₆₁-dependent cell adhesion to thrombospondin-1, thrombospondin-2, and the E8 fragment of murine laminin-1. The Glu residue in this peptide was required for activity, and the corresponding residue (Glu⁹⁰) in the N-terminal module of thrombospondin-1 was required for its recognition by ₆₁, but not by ₄₁. ₆₁ was also expressed in human umbilical vein endothelial cells; but in these cells, only certain agonists could activate the integrin to recognize thrombospondins. Selective activation of ₆₁ integrin in microvascular endothelial cells by the anti-₁ antibody TS2/16 therefore accounts for their adhesion responses to thrombospondins and explains the distinct functions of ₄₁ and ₆₁ integrins as thrombospondin receptors in microvascular and large vessel endothelial cells.

Received for publication, February 25, 2003 , and in revised form, August 6, 2003.

^* 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.

^|| To whom correspondence should be addressed: Lab. of Pathology, NCI, NIH, Bldg. 10, Rm. 2A33, 10 Center Dr., MSC 1500, Bethesda, MD 20892-1500. Tel.: 301-496-6264; Fax: 301-402-0043; E-mail: droberts{at}helix.nih.gov.

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