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Originally published In Press as doi:10.1074/jbc.M206849200 on September 5, 2002

J. Biol. Chem., Vol. 277, Issue 45, 42859-42866, November 8, 2002
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Regulation of Integrin Function by CD47 Ligands
DIFFERENTIAL EFFECTS ON alpha vbeta 3 AND alpha 4beta 1 INTEGRIN-MEDIATED ADHESION*

Heba O. BaraziDagger , Zhuqing LiDagger §, Jo Anne CashelDagger , Henry C. KrutzschDagger , Douglas S. Annis, Deane F. Mosher, and David D. RobertsDagger ||

From the Dagger  Laboratory of Pathology, NCI, National Institutes of Health, Bethesda, Maryland 20892 and  Department of Medicine, University of Wisconsin, Madison, Wisconsin 53706

We examined the regulation of alpha 4beta 1 integrin function in melanoma cells and T cells by ligands of CD47. A CD47 antibody (B6H12) that inhibited alpha vbeta 3-mediated adhesion of melanoma cells induced by CD47-binding peptides from thrombospondin-1 directly stimulated alpha 4beta 1-mediated adhesion of the same cells to vascular cell adhesion molecule-1 and N-terminal regions of thrombospondin-1 or thrombospondin-2. B6H12 also stimulated alpha 4beta 1- as well as alpha 2beta 1- and alpha 5beta 1-mediated adhesion of CD47-expressing T cells but not of CD47-deficient T cells. alpha 4beta 1 and CD47 co-purified as a detergent-stable complex on a CD47 antibody affinity column. CD47-binding peptides based on C-terminal sequences of thrombospondin-1 also specifically enhanced adhesion of melanoma cells and T cells to alpha 4beta 1 ligands. Unexpectedly, activation of alpha 4beta 1 function by the thrombospondin-1 CD47-binding peptides also occurred in CD47-deficient T cells. CD47-independent activation of alpha 4beta 1 required the Val-Val-Met (VVM) motif of the peptides and was sensitive to inhibition by pertussis toxin. These results indicate that activation of alpha 4beta 1 by the CD47 antibody B6H12 and by VVM peptides occurs by different mechanisms. The antibody directly activates a CD47-alpha 4beta 1 complex, whereas VVM peptides may target an unidentified Gi-linked receptor that regulates alpha 4beta 1.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Laboratory of Immunology, NEI, National Institutes of Health, Bldg. 10, 10B22, Bethesda, MD 20892.

|| To whom correspondence should be addressed: 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@helix.nih.gov.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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