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Vol. 9, Issue 4, 865-874, April 1998
2
1 Integrin in Vascular Smooth Muscle Cells
Department of Biochemistry and Molecular Biophysics, Washington
University School of Medicine, St. Louis, Missouri 63110
The carboxyl-terminal domain of thrombospondin-1 enhances the
migration and proliferation of smooth muscle cells.
Integrin-associated protein (IAP or CD47) is a receptor for the
thrombospondin-1 carboxyl-terminal cell-binding domain and binds the
agonist peptide 4N1K (kRFYVVMWKk) from this domain. 4N1K peptide
stimulates chemotaxis of both human and rat aortic smooth muscle cells
on gelatin-coated filters. The migration on gelatin is specifically
blocked by monoclonal antibodies against IAP and a 
1
integrin, rather than 
v3 as found previously for
4N1K-stimulated chemotaxis of endothelial cells on gelatin. Both human
and rat smooth muscle cells displayed a weak migratory response to
soluble type I collagen; however, the presence of 4N1K peptide or
intact thrombospondin-1 provoked a synergistic chemotactic response
that was partially blocked by antibodies to 2 and 1
integrin subunits and to IAP. A combination of anti2 and IAP
monoclonal antibodies completely blocked chemotaxis. RGD peptide and
antiv3 mAb were without effect. 4N1K and thrombospondin-1 did not
augment the chemotactic response of smooth muscle cells to fibronectin,
vitronectin, or collagenase-digested type I collagen. Complex formation
between 21 and IAP was detected by the coimmunoprecipitation of
both 2 and 1 integrin subunits with IAP. These data
suggest that IAP can associate with 21 integrin and
modulate its function.
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