Articles |
vß3 Integrin Mediates Arteriolar Vasodilation in Response to RGD Peptides
the Microcirculation Research Institute and Department of Medical Physiology (J.E.M., S.H.P., G.A.M.) and the Department of Pathology and Laboratory Medicine (G.E.D.), Texas A&M University Health Science Center, Texas A&M University, College Station, Tex.
Correspondence to Gerald A. Meininger, PhD, Department of Medical Physiology, Reynold's Medical Building, Texas A&M University Health Science Center, College Station, TX 77843-1114. E-mail gam@tamu.edu.
Arteriolar vasodilation and the resultant increase in blood flow are characteristic vascular responses to tissue injury. The dilatory mediators signaling these responses are incompletely understood. We show that integrin-binding peptides containing the Arg-Gly-Asp (RGD) tripeptide sequence cause immediate and, in some instances, sustained vasodilation when applied to isolated rat cremaster arterioles. The vasodilation is dependent on interaction of the soluble RGD sequence with the
vß3 integrin expressed by smooth muscle cells in the arteriolar wall. Possible in vivo sources of soluble RGD sequences are fragments of extracellular matrix proteins that are generated after tissue injury. Indeed, protease-generated fragments of denatured collagen type I (a major source of RGD sequences) also cause cremaster arteriolar vasodilation through the
vß3 integrin. Thus, extracellular matrix protein fragments containing the RGD sequence may act as vascular wound recognition signals to regulate blood flow to injured tissue.
Key Words: vasodilation Arg-Gly-Asp
vß3 integrin collagen degradation vascular wound response
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