Vascular smooth muscle alpha v beta 3 integrin mediates arteriolar vasodilation in response to RGD peptides.
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 alpha v beta 3 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 alpha v beta 3 integrin. Thus, extracellular matrix protein fragments containing the RGD sequence may act as vascular wound recognition signals to regulate blood flow to injured tissue.
Mogford
J E
JE
Microcirculation Research Institute, Texas A&M University Health Science Center, Texas A&M University, College Station 77843-1114, USA.
Davis
G E
GE
Platts
S H
SH
Meininger
G A
GA
D000818:Animals; D001160:Arterioles / Q000502:physiology*; D002478:Cells, Cultured; D008297:Male; D009131:Muscle, Smooth, Vascular / Q000502:physiology*; D009842:Oligopeptides / Q000494:pharmacology* / Q000502:physiology; D051381:Rats; D017207:Rats, Sprague-Dawley; D019030:Receptors, Vitronectin / Q000502:physiology*; D014664:Vasodilation / Q000187:drug effects*
D009842:Oligopeptides; D019030:Receptors, Vitronectin; C047981:arginyl-glycyl-aspartic acid