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(Circulation Research. 2002;90:371.)
© 2002 American Heart Association, Inc.

Editorials

Can Integrins Integrate Vascular Myogenic Responses?

Livia C. Hool

From the Department of Physiology, The University of Western Australia, Crawley, Western Australia.

Correspondence to Dr Livia C. Hool, Dept of Physiology, The University of Western Australia, Stirling Highway, Crawley, WA, 6009, Australia. E-mail lhool@cyllene.uwa.edu.au

Key Words: myogenic response • arteriolar constriction • mechanotransduction • cytoskeleton • L-type Ca²⁺ channels

Vascular pathologies associated with the heart, brain, and peripheral blood vessels remain the leading cause of death in the Western world, accounting for over 960 000 deaths in 1999 in the United States alone.¹ One of the difficulties in elucidating the mechanisms contributing to vessel disease has been in fully understanding how the vascular system maintains basal vascular tone and autoregulates blood flow and capillary hydrostatic pressure. It is now known that one of the processes participating in these vital functions is the myogenic response.

The myogenic response, first defined by Bayliss in 1902,² describes the response of arterial blood vessels to changes in luminal pressure. Typically, it involves constriction of the vessel in response to increases in transmural pressure and dilation in response to pressure reduction. It is most pronounced in resistance vessels and arterioles. The myogenic response participates in local regulation of blood flow and protects from large changes in pressure induced by postural changes.³

Recently, interest has focused on the integrin family of adhesion molecules as possible "transducers" of changes in vascular smooth muscle tension. The integrins are a large family of cell-cell adhesion receptors comprising at least 16 and 8 ß subunits that can heterodimerize to produce more than 20 transmembrane receptors. The integrins can recognize ligands of the extracellular matrix and transmit extracellular stimuli into intracellular signaling events⁴ because they are located amongst a network of extracellular matrix proteins including several types of collagen, laminin, elastin, fibronectin, vitronectin, and osteopontin. Association of integrins with extracellular . . . [Full Text of this Article]

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