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Am J Physiol Heart Circ Physiol 286: H1347-H1353, 2004. First published November 20, 2003; doi:10.1152/ajpheart.00909.2003
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Multiple PV1 dimers reside in the same stomatal or fenestral diaphragm

Radu V. Stan

Department of Cellular and Molecular Medicine, University of California-San Diego, La Jolla, California 92093-0651

Submitted 25 September 2003 ; accepted in final form 19 November 2003

Several of the endothelium-specific structures that have been involved in microvascular permeability [such as caveolae, transendothelial channels (TECs), vesiculovacuolar organelles (VVOs), and fenestrae] can be provided with either a stomatal or fenestral diaphragm. In the case of fenestrae, the diaphragm has the presumed function of creating a permselective barrier for solutes from blood plasma and interstitium. PV1 is an endothelium-specific integral membrane glycoprotein that is associated with both the stomatal diaphragms of caveolae, TECs, and VVOs as well as the diaphragms of endothelial fenestrae. The intimate structure of these diaphragms has been shown to consist of a meshwork formed by radial fibrils. We have recently shown that PV1 is a key structural element of both types of diaphragms, with its expression being sufficient to form de novo stomatal and fenestral diaphragms in both endothelial and nonendothelial cell types in culture. We have further tested the role of PV1 in the structure of the diaphragms and demonstrate here that multiple PV1 homodimers reside in close proximity within the same diaphragm. Our data bring further support to the paradigm by which PV1 dimers would form the fibrils of the diaphragms with a function in the microvascular permeability.

caveolae; lipid rafts; cross-linking; vascular permeability


Address for reprint requests and other correspondence: R. V. Stan, Dept. of Cellular and Molecular Medicine, 0651, Univ. of California-San Diego, 9500 Gilman Dr., La Jolla, CA 92093-0651 (E-mail: sraduvirgil{at}ucsd.edu)




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