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Am J Physiol Heart Circ Physiol (November 20, 2003). doi:10.1152/ajpheart.00909.2003
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Submitted on September 25, 2003
Accepted on November 19, 2003

Multiple PV1 Dimers Reside in the Same Stomatal or Fenestral Diaphragm

Radu V. Stan1*

1 Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA, USA

* To whom correspondence should be addressed. E-mail: sraduvirgil{at}ucsd.edu.

Several of the endothelial specific structures that have been involved in microvascular permeability (such as caveolae, transendothelial channels (TEC), vesiculo-vacuolar organelles (VVO) 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 endothelial specific integral membrane glycoprotein that is associated with both the stomatal diaphragms of caveolae, transendothelial channels 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, as its expression being sufficient to form de novo stomatal and fenestral diaphragms in both endothelial and non-endothelial 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.




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