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A novel endocytic pathway

The endothelial adhesion molecules ICAM-1 and PECAM-1 internalize various particles, including natural ligands, apoptotic fragments and antibody conjugates used for drug delivery. The endocytic vesicles involved are 100-300-nm in diameter, which is compatible with both major endocytic mechanisms: the caveolar pathway and the clathrin-dependent pathway. Nevertheless the mode of ICAM-1/PECAM-1 internalization is not known. Michael Koval and co-workers have therefore analysed uptake of fluorescent anti-PECAM-1 and anti-ICAM-1 conjugates by human umbilical vein endothelial cells (see p. 1599). They find that neither conjugate colocalizes with clathrin or caveolin when internalized and that inhibitors of caveolae- or clathrin-mediated endocytosis fail to block their internalization. Moreover, the authors show that actin `cups' do not form around the internalized particles, eliminating the possibility that phagocytosis is responsible. Interestingly, however, they do find that ICAM-1-mediated endocytosis can be inhibited by a dominant negative mutant of dynamin 2 (a GTPase that helps to recruit actin to endocytosis sites) and by inhibitors of protein kinase C (PKC), Src or Rho kinase (ROCK). They have thus identified a novel endocytic mechanism as well as several of the signalling molecules involved.

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A novel endocytic pathway induced by clustering endothelial ICAM-1 or PECAM-1

Silvia Muro, Rainer Wiewrodt, Anu Thomas, Lauren Koniaris, Steven M. Albelda, Vladimir R. Muzykantov, and Michael Koval
JCS 2003 116: 1599-1609. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?