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Vol. 12, Issue 4, 1019-1033, April 2001
Department of Cellular and Molecular Medicine, School of Medicine,
University of California, San Diego, La Jolla, California 92093
We have demonstrated that the plasmalemmal vesicles (caveolae) of
the continuous microvascular endothelium function as transcytotic vesicular carriers for protein molecules >20 Å and that transcytosis is an N-ethylmaleimide-sensitive factor
(NSF)-dependent, N-ethylmaleimide-sensitive process. We have further investigated NSF interactions with endothelial proteins to find out 1) whether a complete set of fusion and targeting proteins is present in the endothelium; 2) whether they are organized in multimolecular complexes as in neurons; and 3) whether the endothelial multimolecular complexes differ from their neuronal counterparts, because of their specialized role in transcytosis. To
generate the complexes, we have used myc-NSF, cultured pulmonary endothelial cells, and rat lung cytosol and membrane preparations; to
detect them we have applied coimmunoprecipitation with myc antibodies;
and to characterize them we have used velocity sedimentation and
cross-linking procedures. We have found that both cytosolic and
membrane fractions contain complexes that comprise beside soluble NSF
attachment proteins and SNAREs (soluble NSF attachment protein
receptor), rab 5, dynamin, caveolin, and lipids. By immunogold labeling and negative staining we have detected in these complexes, myc-NSF, syntaxin, dynamin, caveolin, and endogenous NSF. Similar complexes are formed by endogenous NSF. The results indicate that complexes with a distinct protein-lipid composition exist and suggest
that they participate in targeting, fusion, and fission of caveolae
with the endothelial plasmalemma.
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