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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells.

Caveolin-1 is a protein component (of relative molecular mass 22, 000) of the striated coat that decorates the cytoplasmic surface of caveolae membranes. Previous biochemical and molecular tests have indicated that caveolin-1 is an integral membrane protein that is co-translationally inserted into endoplasmic-reticulum membranes of fibroblast and epithelial cells such that its carboxy- and amino-terminal ends are in the cytoplasm. Here we identify caveolin-1 in the secretory pathway of exocrine cells. Secretion of caveolin-1 from pancreatic acinar cells and a transfected exocrine cell line, but not from Chinese hamster ovary cells, is stimulated by the secretagogues secretin, cholecystokinin and dexamethasone. The secreted caveolin-1 co-fractionates with apolipoproteins, indicating that it may be secreted in a complex with lipids.[1]


  1. Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells. Liu, P., Li, W.P., Machleidt, T., Anderson, R.G. Nat. Cell Biol. (1999) [Pubmed]
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