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

Abstract

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.

Cite this article

Liu, P., Li, WP., Machleidt, T. et al. Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells. Nat Cell Biol 1, 369–375 (1999). https://doi.org/10.1038/14067

View full text

>> Full Text:   Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells