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

Nat Cell Biol. 1999 Oct;1(6):369-75. doi: 10.1038/14067.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apolipoproteins / chemistry
  • Apolipoproteins / metabolism*
  • CHO Cells
  • Caveolin 1
  • Caveolins*
  • Cricetinae
  • Humans
  • Membrane Proteins / analysis
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Inbred C57BL
  • Pancreas / cytology
  • Pancreas / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Transfection

Substances

  • Apolipoproteins
  • CAV1 protein, human
  • Cav1 protein, mouse
  • Cav1 protein, rat
  • Caveolin 1
  • Caveolins
  • Membrane Proteins