Cholesterol ester hydrolysis and hormone-sensitive lipase in lactating rat mammary tissue

Biochim Biophys Acta. 1991 Apr 3;1082(3):251-4. doi: 10.1016/0005-2760(91)90200-2.

Abstract

Neutral cholesterol esterase activity is expressed in extracts of mammary epithelial cells. The identity of the enzyme catalyzing this hydrolysis was investigated. Anti-hormone-sensitive lipase immunoglobulin elicited the total inhibition of this activity and also immunoprecipitated a single phosphoprotein of Mr 84 kDa from mammary cell extracts previously phosphorylated in vitro with [gamma-32P]ATP and cyclic AMP-dependent protein kinase. It is concluded that mammary cell cholesterol esterase activity results from the presence of hormone-sensitive lipase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Cells, Cultured
  • Cholesterol Esters / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Hydrolysis
  • Lactation*
  • Mammary Glands, Animal / enzymology
  • Mammary Glands, Animal / metabolism*
  • Mammary Glands, Animal / physiology
  • Phosphorylation
  • Protein Kinases / metabolism
  • Rats
  • Rats, Inbred Strains
  • Sterol Esterase / metabolism*

Substances

  • Cholesterol Esters
  • Adenosine Triphosphate
  • Protein Kinases
  • Sterol Esterase