Cholesterol ester hydrolysis and hormone-sensitive lipase in lactating rat mammary tissue.
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.
Small
C A
CA
Department of Biochemistry and Genetics, University of Newcastle upon Tyne, U.K.
Yeaman
S J
SJ
West
D W
DW
Clegg
R A
RA
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002478:Cells, Cultured; D002788:Cholesterol Esters / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006868:Hydrolysis; D007774:Lactation; D008321:Mammary Glands, Animal / Q000201:enzymology / Q000378:metabolism* / Q000502:physiology; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D002787:Sterol Esterase / Q000378:metabolism*
D002788:Cholesterol Esters; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D002787:Sterol Esterase