Retinyl ester hydrolysis and retinol efflux from BFC-1 beta adipocytes

被引:86
作者
Wei, SH
Lai, K
Patel, S
Piantedosi, R
Shen, H
Colantuoni, V
Kraemer, FB
Blaner, WS
机构
[1] COLUMBIA UNIV,DEPT MED,NEW YORK,NY 10032
[2] COLUMBIA UNIV,INST HUMAN NUTR,NEW YORK,NY 10032
[3] STANFORD UNIV,SCH MED,DEPT VET AFFAIRS,PALO ALTO,CA 94305
[4] STANFORD UNIV,SCH MED,DEPT MED,PALO ALTO,CA 94305
[5] UNIV NAPLES,DIPARTIMENTO BIOCHIM & BIOTECNOL MED,I-80131 NAPLES,ITALY
关键词
D O I
10.1074/jbc.272.22.14159
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Adipose tissue is an important storage depot for retinol, but there are no data regarding retinol mobilization from adipose stores. To address this, dibutyryl cAMP was provided to murine BFC-1 beta adipocytes and its effects on retinol efflux assessed. High performance liquid chromatography analysis of retinol and retinyl esters in adipocytes and media indicated that cAMP stimulated, in a time- and dose-dependent manner, retinol accumulation in the culture media and decreased cellular retinyl ester concentrations. Study of adipocyte retinol-binding protein synthesis and secretion indicated that cAMP-stimulated retinol efflux into the media did not result from increased retinol-retinol-binding protein secretion but was dependent on the presence of fetal bovine serum in the culture media. Since our data suggested that retinyl esters can be hydrolyzed by a cAMP-dependent enzyme like hormone-sensitive lipase (HSL), in separate studies, we purified a HSL-containing fraction from BFC-1 beta adipocytes and demonstrated that it catalyzed retinyl palmitate hydrolysis. Homogenates of Chinese hamster ovary cells overexpressing HSL catalyzed retinyl palmitate hydrolysis in a time-, protein-, and substrate-dependent manner, with an apparent K-m for retinyl palmitate of 161 mu M, whereas homogenates from control Chinese hamster ovary cells did not.
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页码:14159 / 14165
页数:7
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