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Effect of acylation stimulating protein on the triacylglycerol synthetic pathway of human adipose tissue
Author(s) -
Yasruel Zivart,
Cianflone Katherine,
Sniderman Allan D.,
Rosenbloom Mark,
Walsh Mark,
Rodriguez Miguel A.
Publication year - 1991
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536592
Subject(s) - diacylglycerol kinase , adipose tissue , microsome , clinical chemistry , lipidology , acyl coa , acylation , chemistry , biochemistry , acyltransferase , enzyme , in vitro , phosphatidate , medicine , endocrinology , biology , protein kinase c , catalysis
Acylation stimulating protein (ASP) is a 14 kDa plasma protein which causes in vitro triacylglycerol synthesis in human adipocytes and fibroblasts to increase substantially. ASP was found to stimulate human adipose tissue microsomal glycerophosphate acyltransferase and diacylglycerol acyltransferase activities by 23% and 90%, respectively. However, phosphatidate phosphohydrolase activity showed no increase in activity, nor did microsomal acyl‐CoA synthetase activity. Moreover, ASP did not decrease the apparent K m of diacylglycerol acyltransferase (DGAT), but rather increased its apparent V max suggesting direct interaction of ASP with DGAT.