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J Biol Chem, Vol. 273, Issue 41, 26765-26771, October 9, 1998
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From the The enzyme acyl coenzyme A:cholesterol
acyltransferase 1 (ACAT1) mediates sterol esterification, a crucial
component of intracellular lipid homeostasis. Two enzymes catalyze this
activity in Saccharomyces cerevisiae (yeast), and several
lines of evidence suggest multigene families may also exist in mammals.
Using the human ACAT1 sequence to screen data bases of expressed
sequence tags, we identified two novel and distinct partial human
cDNAs. Full-length cDNA clones for these ACAT related gene
products (ARGP) 1 and 2 were isolated from a hepatocyte (HepG2)
cDNA library. ARGP1 was expressed in numerous human adult tissues
and tissue culture cell lines, whereas expression of ARGP2 was more
restricted. In vitro microsomal assays in a yeast strain
deleted for both esterification genes and completely deficient in
sterol esterification indicated that ARGP2 esterified cholesterol while
ARGP1 did not. In contrast to ACAT1 and similar to liver
esterification, the activity of ARGP2 was relatively resistant to a
histidine active site modifier. ARGP2 is therefore a tissue-specific
sterol esterification enzyme which we thus designated ACAT2. We
speculate that ARGP1 participates in the coenzyme
A-dependent acylation of substrate(s) other than
cholesterol. Consistent with this hypothesis, ARGP1, unlike any other
member of this multigene family, possesses a predicted diacylglycerol
binding motif suggesting that it may perform the last acylation in
triglyceride biosynthesis.
Institute of Human Nutrition,
Departments of Pediatrics and Physiology and Molecular
Biophysics, Columbia University College of Physicians and Surgeons, New
York, New York 10032 and ¶ DuPont Pharmaceutical Company,
Experimental Station, Wilmington, Delaware 19880-0400
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