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J Biol Chem, Vol. 274, Issue 51, 36219-36225, December 17, 1999
From the Mike Rosenbloom Laboratory for Cardiovascular Research,
McGill University Health Centre, Montreal, Quebec, Canada, H3A 1A1
Canada and § Department of Nutrition, University of
California, Davis, California 95616
Acylation stimulating protein (ASP) is a potent
stimulator of triglyceride synthesis in adipocytes. In the present
study, we have examined the effect of an ASP functional knockout
(ASP(
Acylation Stimulating Protein (ASP) Deficiency Alters
Postprandial and Adipose Tissue Metabolism in Male Mice*
,
/)) on lipid metabolism in male mice. In both young (14 weeks)
and older (26 weeks) mice there were marked delays in postprandial triglyceride clearance (80% increase at 14 weeks and 120% increase at
26 weeks versus wild type (+/+)). Postprandial
nonesterified fatty acids were also increased in ASP(/) mice
versus ASP(+/+) mice by 37% (low fat 10% Kcal) and by
73% (high fat 40% Kcal) diets, although there were no differences in
fasting lipid levels. The ASP(/) mice had moderately increased
energy intake (16% ± 2% p < 0.0001) and reduced
feed efficiency (33% increase in calories/g of body weight gained on
low fat diet) versus wild type. The ASP(/) mice also
had modest changes in insulin/glucose metabolism (30% to 40% decrease
in insulin·glucose product), implying increased insulin sensitivity.
As well, there were decreases in leptin (29% shift in leptin to body
weight ratio) and up to a 26% decrease in specific adipose tissue
depots versus the wild type mice on both low fat and high
fat diets. These results demonstrate that ASP plays an important role
in adipose tissue metabolism and fat partitioning.
*
This study was supported by grants from National Science and
Engineering Council of Canada (to K. C.) and Servier Pharmaceuticals (to A. D. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
A recipient of the Colonel Renouf Fellowship (Royal Victoria
Hospital Research Institute).
¶
Supported by National Institutes of Health Grants DK-35747 and
DK-50129 and grants from the U. S. Department of Agriculture and the
American Diabetes Association.
A research scholar of the Fonds de Recherche en Sante du
Quebec. To whom correspondence should be addressed: Cardiology, H 7.30, Royal Victoria Hospital, 687 Pine Ave. West, Montreal, Quebec, Canada,
H3A 1A1. Tel.: 514-842-1231 (ext. 5426); Fax: 514-982-0686; E-mail:
mdkc@musica.mcgill.ca.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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