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J Biol Chem, Vol. 274, Issue 51, 36219-36225, December 17, 1999

Acylation Stimulating Protein (ASP) Deficiency Alters Postprandial and Adipose Tissue Metabolism in Male Mice^*

Ian Murray, Allan D. Sniderman, Peter J. Havel^§¶, and Katherine Cianflone

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(/)) 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.

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^* 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.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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