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J. Biol. Chem., Vol. 277, Issue 48, 45874-45879, November 29, 2002
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From the Mike Rosenbloom Laboratory for Cardiovascular Research,
McGill University Health Center, Montreal, Quebec H3A 1A1,
Canada
Acylation-stimulating protein (ASP) acts as a
paracrine signal to increase triglyceride synthesis in adipocytes. ASP
administration results in more rapid postprandial lipid clearance. In
mice, C3 (the precursor to ASP) knockout results in ASP deficiency and leads to reduced body fat and leptin levels. The protective potential of ASP deficiency against obesity and involvement of the leptin pathway
were examined in ob/ob C3(
Acylation-stimulating Protein (ASP) Deficiency Induces Obesity
Resistance and Increased Energy Expenditure in ob/ob
Mice*
/) double knockout mice
(2KO). Compared with age-matched ob/ob mice, 2KO mice had
delayed postprandial triglyceride and fatty acid clearance; associated
with decreased body weight (4-17 weeks age: male: 13.7%, female:
20.6%, p < 0.0001) and HOMA (homeostasis model
assessment) index (37.7%), suggesting increased insulin sensitivity.
By contrast, food intake in 2KO mice was +9.1% higher over
ob/ob mice (p < 0.001, 2KO 5.1 ± 0.2 g/day, ob/ob 4.5 ± 0.2 g/day, wild type 2.6 ± 0.1 g/day). The hyperphagia/leanness was balanced by a 28.5%
increase in energy expenditure (oxygen consumption: 2KO, 131 ± 8.9 ml/h; ob/ob, 102 ± 4.5 ml/h; p < 0.01; wild type, 144 ± 8.9 ml/h). These results suggest
that the ASP regulation of energy storage may influence energy
expenditure and dynamic metabolic balance.
*
This work was supported by a grant from Natural Sciences and
Engineering Research Council of Canada (NSERC) (to K. C.) and by ServierPharmaceuticals (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.
Supported by a scholarship from the Fonds de la Recherche en
Santé du Québec (FRSQ). To whom correspondence
should be addressed: Cardiology, H7.30, Royal Victoria Hospital, 687 Pine Ave. W., Montreal, Quebec H3A 1A1, Canada. Tel.: 514-842-1231 (ext. 35426); Fax: 514-843-2843; E-mail:
katherine.cianflone@mcgill.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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