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Am J Physiol Endocrinol Metab 277: E474-E480, 1999;
0193-1849/99 $5.00
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Vol. 277, Issue 3, E474-E480, September 1999

EPILOGUE
Enhanced triglyceride clearance with intraperitoneal human acylation stimulating protein in C57BL/6 mice

Ian Murray, Allan D. Sniderman, and Katherine Cianflone

Mike Rosenbloom Laboratory for Cardiovascular Research, McGill University Health Centre, Montreal, Quebec, Canada H3A 1A1

Acylation stimulating protein (ASP), a novel adipocyte-derived autocrine protein, stimulates triglyceride synthesis and glucose transport in vitro in human and murine adipocytes. In vitro, chylomicrons increase ASP and precursor complement C3 production in adipocytes. Furthermore, in vivo, ASP production from human adipose tissue correlates positively with triglyceride clearance postprandially. The aim of the present study was to determine if intraperitoneally injected ASP accelerated triglyceride clearance in vivo after a fat load in C57Bl/6 mice. ASP increased the triglyceride clearance with a reduction of the triglyceride area under the curve over 6 h (AUC0-6) from 102.6 ± 30.0 to 61.0 ± 14.5 mg · dl-1 · h-1 (P < 0.05), especially in the latter postprandial period (AUC3-6; 56.2 ± 18.0 vs. 24.9 ± 8.9 mg · dl-1 · h-1, P < 0.025). ASP also reduced plasma glucose both in the mice with accelerated plasma triglyceride clearance and in those with relatively delayed triglyceride clearance (P < 0.025). Therefore, ASP alters postprandial triglyceride and glucose metabolism.

complement C3a; adipose tissue; glucose; free fatty acid; fat load


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