Sterol carrier protein-2 suppresses microsomal acyl-CoA hydrolysis |
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Authors: | Jolly Christopher A Chao Hsu Kier Ann B Billheimer Jeffrey T Schroeder Friedhelm |
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Institution: | (1) Department of Physiology and Pharmacology, Texas A&M University, TVMC, College Station, TX 77843-4466, USA;(2) Department of Pathobiology, Texas A&M University, TVMC, College Station, TX 77843-4466, USA;(3) Cardiovascular Department, DuPont Merck Pharmaceutical Company, Experimental Station 400-3231, Wilmington, DE 19898-0400, USA |
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Abstract: | Although sterol carrier protein 2 (SCP-2) has long been regarded primarily as a sterol transfer protein, its actual physiological function is not known. The recent discovery that SCP-2 binds long chain fatty acyl-CoAs (LCFA-CoAs) with high affinity suggests additional roles for SCP-2 in cellular utilization of LCFA-CoAs for synthesis of glycerides and cholesterol esters. Concomitant to these anabolic pathways, LCFA-CoAs are also degraded by cellular hydrolases. The purpose of the work presented herein was to determine if SCP-2 altered the aqueous pool of LCFA-CoA by (i) extracting LCFA-CoA from microsomal membranes, and (ii) protecting LCFA-CoA from microsomal hydrolase activity. The data demonstrated for the first time that SCP-2 increases the aqueous pool of oleoyl-CoA by increasing the aqueous/membrane distribution oleoyl-CoA by 2.4-fold. In addition, SCP-2 inhibited the hydrolysis of oleoyl-CoA by microsomal acyl-CoA hydrolase 1.6-2.4 fold, depending on the concentration of oleoyl-CoA. By simultaneously extracting LCFA-CoA from membranes and inhibiting LCFA-CoA degradation SCP-2 may potentiate LCFA-CoA transacylation and modulate the role of LCFA-CoAs as intracellular signaling molecules. |
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Keywords: | sterol carrier protein-2 fatty acid fatty acyl-CoA fluorescence hydrolase microsomes |
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