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Am J Physiol Cell Physiol 279: C1259-C1269, 2000;
0363-6143/00 $5.00
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Vol. 279, Issue 4, C1259-C1269, October 2000

Sterol carrier protein-2 localization in endoplasmic reticulum and role in phospholipid formation

O. Starodub1, C. A. Jolly2, B. P. Atshaves2, J. B. Roths1, E. J. Murphy2, A. B. Kier1, and F. Schroeder2

1 Department of Pathobiology and 2 Department of Physiology and Pharmacology, Texas A&M University, College Station, Texas 77843-4466

Although sterol carrier protein-2 (SCP-2; also called nonspecific lipid transfer protein) binds fatty acids and fatty acyl-CoAs, its role in fatty acid metabolism is not fully understood. L-cell fibroblasts stably expressing SCP-2 were used to resolve the relationship between SCP-2 intracellular location and fatty acid transacylation in the endoplasmic reticulum. Indirect immunofluorescence double labeling and laser scanning confocal microscopy detected SCP-2 in peroxisomes > endoplasmic reticulum > mitochondria > lysosomes. SCP-2 enhanced incorporation of exogenous [3H]oleic acid into phospholipids and triacylglycerols of overexpressing cells 1.6- and 2.5-fold, respectively, stimulated microsomal incorporation of [1-14C]oleoyl-CoA into phosphatidic acid in vitro 13-fold, and exhibited higher specificity for unsaturated versus saturated fatty acyl-CoA. SCP-2 enhanced the rate-limiting step in microsomal phosphatidic acid biosynthesis mediated by glycerol-3-phosphate acyltransferase. SCP-2 also enhanced microsomal acyl-chain remodeling of phosphatidylethanolamine up to fivefold and phosphatidylserine twofold, depending on the specific fatty acyl-CoA, but had no effect on other phospholipid classes. In summary, these results were consistent with a role for SCP-2 in phospholipid synthesis in the endoplasmic reticulum.

fluorescence; microscopy; peroxisomes


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