| First Author | Starodub O | Year | 2000 |
| Journal | Am J Physiol Cell Physiol | Volume | 279 |
| Issue | 4 | Pages | C1259-69 |
| PubMed ID | 11003606 | Mgi Jnum | J:296154 |
| Mgi Id | MGI:6467919 | Doi | 10.1152/ajpcell.2000.279.4.C1259 |
| Citation | Starodub O, et al. (2000) Sterol carrier protein-2 localization in endoplasmic reticulum and role in phospholipid formation. Am J Physiol Cell Physiol 279(4):C1259-69 |
| abstractText | 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 [(3)H]oleic acid into phospholipids and triacylglycerols of overexpressing cells 1.6- and 2.5-fold, respectively, stimulated microsomal incorporation of [1-(14)C]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. |
