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仅FAT/CD36表达不足以增强细胞对油酸的摄取。

FAT/CD36 expression alone is insufficient to enhance cellular uptake of oleate.

作者信息

Eyre Nicholas S, Cleland Leslie G, Mayrhofer Graham

机构信息

School of Molecular and Biomedical Science, University of Adelaide, Adelaide, SA, Australia.

出版信息

Biochem Biophys Res Commun. 2008 Jun 6;370(3):404-9. doi: 10.1016/j.bbrc.2008.02.164. Epub 2008 Mar 24.

Abstract

Fatty acid translocase (FAT/CD36) is one of several proteins implicated in receptor-mediated uptake of long-chain fatty acids (LCFAs). We have tested whether levels of FAT/CD36 correlate with cellular oleic acid import, using a Tet-Off inducible transfected CHO cell line. Consistent with our previous findings, FAT/CD36 was enriched in lipid raft-derived detergent-resistant membranes (DRMs) that also contained caveolin-1, the marker protein of caveolae. Furthermore in transfected cells, plasma membrane FAT/CD36 co-localized extensively with the lipid raft-enriched ganglioside GM1, and partially with a caveolin-1-EGFP fusion protein. Nevertheless, even at high levels of expression, FAT/CD36 did not affect uptake of oleic acid. We propose that the ability of FAT/CD36 to mediate enhanced uptake of LCFAs is dependent on co-expression of other proteins or factors that are lacking in CHO cells.

摘要

脂肪酸转运蛋白(FAT/CD36)是参与受体介导的长链脂肪酸(LCFA)摄取的几种蛋白质之一。我们使用四环素调控诱导转染的CHO细胞系,测试了FAT/CD36水平是否与细胞油酸摄取相关。与我们之前的发现一致,FAT/CD36在富含脂筏的耐去污剂膜(DRM)中富集,这些膜中还含有小窝蛋白-1,即小窝的标记蛋白。此外,在转染细胞中,质膜FAT/CD36与富含脂筏的神经节苷脂GM1广泛共定位,并与小窝蛋白-1-EGFP融合蛋白部分共定位。然而,即使在高表达水平下,FAT/CD36也不影响油酸的摄取。我们认为,FAT/CD36介导LCFA摄取增强的能力取决于CHO细胞中缺乏的其他蛋白质或因子的共表达。

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