Specificity of the glycolipid transfer protein from pig brain.
Specificity of the glycolipid transfer protein from pig brain.
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猪脑糖脂转移蛋白的特异性。
DOI：
10.1016/s0021-9258(18)89115-3
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Terukatsu Sasaki
中科院分区：
文献类型：
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作者：
K. Yamada;Akira Abe;Terukatsu Sasaki
研究了猪脑糖脂转移蛋白促进脂质转移反应的脂质特异性。脂质转移是通过测定放射性同位素标记的脂质从供体脂质体转移到受体脂质体或线粒体来测量的。只要有可能，脂质体就含有1摩尔%的脂质，其转移正在研究中。该转移蛋白可加速葡萄糖神经酰胺、半乳糖神经酰胺（GalCer）、乳糖神经酰胺（LacCer）、半乳糖神经酰胺3-硫酸盐、globotriaosyl神经酰胺、LacCer硫酸盐、唾液酰-LacCer、globotetraosyl神经酰胺和gloopentaosyl神经酰胺的转移。鞘糖脂的糖链长度与转移速率成反比关系。除了鞘糖脂外，转移蛋白还促进半乳糖二酰基甘油、二乳糖二酰基甘油、葡萄糖二酰基甘油和二葡萄糖二酰基甘油的转移。这种蛋白质不能促进二甘露二酰基甘油的转移。高盐氧化和随后还原的GalCer和LacCer衍生物的转移是由转移蛋白促进的。GalCer的衍生物的转移速率比GalCer低，而LacCer的衍生物的转移速率比LacCer高。转移蛋白不能促进磷脂酰胆碱、磷脂酰肌醇、胆固醇或油酸胆固醇的转移。这些结果表明，猪脑糖脂转移蛋白对直接与神经酰胺或二酰基甘油相连的糖渣中的羟基具有特异性。与这些疏水基团相连的葡萄糖或半乳糖的存在使糖脂可通过蛋白质转移。
Lipid specificity has been studied in the lipid transfer reaction facilitated by the glycolipid transfer protein from pig brain. The lipid transfer was measured by determining the transfer of a radioisotopically labeled lipid from donor liposomes to either acceptor liposomes or mitochondria. Whenever possible, the liposomes contained 1 mol % of the lipid whose transfer was under study. The transfer protein accelerates the transfer of glucosylceramide, galactosylceramide (GalCer), lactosylceramide (LacCer), galactosylceramide 3-sulfate, globotriaosylceramide, LacCer sulfate, sialosyl-LacCer, globotetraosylceramide, and globopentaosylceramide. An inverse relationship is found between the length of sugar chains in glycosphingolipids and the transfer rates. In addition to the glycosphingolipids, the transfer protein facilitates the transfer of galactosyldiacylglycerol, digalactosyldiacylglycerol, glucosyldiacylglycerol, and diglucosyldiacylglycerol. The protein does not facilitate the transfer of dimannosyldiacylglycerol. The transfer of periodate-oxidized and subsequently reduced derivatives of GalCer and LacCer is facilitated by the transfer protein. The derivatives of GalCer are transferred at lower rates than GalCer, whereas the derivatives of LacCer are transferred at higher rates than LacCer. The transfer protein does not facilitate the transfer of phosphatidylcholine, phosphatidylinositol, cholesterol, or cholesteryloleate. These results suggest that the glycolipid transfer protein from pig brain has specificity to hydroxyl groups present in the sugar residue directly linked to either ceramide or diacylglycerol. The presence of glucose or galactose linked to these hydrophobic moieties makes the glycolipid transferable by the protein.