Santiago-García J, Mas-Oliva J
Instituto de Fisiología Celular, Universidad Nacional Autónoma de México.
Mol Cell Biochem. 1991 Jan 16;100(1):51-9. doi: 10.1007/BF00230809.
In contrast to several sterol carrier proteins isolated from soluble cytosolic fractions, a cholesterol transfer protein (CHTP) with an apparent molecular weight of 73,000 was isolated from a cardiac sarcolemmal fraction by detergent solubilization, column chromatography, and preparative electrophoresis using nondissociating polyacrylamide gels. This protein must be reconstituted into an artificial membrane in order to mediate cholesterol transfer activity. For the expression of its full activity, CHTP must also be present in the membrane in a multimeric form, since the monomer was shown not to be active. We believe this novel protein might represent an important molecule in the regulation of the homeostasis of cholesterol in cardiac sarcolemma.
与从可溶性胞质组分中分离出的几种固醇载体蛋白不同,通过去污剂增溶、柱色谱以及使用非解离聚丙烯酰胺凝胶的制备电泳,从心肌肌膜组分中分离出一种表观分子量为73,000的胆固醇转移蛋白(CHTP)。为了介导胆固醇转移活性,这种蛋白质必须重构到人工膜中。为了充分发挥其活性,CHTP还必须以多聚体形式存在于膜中,因为已证明单体没有活性。我们认为这种新蛋白可能是调节心肌肌膜胆固醇稳态的重要分子。