E-NTPase/NTPDase在脂肪/CD36介导的脂肪酸摄取中的调节作用。

Regulatory role of E-NTPase/NTPDase in fat/CD36-mediated fatty acid uptake.

作者信息

Kannan Subburaj

机构信息

Division of Gastroenterology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

出版信息

Cell Biol Int. 2003;27(2):147-51. doi: 10.1016/s1065-6995(02)00294-9.

DOI:10.1016/s1065-6995(02)00294-9

PMID:12662971

Abstract

Fatty acid translocase (FAT)/CD36-mediated long-chain fatty acid uptake in human umbilical vessel endothelial cells is associated with as yet uncharacterized translocase activity. The molecular mechanism of its function is not yet understood. Numerous attempts to purify rat cardiac sarcolemmal E-NTPase (an integral membrane protein also referred to as ecto-Ca(2+)/Mg(2+)ATPase) have revealed a complete amino acid sequence identity for FAT/CD36 protein. The most striking observation is that purified CD36 from human platelets shows significant E-NTPase activity. In view of recent progress in understanding CD36 functional properties, an attempt is made in this article to illustrate the point that association of E-NTPase (possibly extracellular Ca(2+)/Mg(2+)nucleotide triphosphate diphosphohydrolase) activity with CD36 may be of potential functional significance.

摘要

脂肪酸转位酶（FAT）/CD36介导的人脐静脉内皮细胞对长链脂肪酸的摄取与尚未明确的转位酶活性有关。其功能的分子机制尚不清楚。众多纯化大鼠心肌肌膜E-NTP酶（一种也称为胞外Ca(2+)/Mg(2+)ATP酶的整合膜蛋白）的尝试揭示了FAT/CD36蛋白的完整氨基酸序列同一性。最引人注目的发现是，从人血小板中纯化的CD36具有显著的E-NTP酶活性。鉴于在理解CD36功能特性方面的最新进展，本文试图阐明E-NTP酶（可能是胞外Ca(2+)/Mg(2+)核苷酸三磷酸二磷酸水解酶）活性与CD36的关联可能具有潜在功能意义这一观点。