Glatz J F, van Nieuwenhoven F A, Luiken J J, Schaap F G, van der Vusse G J
Department of Physiology, Cardiovascular Research Institute Maastricht, The Netherlands.
Prostaglandins Leukot Essent Fatty Acids. 1997 Oct;57(4-5):373-8. doi: 10.1016/s0952-3278(97)90413-0.
A number of membrane-associated and cytoplasmic fatty acid-binding proteins (FABPs) are now being implicated in the cellular uptake and intracellular transport of long-chain fatty acids (FA). These proteins each have the capacity of non-covalent binding of FA, are present in tissues actively involved in FA metabolism, and are upregulated in conditions of increased cellular FA metabolism. To date, five distinct membrane FABPs have been described, ranging in mass from 22 to 88 kDa and each showing a characteristic tissue distribution. Evidence for involvement in cellular fatty acid uptake has been provided for several of them, because it was recently found that isolated cell lines transfected with 88-kDa putative fatty acid translocase (FAT; homologous to CD36) or with 63-kDa fatty acid-transport protein show an increased rate of FA uptake. The (at least nine) FABPs of cytoplasmic origin belong to a family of small (14-15 kDa) lipid binding proteins, all having a similar tertiairy structure but differing in binding properties and in tissue occurrence. The biological functions of the various FABPs, possibly exerted in a concerted action among them, comprise solubilization and compartmentalization of FA, facilitation of the cellular uptake and intracellular trafficking of FA, and modulation of mitosis, cell growth, and cell differentiation. In addition, the FABPs have been suggested to participate in and/or modulate FA-mediated signal transduction pathways and FA regulation of gene expression, and to prevent local high FA concentrations thereby contributing to the protection of cells against the toxic effects of FA. In conclusion, long-chain fatty acids are subject to continuous interaction with multiple proteins, which interplay influences their cellular metabolism.
目前，一些膜相关和细胞质脂肪酸结合蛋白（FABP）被认为与长链脂肪酸（FA）的细胞摄取和细胞内转运有关。这些蛋白均具有非共价结合FA的能力，存在于积极参与FA代谢的组织中，并且在细胞FA代谢增加的情况下会被上调。迄今为止，已描述了五种不同的膜FABP，质量范围从22至88 kDa，每种都显示出特征性的组织分布。其中一些已被证明参与细胞脂肪酸摄取，因为最近发现，用88 kDa推定脂肪酸转运蛋白（FAT；与CD36同源）或63 kDa脂肪酸转运蛋白转染的分离细胞系显示FA摄取速率增加。细胞质来源的（至少九种）FABP属于一个小（14 - 15 kDa）脂质结合蛋白家族，它们都具有相似的三级结构，但结合特性和组织分布不同。各种FABP的生物学功能可能在它们之间协同发挥作用，包括FA的溶解和分隔、促进FA的细胞摄取和细胞内运输，以及调节有丝分裂、细胞生长和细胞分化。此外，有人提出FABP参与和/或调节FA介导的信号转导途径以及FA对基因表达的调节，并防止局部FA浓度过高，从而有助于保护细胞免受FA的毒性作用。总之，长链脂肪酸与多种蛋白质持续相互作用，这种相互作用影响它们的细胞代谢。
