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溶血磷脂酰基转移酶产生膜多样性。

Generation of membrane diversity by lysophospholipid acyltransferases.

机构信息

Department of Lipid Signaling Project, Research Institute, National Center for Global Health and Medicine, 1-21-1 Toyama, Shinjuku-ku, Tokyo 162-8655, Japan.

出版信息

J Biochem. 2013 Jul;154(1):21-8. doi: 10.1093/jb/mvt048. Epub 2013 May 21.

DOI:10.1093/jb/mvt048
PMID:23698096
Abstract

Glycerophospholipids are main components of cellular membranes and have numerous structural and functional roles to regulate cellular functions. Polyunsaturated fatty acids, such as arachidonic acid and eicosapentaenoic acid, are mainly located at the sn-2, but not the sn-1 position of glycerophospholipids in an asymmetrical manner and the fatty acid compositions at both the sn-1 and sn-2 positions differ in various cell types and tissues. Asymmetry and diversity of membrane glycerophospholipids are generated in the remodelling pathway (Lands' cycle), which are conducted by the concerted actions of phospholipases A2 (PLA2s) and lysophospholipid acyltransferases (LPLATs). The Lands' cycle was first reported in the 1950s. While PLA2s have been well characterized, little is known about the LPLATs. Recently, several laboratories, including ours, isolated LPLATs that function in the Lands' cycle from the 1-acylglycerol-3-phosphate O-acyltransferase family and the membrane bound O-acyltransferases family. In this review, we summarize recent studies on cloning and characterization of LPLATs that contribute to membrane asymmetry and diversity.

摘要

甘油磷脂是细胞膜的主要成分,具有许多结构和功能作用,以调节细胞功能。多不饱和脂肪酸,如花生四烯酸和二十碳五烯酸,主要以不对称的方式位于甘油磷脂的 sn-2 位,而不是 sn-1 位,并且在不同的细胞类型和组织中,sn-1 和 sn-2 位的脂肪酸组成不同。膜甘油磷脂的不对称性和多样性是通过磷脂酶 A2 (PLA2) 和溶血磷脂酰基转移酶 (LPLAT) 的协同作用在重塑途径(Lands' 循环)中产生的。Lands' 循环于 20 世纪 50 年代首次报道。虽然 PLA2 已经得到很好的描述,但对 LPLAT 知之甚少。最近,包括我们实验室在内的几个实验室从 1-酰基甘油-3-磷酸 O-酰基转移酶家族和膜结合 O-酰基转移酶家族中分离出了在 Lands' 循环中起作用的 LPLAT。在这篇综述中,我们总结了最近关于有助于膜不对称性和多样性的 LPLAT 克隆和特性的研究。

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