Structure and function of phosphatidylserine-specific phospholipase A1

被引：101

作者：

Aoki, J ^{[1
]}

Nagai, Y ^{[1
]}

Hosono, H ^{[1
]}

Inoue, K ^{[1
]}

Arai, H ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Pharmaceut Sci, Bunkyo Ku, Tokyo 1130033, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2002年 / 1582卷 / 1-3期

关键词：

phospholipase A(1); phosphatidylserine; lysophosphatidylserine; mast cell;

D O I：

10.1016/S1388-1981(02)00134-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Phospholipase A(1) (PLA(1)) is an enzyme that hydrolyzes the sn-1 fatty acids from phospholipids and produces 2-acyl-lysophospholipids. Although PLA(1) activities are detected in many tissues and cell lines, a limited number of PLA(1)s have been purified and cloned so far. These include phosphatidylserine (PS)-specific PLA(1) (PS-PLA(1)) from rat platelets, PLA(1) from vespid venom, and phosphatidic acid (PA)preferential PLA(1) (PA-PLA(1)). Structurally, the former two PLA(1)s belong to the lipase family, where they form a subfamily among the lipase family. An alignment of the PLA(1)s with other members of the lipase family revealed two molecular characteristics of PLA(1): the presence of extremely short lids and deleted 139 loops. The two surface loops have been implicated in the ligand recognition in human pancreatic lipase (PL) and guinea pig PL-related protein 2. Under physiological conditions, accessibility of PS-PLA(1) to its substrate is limited as it is a secreted enzyme and PS is normally located in the inner leaflet of the lipid bilayer. However, PS-PLA(1) efficiently hydrolyzes PS exposed on the surface of cells such as apoptotic cells and activated platelets, and produces 2-acyl-lysophosphatidylserine (lysoPS), which is a lipid mediator for mast cells, T cells and neural cells. Identification of PS-PLA(1) reveals the presence of PLA, subfamily within the lipase family and suggests that PLA(1) has a role in the production of lysophospholipid mediators. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：26 / 32

页数：7

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