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pla2g7

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Official Full Name
phospholipase A2, group VII (platelet-activating factor acetylhydrolase, plasma)
Background
The PLA2G7 gene encodes platelet-activating factor (PAF) acetylhydrolase (EC 3.1.1.47), a secreted enzyme that catalyzes the degradation of PAF to inactive products by hydrolysis of the acetyl group at the sn-2 position, producing the biologically inactive products LYSO-PAF and acetate.
Synonyms
PLA2G7; phospholipase A2, group VII (platelet-activating factor acetylhydrolase, plasma); platelet-activating factor acetylhydrolase; LDL PLA2; PAFAH; LDL-PLA(2); gVIIA-PLA2; PAF 2-acylhydrolase; PAF acetylhydrolase; group-VIIA phospholipase A2; LDL-associated phospholipase A2; lipoprotein-associated phospholipase A2; 1-alkyl-2-acetylglycerophosphocholine esterase; 2-acetyl-1-alkylglycerophosphocholine esterase; PAFAD; LP-PLA2; LDL-PLA2; 1-alkyl-2-acetylglycerophosphochol; zgc:77563

Introduction

Lp-PLA2, also known as platelet-activating factor acetylhydrolase or type VIIA PLA2, is encoded by Pla2g7 gene and composes of 441 amino acids, which is a unique member of PLA2 super-family. Lp-PLA2 is a Ca2+-independent phospholipase belonging to phospholipase A2 superfamily. The initial association between the Lp-PLA2 levels and the risk of cardiovascular disease was reported by the WOSCOPS (West of Scotland Coronary Prevention Study), subsequent studies also successfully reproduced these observations. According to previous clinical and epidemiological studies, Lp-PLA2 is an inflammatory marker and a risk factor for mortality from coronary heart disease, stroke, and cardiovascular disease (CVD), some scientific researches in different animal models have also shown that increasing serum level of Lp-PLA2 can mitigate vascular inflammation and attenuate atherosclerosis.

Lp-PLA2 and Atherosclerosis

Lp-PLA2 is recognized as a pro-atherogenic enzyme responsible for regulating lipid metabolism and inflammatory respond because of its capability of hydrolyzing platelet activating factor (PAF) and LDLC, both of which are considered to be detrimental to vessel wall. Intriguingly, a substantial amount of studies have gradually reported that the activity or mass of Lp-PLA2 is positively associated with the severity of atherosclerosis and CV risk, both of which play crucial roles in the development and progress of atherosclerosis. The atherogenic effect of Lp-PLA2 is largely associated with conventional atherogenic-lipids, and the effect of Lp-PLA2 on cardiovascular system outweighs the so-call anti-atherogenesis effect and has been evidenced by large number of scientific and clinical research.

Lp-PLA2 Secretion and Circulation in the Blood-Stream

In the bloodstream, Lp-PLA2 circulates by two-thirds bounding to the LDLs and one-third to HDLs. Plasma ultracentrifugation leads to partial separation of Lp-PLA2 from the lipoproteins indicating the presence of a dissociable and a non-dissociable form of the enzyme. The transition between them might be the mechanisms regulating the activity of Lp-PLA2 in vivo. The association with HDL and LDL is controlled by post-translational chemical modifications: glycosylation of specific residues decreases the association of Lp-PLA2 and lipoproteins, even though these changes do not seem to influence the enzyme secretion by the cells.

Figure 1. Pathogenic role of lipoprotein-associated phospholipase A2 in atherosclerosis development.
(DOI: 10.4330/wjc.v7.i10.609)

References:

  1. Giuseppe Maiolino, Valeria Bisogni, Giacomo Rossitto and Gian Paolo Rossi. (2015) 'Lipoprotein-associated phospholipase A2 prognostic role in atherosclerotic complications', World J Cardiol, 7(10): 609-620.
  2. Anping Caia, Dongdan Zhengb, Ruofeng Qiub, WeiyiMaib and Yingling Zhoua. (2013) 'Lipoprotein-associated phospholipase A2 (Lp-PLA2): A novel and promising biomarker for cardiovascular risks assessment', Disease Markers, 34: 323-331.
  3. Gopal Kedihitlu Marathe, Chaitanya Pandit, Chikkamenahalli Lakshminarayana Lakshmikanth, Vyala Hanumanthareddy Chaithra, Shancy Petsel Jacob and Cletus Joseph Michael D’Souza. (2014) 'To hydrolyze or not to hydrolyze: the dilemma of plateletactivating factor acetylhydrolase', J. Lipid Res, 55: 1847-1854.