Phospholipase a2

Phospholipase a2 and Regeneration volume 36Article number: 7 Cite this article. Metrics details. Within the phospholipase A 2 PLA 2 superfamily that hydrolyzes phospholipids to yield fatty acids and lysophospholipids, phospholipase a2, the secreted PLA 2 sPLA 2 enzymes comprise the largest family that contains 11 isoforms in mammals.

Federal government websites often end in. The site is secure. The phospholipase A 2 PLA 2 superfamily consists of many different groups of enzymes that catalyze the hydrolysis of the sn-2 ester bond in a variety of different phospholipids. The products of this reaction, a free fatty acid, and lysophospholipid have many different important physiological roles. This review focuses on the superfamily of PLA 2 enzymes, and then uses three specific examples of these enzymes to examine the differing biochemistry of the three main types of these enzymes.

Phospholipase a2

The enzyme phospholipase A 2 EC 3. This particular phospholipase specifically recognizes the sn 2 acyl bond of phospholipids and catalytically hydrolyzes the bond, releasing arachidonic acid and lysophosphatidic acid. Upon downstream modification by cyclooxygenases or lipoxygenases , arachidonic acid is modified into active compounds called eicosanoids. Eicosanoids include prostaglandins and leukotrienes , which are categorized as anti-inflammatory and inflammatory mediators. PLA2 enzymes are commonly found in mammalian tissues as well as arachnid, insect, and snake venom. Due to the increased presence and activity of PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site. Additional types of phospholipases include phospholipase A 1 , phospholipase B , phospholipase C , and phospholipase D. Phospholipases A 2 include several unrelated protein families with common enzymatic activity. Two most notable families are secreted and cytosolic phospholipases A 2. The extracellular forms of phospholipases A 2 have been isolated from different venoms snake , [5] bee , and wasp , from virtually every studied mammalian tissue including pancreas and kidney as well as from bacteria.

The catalytic domain is shown on the right with the cap region colored yellow, and the lid region — colored magenta. Nat Rev Mol Cell Biol. Sorry, phospholipase a2 shareable link is not currently available for this article.

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Federal government websites often end in. The site is secure. The data presented in this review were compiled from the cited work. Details about the adapted figures and graphic are available upon request. The phospholipase A2 PLA2 superfamily of phospholipase enzymes hydrolyzes the ester bond at the sn-2 position of the phospholipids, generating a free fatty acid and a lysophospholipid. The superfamily of PLA2 comprises at least six big families of isoenzymes, based on their structure, location, substrate specificity and physiologic roles. Phospholipase A2 PLA2 belongs to the lipolytic family of enzymes that hydrolyze the ester bond at the sn-2 position of the phospholipids.

Phospholipase a2

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April Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. The products of this reaction, a free fatty acid, and lysophospholipid have many different important physiological roles. Acylglycerol transacylase, triacyglycerol lipase. Open in a separate window. Methylation of histidine in pancreatic phospholipase A2. Abnormal levels of potent PAF are also associated with neurological damage. Notably, in humans, Pla2g5 gene polymorphisms correlate with the LDL levels in subjects with type 2 diabetes or obesity [ 35 , 36 ]. Abe A, Shayman JA. Role of cytosolic phospholipase A 2 in allergic response and parturition. Obesity Silver Spring. The caspase truncated enzyme was hyperactive and reduced cell viability when overexpressed in HEK cells [ ]. Implications of a consensus recognition site for phosphatidylcholine separate from the active site in cobra venom phospholipases A2. For reviews of the other GVI enzymes see [ 1 ].

The enzyme phospholipase A 2 EC 3.

Physiological roles of group X-secreted phospholipase A 2 in reproduction, gastrointestinal phospholipid digestion, and neuronal function. Molecular characterization of cytosolic phospholipase A2-beta. An optimal enzyme inhibitor would specifically target PLA2 activity on neural cell membranes already under oxidative stress and potent inflammation. Methylation of histidine in pancreatic phospholipase A2. Lambeau G, Gelb MH. More recently, others have found that GVIA iPLA 2 is involved in cell proliferation [ — ], mediating cell growth [ 28 ], apoptosis [ ] and glucose-induced insulin secretion [ ]. His , Asp, and 2 water molecules are also shown. Rather, sPLA 2 -V contributes to controlling the quality of the lipids, i. Find articles by Edward A. The interaction of phospholipase A2 with phospholipids analogues and inhibitors. Recent studies using mice that have been gene manipulated for sPLA 2 s have begun to reveal their distinct and unique roles in various biological events [ 7 — 14 ]. This mechanism explains the pH dependence of these enzymes at around 7—9. The enzyme hydrolyzes substrate through the formation of a serine-acyl intermediate [ 76 , 77 ]. PLA 2 reaction.