PLA2G6: A Calcium-Independent Phospholipase A2 Isoform (G8398)

Target Name: PLA2G6

NCBI ID: G8398

PLA2G6

PLA2G6: A Calcium-Independent Phospholipase A2 Isoform

PLA2G6 (85/88 kDa calcium-independent phospholipase A2 isoform) is a protein that is expressed in various cell types, including neurons, endothelial cells, and epithelial cells. It is a member of the A2 family of phospholipase A2 isoforms and is characterized by its catalytic active site, which is located at the N-terminus of the protein.

PLA2G6 is a calcium-independent enzyme, which means that it does not require calcium ions to function. This is important because many cellular processes that involve the regulation of calcium ions, such as muscle contractions and nerve function, are calcium-dependent. By not requiring calcium ions, PLA2G6 can be found in a wide range of cellular processes that are not influenced by the availability of calcium ions.

One of the unique features of PLA2G6 is its catalytic active site. The active site is located at the N-terminus of the protein and is composed of a helical region and a catalytic domain. The helical region is responsible for the overall stability of the protein and is involved in the formation of a disulfide bond that links the catalytic domain to the rest of the protein. The catalytic domain is the active site of the enzyme and is responsible for the catalytic activity of PLA2G6.

The catalytic activity of PLA2G6 is dependent on the presence of calcium ions. When calcium ions are present in the surrounding solution, PLA2G6 can catalyze a variety of lipid metabolism reactions, including the breakdown of phosphatidylcholine and the addition of the phosphate groups to lipids. These reactions are important for the cellular functions of the cell, such as the production of energy and the maintenance of cell structure.

PLA2G6 is also known as the isoform A2 (A2) of the phospholipase A2 family. Isoforms A2 and A3 (86/88 kDa) are different from isoform A1 (74 kDa) in their catalytic activity and subcellular localization. Isoform A2 is mainly found in the cytosol, whereas isoform A3 is mainly found in the endoplasmic reticulum.

PLA2G6 is a potential drug target or biomarker because of its unique catalytic activity and subcellular localization. The active site of PLA2G6 makes it a attractive target for small molecules that can modulate its catalytic activity and/or its subcellular localization. Additionally, the fact that PLA2G6 is a calcium-independent enzyme makes it a unique target for small molecules that can modulate its activity without the need for calcium ions.

In conclusion, PLA2G6 is a protein that is characterized by its catalytic active site and its calcium-independent nature. It is expressed in various cell types and is involved in a wide range of cellular processes that are important for the maintenance of cell structure and function. PLA2G6 is a potential drug target or biomarker due to its unique catalytic activity and subcellular localization, and further research is needed to understand its role in cellular processes and its potential as a therapeutic agent.

Protein Name: Phospholipase A2 Group VI

Functions: Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity respectively), producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:9417066, PubMed:10092647, PubMed:10336645, PubMed:20886109). Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position (PubMed:10092647, PubMed:10336645, PubMed:20886109). Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity) (PubMed:20886109). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (PubMed:23533611). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species (By similarity). Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (By similarity). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (PubMed:20886109). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (By similarity). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (PubMed:18208975). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-protein receptors in various cell types (By similarity). Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent pro-inflammatory signaling lipid (By similarity). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (By similarity)

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