PLA2G1B: Key Enzyme in Phospholipid Production and Breakdown (G5319)

Target Name: PLA2G1B

NCBI ID: G5319

PLA2G1B: Key Enzyme in Phospholipid Production and Breakdown

PLA2G1B, also known as phospholipase A2 group IB, is a protein that is expressed in various cell types throughout the body, including platelets, endothelial cells, and cancer cells. It is a key enzyme in the phosphatidylcholine (PA) synthesis pathway , which is a critical step in the production of phospholipids, which are the major components of cell membranes.

PLA2G1B is a 23-kDa protein that consists of two distinct subunits, A and B. The A subunit consists of 116 amino acids, while the B subunit consists of 82 amino acids. Both subunits contain a catalytic active site, a substrate recognition site, and a carboxylic acid terminator.

PLA2G1B is involved in the production of PA from its precursor, phosphatidylcholine (PCh), which is derived from the soybean oil. The PCh is first converted to its active form, P-Choline, by the addition of a phosphate group. This conversion occurs via the action of the enzyme PLA2G1B, which adds a phosphate group to the carbon atom of the PCh side chain.

Once the PCh has been converted to P-Choline, it can be further modified to produce different types of phospholipids, including PA. The conversion of PCh to PA is a critical step in the production of cell membranes, as cell membranes are the physical and functional barriers that regulate the movement of substances into and out of cells.

PLA2G1B is also involved in the breakdown of PA, which is a vital component of cell membranes and plays a crucial role in maintaining the integrity of the cell membrane. The breakdown of PA occurs via the action of the enzyme PLA2G1B, which adds a phosphate group to the carbon atom of the PA molecule. This modification allows the enzymes of the PA synthesis pathway to remove the phosphate group, which in turn leads to the breakdown of PA and its release from the cell membrane.

In addition to its role in the production and breakdown of PA, PLA2G1B is also involved in the regulation of various cellular processes, including cell signaling, inflammation, and metabolism. For example, PLA2G1B has been shown to play a role in the regulation of angiogenesis , the formation of new blood vessels, and the development of cancer.

PLA2G1B is also a potential drug target in the treatment of various diseases. For example, PLA2G1B has been shown to be involved in the development and progression of cancer, including breast, ovarian, and prostate cancers. Therefore, inhibitors of PLA2G1B have been shown to be effective in treating these cancers. Additionally, PLA2G1B has also been shown to be involved in the regulation of inflammation, and inhibitors of PLA2G1B have been shown to be effective in treating various inflammatory disorders.

In conclusion, PLA2G1B is a highly conserved protein that is involved in the production and breakdown of phospholipids, which are critical components of cell membranes. PLA2G1B is a potential drug target for the treatment of various diseases, including cancer and inflammatory disorders. Further research is needed to fully understand the role of PLA2G1B in cellular processes and its potential as a drug target.

Protein Name: Phospholipase A2 Group IB

Functions: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (PubMed:1420353, PubMed:10681567, PubMed:17603006). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (PubMed:1420353, PubMed:10681567, PubMed:17603006). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (PubMed:7721806, PubMed:25335547). Upon binding to the PLA2R1 receptor can regulate podocyte survival and glomerular homeostasis (PubMed:25335547). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity)

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