1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta 2 (Phospholipase C beta 2) (PLCB2)

Phospholipase C beta 2 (PLCB2) is a critical enzyme in the signal transduction pathways of human polymorphonuclear neutrophils (PMNs). The input provided, GPCR-stimulated PLC signaling in human PMNs – Ca2+ flux, describes the functional pathway where PLCB2 is the central effector. Upon the binding of chemoattractants to G protein-coupled receptors (GPCRs), PLCB2 is activated primarily by G protein beta-gamma subunits. It catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) into two second messengers: inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 then binds to receptors on the endoplasmic reticulum, triggering the rapid release of calcium ions into the cytosol, a process known as Ca2+ flux. This calcium surge is essential for neutrophil activation, including the release of reactive oxygen species and directed migration toward sites of infection. While PLCB2 is a vital component of the inflammatory response, its overactivation is linked to chronic inflammatory conditions, making it a subject of interest for therapeutic modulation. Most current drugs target the upstream GPCRs, but direct PLC inhibitors like Edelfosine are used in research to study this signaling node (Source: UniProt P16885; PubMed: 10866654, 21907142).

Other names

Phosphoinositide phospholipase C-beta-2PLC-beta-2Phospholipase C-beta-2PLC-B2

Phospholipase C inhibition