Phosphatidylcholine-specific phospholipase C (PC-PLC)

Phosphatidylcholine-specific phospholipase C (PC-PLC) is an enzyme present in bacteria, plants, and mammals that catalyzes the hydrolysis of phosphatidylcholine, a major cell membrane phospholipid, into diacylglycerol (DAG) and phosphocholine. This reaction is a pivotal step in cellular signaling, with DAG activating protein kinase C (PKC), which impacts pathways governing cell proliferation, differentiation, apoptosis, and immune functions. PC-PLC is implicated as a pathogenic factor in various diseases, acting through modulation of growth factor receptors (such as EGFR, HER2, CXCR4) and serving as a molecular adapter at the plasma membrane, which can be targeted for therapeutic intervention in cancer and cardiovascular diseases. Inhibitors like D609 have shown promise in preclinical models by downregulating oncogenic signaling and disease progression. The protein also regulates immune responses by modulating CD16 in natural killer cells and participates in atherogenic inflammatory signaling. Research continues to elucidate the molecular structure and therapeutic potential of PC-PLC inhibition across diseases.

Other names

Phosphatidylcholine phospholipase CPC-PLCType C phospholipase

Inhibition of signal transduction by blocking DAG and phosphocholine production Downregulation of EGFR and HER2 signaling via physical interaction and membrane localization disruption (notably D609) Modulation of PKC/NF-κB activation (in cardiovascular disease)