PRKCA Protein, Human (Active, sf9, GST)

PKC alpha is a calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that regulates cell proliferation, apoptosis, differentiation, migration, adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function, and inflammation by directly phosphorylating targets like RAF1, BCL2, CSPG4, and TNNT2/CTNT or activating signaling cascades involving MAPK1/3 (ERK1/2) and RAP1GAP. It promotes cell growth in glioma cells via RAF1 phosphorylation or CDKN1A upregulation, while inducing cell cycle arrest in PMA-stimulated intestinal cells. During macrophage differentiation, it translocates to the nucleus and modulates desmosomal adhesion post-wounding. PKC alpha enhances cell motility by phosphorylating CSPG4 and is overexpressed in cancers, acting as an oncogene. It negatively regulates myocardial contractility but positively controls angiogenesis and platelet aggregation. The kinase phosphorylates cardiac troponin T (TNNT2/CTNT) to reduce myocardial contractility and stabilizes VEGFA mRNA to promote angiogenesis. In platelets, it mediates granule release via CD36/GP4 and activates ITGA2B-ITGB3 integrin through RAP1GAP. PKC alpha also modulates LPS-induced macrophage functions and negatively regulates NF-κB via IL1A-dependent NFKBIA induction. It phosphorylates EIF4G1, KIT, and ATF2 to influence translation and transcription. Similar functions (By similarity) include SOCS2 phosphorylation for degradation and KLHL3 phosphorylation to disrupt WNK4 binding. Recent studies (PubMed:36040231) show it activates LRRK1 to regulate RAB proteins in intracellular trafficking.