protein kinase C


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protein kinase C

any of a number of cytoplasmic calcium-activated kinases involved in numerous processes, including hormonal binding, platelet activation, and tumor promotion.

pro·tein kin·ase C

(prō'tēn kī'nās)
Any of several cytoplasmic calcium-activated kinases involved in numerous processes, including hormonal binding, platelet activation, and tumor promotion.

kinase

1. a subclass of the transferases, comprising the enzymes that catalyze the transfer of a high-energy group from a donor (usually ATP) to an acceptor, and named, according to the acceptor, as creatine kinase, fructokinase, etc.
2. an enzyme that activates a zymogen, and named, according to its source, as enterokinase, streptokinase, etc.

protein k's
cellular enzymes which utilize ATP to phosphorylate proteins, usually at a selected OH group of serine, threonine or tyrosine residue in the protein, so as to increase or decrease the activity of the protein.
protein kinase C
membrane bound protein kinase designated C because it requires Ca2+ and phosphatidyl serine for its activity. Activated by sn-1,2-diacylglycerol (DAG) produced from phosphatidyl inositol 4,5-bisphosphate. Phosphorylates target proteins such as the insulin receptor, β-adrenergic receptor, glucose transporter, HMG-CoA reductase, cytochrome P-450 and tyrosine hydroxylase.
References in periodicals archive ?
The involvement of lipid activators of protein kinase C in the induction of ZIF268 in PC12 cells exposed to lead.
Analysis of differential effects of Pb2+ on protein kinase C isozymes.
I am particularly excited about the company's recently initiated Phase I/II clinical study of its lead therapeutic program, KAI-9803, a protein kinase C inhibitor to reduce reperfusion injury associated with acute myocardial infarction.
The treatment of washed platelets with a protein kinase C inhibitor, Ro 31-8220 (10 [micro]M), did not modify the aggregometrical response to 1 mM Ni[Cl.
KAI Pharmaceuticals, with headquarters in South San Francisco, California, addresses unmet medical needs with the development of therapeutics that selectively modulate protein kinase C (PKC) enzymes without simultaneous activation or inhibition of closely related enzymes.
The up-regulation of L- and N-type calcium channels in PC12 cells by ethanol is due in part to effects on protein kinase C (PKC); chronic exposure to ethanol increases PKC-mediated phosphorylation and the abundance of PKC [Delta] and isozymes.
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