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 ?
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.
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.
In our study, 1 and 5 mM nickel in the presence of fibrinogen induced platelet aggregation (independently of protein kinase C activation) and secretion.
Intracellular lead may also activate protein kinase C and various calmodulin-dependent enzymes, such as calmodulin-dependent protein kinase, phosphodiesterase, and calcineurin, at picomolar concentrations.
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