Inhibition of protein kinase C from polymorphonuclear neutrophils by long chain acyl coenzyme A and counteraction by Mg-ATP.
The Ca2+- and phospholipid-dependent protein kinase (protein kinase C) from bovine polymorphonuclear neutrophils was inhibited by micromolar amounts of long chain acyl-CoAs. The extent of inhibition at a given concentration of the acyl-CoAs depended on the length of the chain. A chain length of at least 12C was required for inhibition. Inhibition of protein kinase C activity was counteracted specifically by Mg-ATP.
D000214:Acyl Coenzyme A / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D009504:Neutrophils / Q000201:enzymology*; D010171:Palmitoyl Coenzyme A / Q000494:pharmacology; D011493:Protein Kinase C / Q000037:antagonists & inhibitors* / Q000378:metabolism; D013329:Structure-Activity Relationship
D000214:Acyl Coenzyme A; D010171:Palmitoyl Coenzyme A; D000255:Adenosine Triphosphate; D011493:Protein Kinase C