Regulatory effects of S-100 protein and parvalbumin on protein kinases and phosphoprotein phosphatases from brain and skeletal muscle.
In the eluted fractions of histone-treated crude extracts separated by Sephadex G-200 filtration, multiple protein kinase (PK) activities, including three from brain and two from skeletal muscle, were augmented by both S-100 protein and parvalbumin on the phosphorylation of endogenous substrates. One additional PK activity suppressed by both S-100 and parvalbumin was also found in muscle. In comparison, phosphoprotein phosphatases (PPase), which were also prepared by the same procedure of initial step of histone-treatment followed by the steps of Bio-Gel P-6DG for brain and DNA-cellulose for muscle, were all activated by S-100 while inhibited by parvalbumin and phosphatidylserine.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002850:Chromatography, Gel; D004789:Enzyme Activation / Q000187:drug effects; D066298:In Vitro Techniques; D008297:Male; D009124:Muscle Proteins / Q000494:pharmacology*; D009132:Muscles / Q000201:enzymology*; D010320:Parvalbumins / Q000494:pharmacology*; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits; D009418:S100 Proteins / Q000494:pharmacology*
D009124:Muscle Proteins; D010320:Parvalbumins; D047428:Protein Kinase Inhibitors; D009418:S100 Proteins; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases