Regulatory effects of S-100 protein and parvalbumin on protein kinases and phosphoprotein phosphatases from brain and skeletal muscle |
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Authors: | Wu-Nan Kuo Thomas Blake Ijaz R. Cheema Jorge Dominguez James Nicholson Katia Puente Phaedra Shells Jimmie Lowery |
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Affiliation: | (1) Division of Science and Mathematics, Bethune-Cookman College, 32015 Daytona Beach, FL, USA |
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Abstract: | Summary 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. |
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Keywords: | S-100 protein parvalbumin protein kinase phosphoprotein phosphatase brain skeletal muscle |
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