Modulation of the catalytic subunit of cyclic AMP-dependent protein kinase by calmodulin, S-100 protein, parvalbumin and troponin

The activity of the catalytic subunit of cyclic AMP-dependent protein kinase (A-PK), utilizing type II-S, III-S histone or protamine (free base) as a substrate, was augmented in the presence of regulatory protein including calmodulin, S-100 protein, parvalbumin, or troponin. However, inhibition by c...

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Bibliographic Details
Published inCytobios Vol. 46; no. 186-187; p. 139
Main Authors Kuo, W N, Dominguez, J L, Shabazz, K A, White, D J, Nicholson, J, Puente, K, Shells, P, Redding, C, Blake, T, Sen, S
Format Journal Article
LanguageEnglish
Published England 1986
Subjects
Animals
Calmodulin - pharmacology
Cattle
Histones - metabolism
Kinetics
Macromolecular Substances
Magnesium - pharmacology
Muscle Proteins - pharmacology
Parvalbumins - pharmacology
Protein Kinases - metabolism
Rabbits
S100 Proteins - pharmacology
Substrate Specificity
Troponin - pharmacology
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Summary:The activity of the catalytic subunit of cyclic AMP-dependent protein kinase (A-PK), utilizing type II-S, III-S histone or protamine (free base) as a substrate, was augmented in the presence of regulatory protein including calmodulin, S-100 protein, parvalbumin, or troponin. However, inhibition by calmodulin or S-100 but stimulation by parvalbumin or troponin on this A-PK subunit was observed when II-S histone was replaced by V-S, VI-S, VII-S, or VIII-S histone. In addition, the stimulatory effect of calmodulin or S-100 on this A-PK subunit utilizing III-S histone was greatly diminished when half the dose of III-S was replaced by other histones in a bi-mixed form.
ISSN:0011-4529