S‐100 Modulates Ca2+‐Independent Phosphorylation of an Endogenous Protein (Mr= 19K) in Brain
- 1 July 1984
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 43 (1) , 256-260
- https://doi.org/10.1111/j.1471-4159.1984.tb06704.x
Abstract
A new brain enzyme (tentatively named protein kinase X), which catalyzes protamine phosphorylation modulated by S-100, was reported recently. An endogenous substrate protein (MW = 19K [kilodalton]) for protein kinase X was isolated from brain by means of S-100-Sepharose 4B affinity chromatography. S-100, but not calmodulin, promoted phosphorylation of the 19K MW protein in a Ca2+-independent manner, and this reaction was inhibited by gossypol. The substrate protein, localized in the particulate fraction, was presented at a much higher level in brain from adult than neonatal rats (2-day-old), a developmental change similar to that seen for protein kinase X. A protein phosphorylation system modulated by S-100 exists in brain, and that this process may be involved in regulation of certain neural functions.Keywords
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