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A potent inhibitor of protein kinase C (PKC), inhibitor protein-1 (KCIP-1), isolated from sheep brain has been shown to consist of eight isoforms by reverse-phase HPLC. Direct protein sequence analysis has revealed these to be the same as those of 14-3-3 protein, described as an activator of tyrosine and tryptophan hydroxylases involved in neurotransmitter biosynthesis. The N-termini of KCIP-1 isoforms were shown to be acetylated, and secondary structure predictions revealed a high degree of alpha-helix with an amphipathic nature. KCIP-1 showed no inhibitory activity towards protein kinase M (the catalytic fragment of PKC) and had no effect on the activities of three other protein kinases, cAMP-dependent protein kinase, Ca2+/calmodulin-dependent protein kinase II and casein kinase 2. Four forms of KCIP-1 were shown to be substrates for PKC in vitro, but none were phosphorylated by the other protein kinases mentioned above.

Original publication

DOI

10.1111/j.1432-1033.1992.tb16946.x

Type

Journal article

Journal

European journal of biochemistry

Publication Date

06/1992

Volume

206

Pages

453 - 461

Addresses

Laboratory of Protein Structure, National Institute for Medical Research, Mill Hill, London, England.

Keywords

Animals, Sheep, Tyrosine 3-Monooxygenase, Protein Kinases, Protein Kinase C, 14-3-3 Proteins, Nerve Tissue Proteins, Cross-Linking Reagents, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Spectrometry, Mass, Fast Atom Bombardment, Sequence Alignment, Brain Chemistry, Amino Acid Sequence, Phosphorylation, Molecular Sequence Data, Calcium-Calmodulin-Dependent Protein Kinases