Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

Eur J Biochem

Publication Date

01/06/1992

Volume

206

Pages

453 - 461

Keywords

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