Details

Autor(en) / Beteiligte

• TOKER, A
• SELLERS, L. A
• AMESS, B
• PATEL, Y
• HARRIS, A
• AITKEN, A

Titel

Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from sheep brain : amino acid sequence of phosphorylated forms

Ist Teil von

• European journal of biochemistry, 1992-06, Vol.206 (2), p.453-461

Ort / Verlag

Oxford: Blackwell

Erscheinungsjahr

1992

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.