Isoform specificity of activators and inhibitors of protein kinase C γ and δ

FEBS Letters

Keenan, Carolyn¹  Goode, Nigel²  Pears, Catherine¹ 

[1] Biochemistry Department, Oxford University, South Parks Road, Oxford OX1 3QU, UK;Royal Veterinary College, Royal College Street, London NW1 0TU, UK

关键词: Protein kinase C;    Isoform;    Inhibitor;    Activator;    Schizosaccharomyces pombe;    PKC;    protein kinase C;    TPA;    12-O-tetradecanoylphorbol 13-acetate;   

DOI  :  10.1016/S0014-5793(97)01104-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Expression of certain mammalian protein kinase C (PKC) isoforms inhibits the proliferation of Schizosaccharomyces pombe (Goode et al., Mol. Biol. Cell 5 (1994) 907–920). We have taken advantage of this fact to determine the in vivo isoform preference of a number of PKC inhibitors, using a microtitre plate assay which allows rapid screening. This in vivo model has revealed previously unreported preferences; calphostin C is a more efficient inhibitor of the novel PKCδ than chelerythrine chloride whereas the efficiencies are reversed for inhibition of the classical PKCγ. We have also shown that the anti-leukaemic agent bryostatin 1 inhibits or activates in vivo in an isoform-specific manner.

【 授权许可】

Unknown