Curcumin is a non‐competitive and selective inhibitor of phosphorylase kinase

FEBS Letters

Reddy, Shrikanth¹  Aggarwal, Bharat B.¹ 

[1] Cytokine Research Laboratory, Department of Clinical Immunology and Biological Therapy, The University of Texas M.D. Anderson Cancer Center, Houston, TX 77030, USA

关键词: Curcumin;    Phosphorylase kinase;    pp60c-src;    Inhibitor;    Protein kinase;    Phosphorylation;    PkA;    protein kinase A;    PkC;    protein kinase C;    cPK;    protamine kinase;    PhK;    phosphorylase kinase;    AK;    autophosphorylation-activated protein kinase;    pp60c-src;    cellular tyrosine kinase with a molecular weight of 60 kDa;    TCA;    trichloroacetic acid;   

DOI  :  10.1016/0014-5793(94)80232-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recently, we reported that curcumin (diferuloylmethane) inhibits the growth of several different kinds of tumor cells. In order to investigate the mechanism of this inhibition, we examined the effects of curcumin on different protein kinases: highly purified protein kinase A (PkA), protein kinase C (PkC), protamine kinase (cPK), phosphorylase kinase (PhK), autophosphorylation-activated protein kinase (AK) and pp60^c-src tyrosine kinase. While all kinases tested were inhibited by curcumin, only PhK was completely inhibited at relatively lower concentrations. At around 0.1 mM curcumin, PhK, pp60^c-src, PkC, PkA, AK, and cPK were inhibited by 98%, 40%, 15%, 10%, 1%, and 0.5%, respectively. Lineweaver-Burk plot analysis indicated that curcumin is a non-competitive inhibitor of PhK with a K _i of 0.075 mM. Overall, our results indicate that curcumin is a potent and selective inhibitor of phosphorylase kinase, a key regulatory enzyme involved in the metabolism of glycogen. This has important implications for the anti-proliferative effects of curcumin.

【 授权许可】

Unknown