Potentiation of diacylglycerol‐induced activation of protein kinase C by lysophospholipids

FEBS Letters

Sasaki, Yukio²  Asaoka, Yoshinori¹  Nishizuka, Yasutomi¹ 

[1] Biosignal Research Center, Kobe University, Kobe 657 Japan;Graduate School of Science and Technology, Kobe University, Kobe 657 Japan

关键词: Protein kinase C;    Lysophosphatidylcholine;    Phospholipase A2;    lysoPtdCho;    2-lysophosphatidylcholine;    PtdCho;    phosphatidylcholine;    DAG;    diacylglycerol;    PKC;    protein kinase C;    cPKC;    classical or conventional PKC;    nPKC;    new PKC;    aPKC;    atypical PKC;    MARCKS;    myristoylated alanine-rich C kinase substrate;    MBP;    myelin basic protein;    PtdSer;    phosphatidylserine;   

DOI  :  10.1016/0014-5793(93)81655-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Lysophospholipid, particularly 2-lysophosphatidylcholine (lysoPtdCho), significantly potentiates the diacylglycerol (DAG)-induced activation of protein kinase C (PKC) in vitro. LysoPtdCho shows no effect, unless DAG and phosphatidylserine (PtdSer) are present. This lysoPtdCho action also depends on its own as well as on Ca²⁺ concentration. At physiological Ca²⁺ concentrations, the activation of the α-, β-, and γ-subspecies (cPKC) is enhanced by lysoPtdCho in the 10⁻⁶ M range, but inversely inhibited in the 10⁻⁵ M range. The δ- and ε-subspecies (nPKC), which are enzymatically insensitive to Ca²⁺, are mostly inhibited by lysoPtdCho at its low concentrations. The enhancement of cPKC activation by lysoPtdCho is due to the increase in an apparent affinity of the enzyme for PtdSer but not for DAG. The results may account, at least in part, for the previous observations made with intact cell systems that lysoPtdCho significantly potentiates the DAG-induced cellular responses such as T-lymphocyte activation and HL-60 cell differentiation [(1992) Trends Biochem. Sci. 17, 414–4171].

【 授权许可】

Unknown