Substitution of phosphatidylserine by lipid A in the activation of purified rabbit brain protein kinase C

FEBS Letters

Ellis, Christine A.³  Takayama, Kuni²  Aitken, Alastair¹  Qureshi, Nilofer² 

[1] Mycobacteriology Research Laboratory, William S. Middleton Memorial Veterans Hospital, Madison, WI 53705 and Department of Bacteriology, College of Agricultural and Life Sciences, University of Wisconsin, Madison, WI 53706, USA;Department of Pharmaceutical Chemistry, School of Pharmacy, University of London, 29/39 Brunswick Square, London WC1N 1AX, England

关键词: Lipopolysaccharide;    Lipid A;    Protein kinase C;    Phorbol ester;    Phosphatidylserine;    LPS;    lipopolysaccharide;    MPLA;    monophosphoryl lipid A;    DPLA;    disphoryl lipid A;    IV A;    disaccharide precursor lipid A (tetraacyl);    PS;    phosphatidylserine;    TPA;    12-O-tetradecanoyl phorbol 13-acetate;    PDBu;    phorbol 12;    13-dibutyrate;   

DOI  :  10.1016/0014-5793(87)81053-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three lipid A derivatives (hexaacyl monophosphoryl lipid A, hexaacyl diphosphoryl lipid A, and disaccharide precursor IV A) were shown to activate protein kinase C from rabbit brain. These derivatives substituted for phosphatidylserine in a concentration-dependent manner and did not compete for binding of [³H]phorbol dibutyrate to its receptor site. Instead, phorbol dibutyrate binding was increased on raising the concentration of the derivatives in a similar manner to phosphatidylserine. The phorbol ester 12-0-tetra-decanol 13-acetate augmented the activation of protein kinase C by the lipid A derivatives.

【 授权许可】

Unknown