Substitution of phosphatidylserine by lipid A in the activation of purified rabbit brain protein kinase C.
Three lipid A derivatives (hexaacyl monophosphoryl lipid A, hexaacyl diphosphoryl lipid A, and disaccharide precursor IVA) 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.
Ellis
C A
CA
Aitken
A
A
Takayama
K
K
Qureshi
N
N
D000818:Animals; D001921:Brain / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D008050:Lipid A / Q000031:analogs & derivatives / Q000494:pharmacology*; D015240:Phorbol 12,13-Dibutyrate; D010703:Phorbol Esters / Q000378:metabolism; D010718:Phosphatidylserines / Q000494:pharmacology*; D011493:Protein Kinase C / Q000378:metabolism*; D011817:Rabbits; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D008050:Lipid A; D010703:Phorbol Esters; D010718:Phosphatidylserines; D015240:Phorbol 12,13-Dibutyrate; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate