A. Yamashita et al., INDUCTION OF COENZYME-A-DEPENDENT TRANSACYLATION ACTIVITY IN RAT-LIVER MICROSOMES BY ADMINISTRATION OF CLOFIBRATE, Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1211(3), 1994, pp. 263-269
The effect of administration of clofibrate on the activity of coenzyme
A-dependent (CoA-dependent) transacylation of 1-acyl-glycerophosphoch
oline (1-acyl-GPC) was examined in rat liver microsomes. Administratio
n of clofibrate to rats increased the activity of CoA-dependent transa
cylation of 1-[C-14]acyl-GPC and the activity reached a value (8.37 nm
ol/min per mg protein) twice that in control rats (3.95 nmol/min per m
g protein) without any changes in apparent K(m) values for CoA (1.2 mu
M in control and 1.0 muM in clofibrate-treated) and 1-acyl-GPC (33.4 m
uM in control and 27.8 muM in clofibrate-treated). The rate of CoA-dep
endent transfer of [C-14]arachidonic acid (20:4) from 1-acyl-2-[C-14]2
0:4-glycerophosphoethanolamine (GPE) or 1-acyl-2-[C-14]20:4-glyceropho
sphoinositol (GPI) to 1-acyl-GPC (synthesis of 1-acyl-2-[C-14]20:4-GPC
) was also increased by treatment with clofibrate (1.9-fold and 1.5-fo
ld increases, respectively). These results suggest that a CoA-dependen
t transacylation system of 1-acyl-GPC was induced by treatment with cl
ofibrate.