A. Dibas et al., IS PROTEIN-KINASE-C-ALPHA (PKC-ALPHA) INVOLVED IN VASOPRESSIN-INDUCEDEFFECTS ON LLC-PK1 PIG-KIDNEY CELLS, Biochemistry and molecular biology international, 39(3), 1996, pp. 581-588
The involvement of protein kinase C (PKC) in vasopressin-induced effec
ts on renal water reabsorption is still unresolved, Activation of PKC
can be detected by its translocation from the cytosol (C) to the plasm
a membrane(PM). In LLC-PK1 cells, the redistribution of PKC alpha, a p
redominant isoform of PKC detected, was studied utilizing western blot
ting after stimulation with vasopressin. Vasopressin (100 mU/ml) faile
d to induce a translocation of PKC alpha from the C to the PM. By cont
rast, phorbol myristate acetate (BMA, 200 nM), a potent activator of P
KC, induced a relocalization of PKC alpha from the C to the PM. After
2 hours of treatment of cells with PMA, PKC alpha was predominantly de
tected in the PM and absent from the C. These results suggest that the
signal transduction pathway of vasopressin in LLC-PK1 cells does not
involve PKC alpha activation and translocation.