Ciprofibrate, an hypolipidaemic peroxisome proliferator, induced differenti
ation of HL-60 cells. The effect was greatly potentiated by phorbol 12-myri
state W-acetate at a concentration where neither phorbol ester nor ciprofib
rate alone had any effect on these cells. As occurs for HL-60 cell differen
tiation induced by high phorbol ester concentration, the ciprofibrate-induc
ed phorbol eater-dependent differentiation of HL-60 cells proceeded through
the monocytic/macrophage pathway and induced the phosphorylation of protei
ns with similar molecular weights suggesting that increased protein kinase
C activity may be involved in the effect, The peroxisome proliferator-activ
ated receptor (PPAR alpha) transcription factor is expressed in HL-60 cells
, but no changes were observed in its expression upon HL-60 cell differenti
ation.