Changes in glycosaminoglycan sulfation and protein kinase C subcellular distribution during differentiation of the human colon tumor cell line Caco-2.

During the spontaneous differentiation (day 5 to day 15 of the culture) of Caco-2 cells, the sulfation of cell layer glycosaminoglycans increased, whereas protein kinase C activity was concomitantly redistributed from the membrane to the cytosol. The protein kinase C activators, 4 beta-phorbol 12 beta-myristate, 13 alpha-acetate and 1,2-dioctanoylglycerol inhibited glycosaminoglycan sulfation. By contrast, 4 alpha-phorbol 12, 13 didecanoate was ineffective. These results suggest that membrane-bound PKC may exert a modulatory effect on glycosaminoglycan sulfation, and this effect is gradually attenuated as Caco-2 cell differentiation progresses.