Summary
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, 4β-phorbol 12β-myristate, 13α-acetate and 1,2-dioctanoyl-glycerol inhibited glycosaminoglycan sulfation. By contrast, 4α-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.
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Levy, P., Cherqui, G., Robert, A. et al. Changes in glycosaminoglycan sulfation and protein kinase C subcellular distribution during differentiation of the human colon tumor cell line Caco-2. Experientia 45, 588–591 (1989). https://doi.org/10.1007/BF01990515
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DOI: https://doi.org/10.1007/BF01990515