Changes in glycosaminoglycan sulfation and protein kinase C subcellular distribution during differentiation of the human colon tumor cell line Caco-2 |
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Authors: | P. Levy G. Cherqui A. Robert D. Wicek J. Picard |
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Affiliation: | (1) Laboratoire de Biochimie, INSERM, Faculté de Médecine Saint-Antoine, 27 rue Chaligny, F-75 571 Paris Cédex 12, France |
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Abstract: | 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, 4-phorbol 12-myristate, 13-acetate and 1,2-dioctanoyl-glycerol inhibited glycosaminoglycan sulfation. By contrast, 4-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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Keywords: | Differentiation glycosaminoglycan sulfation protein kinase C phorbol esters Caco-2 cells |
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