Activation of protein kinase C increases proteoglycan synthesis in immature rat Sertoli cells.

G Fagnen, N T Phamantu, J Bocquet, P J Bonnamy

Index: Biochim. Biophys. Acta 1472(1-2) , 250-61, (1999)

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Abstract

In order to determine the signal transduction pathways involved in the regulation of proteoglycan (PG) synthesis in immature rat Sertoli cells (SC), we have examined the effect of the tumor promoter phorbol ester PMA (phorbol myristate acetate) on [35S]sulfate and [3H]glucosamine incorporation into PG molecules neosynthesized by cultured rat SC. PMA induced a dose- and time-dependent stimulation of labeled cell-associated PG as determined by quantitative solid phase assay. The overall effect of PMA resulted from enhancement of both glycosylation and catabolism of cell PG, this latter effect leading to a drastic decrease of their residence time in the membrane. Besides these quantitative effects, activation of protein kinase C by PMA induced qualitative changes as reflected by increase in relative proportion of heparan sulfate PG (HSPG) in cell membrane PG. In light of our previous results suggesting an inverse relationship between PG synthesis and FSH responsiveness in immature rat Sertoli cells, the PMA-induced upregulation of cell membrane PG, and particularly HSPG, could constitute one mechanism involved in the repression of FSH-stimulated steroidogenesis induced by PKC activation.