Title : Selective translocation of non-conventional protein kinase C isoenzymes by gonadotropin-releasing hormone (GnRH) in the gonadotrope-derived alpha T3-1 cell line.

Pub. Date : 1996 Apr 19

PMID : 8735596






3 Functional Relationships(s)
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1 In many systems translocation of PKC (from cytosolic to particulate fractions of cellular homogenates) has been taken as evidence of hormonal activation of PKC and down regulation of PKC (by prolonged treatment with PKC-activating phorbol esters) has been used extensively to investigate the role of PKC in hormone action. Phorbol Esters protein kinase C, alpha Mus musculus
2 Here we have assessed the influence of GnRH and phorbol esters on translocation and down regulation of PKC isoenzymes identified by Western blotting with isoenzyme-specific antibodies in alpha T3-1 cells (a gonadotrope-derived cell line). Phorbol Esters protein kinase C, alpha Mus musculus
3 In short-term stimulations (10 min), the PKC-activating phorbol esters, PMA and PDBu, caused concentration-dependent increases in the proportion of PKC alpha and PKC epsilon recovered from the particulate fraction of alpha T3-1 cells, but did not induce measurable translocation of PKC zeta. Phorbol Esters protein kinase C, alpha Mus musculus