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Protein kinases and protein synthesis are involved in desensitization of the plasminogen activator response of rat Sertoli cells by follicle‐stimulating hormone
Author(s) -
Laurent-Cadoret V.,
Guillou F.,
Combarnous Y.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00906-6
Subject(s) - protein kinase c , sertoli cell , medicine , endocrinology , desensitization (medicine) , activator (genetics) , follicle stimulating hormone , plasminogen activator , follicle stimulating hormone receptor , secretion , homologous desensitization , protein kinase a , hormone , chemistry , receptor , biology , kinase , microbiology and biotechnology , luteinizing hormone , spermatogenesis
Tissue‐type plasminogen activator (tPA) secretion is a specific response of Sertoli cells to follicle‐stimulating hormone (FSH), which is lower after preincubation of the cells with low FSH concentrations because of FSH receptor/G s protein uncoupling. In this report, we present evidence that this desensitization induced by the lowest FSH concentrations is suppressed by specific peptidic inhibitors of endogenous PKA and PKC in permeabilized Sertoli cells. In contrast, desensitization promoted by slightly higher FSH concentrations is not mediated through PKA or PKC activation but is dependent on protein neosynthesis.