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• W2121855462 endingPage "997" @default.
• W2121855462 startingPage "993" @default.
• W2121855462 abstract "Endogenous protein phosphorylation was investigated in cultured rat Sertoli cells after treatment with follicle-stimulating hormone (FSH) and pharmacological agents that activate cAMP-dependent protein kinases. In intact Sertoli cells, both phosphorylation and dephosphorylation of proteins occurred in response to treatment with these agents. Studies using cell-free preparations suggest that four phosphoproteins phosphorylated by cAMP or the catalytic subunit of cAMP-dependent protein kinase were also phosphorylated in a FSH-dependent manner in intact cells. These data suggest that FSH-dependent phosphorylation in Sertoli cells occurs through activation of a cAMP-dependent protein kinase. A FSH-dependent phosphoprotein with a molecular weight of 58,000 was identified as the intermediate filament protein vimentin, based on its migration in two-dimensional gels and its peptide map. The cellular distribution of vimentin was monitored by immunofluorescence in Sertoli cells after treatment with FSH. Results of this study support a role for intermediate filaments in FSH-dependent events in Sertoli cells." @default.
• W2121855462 created "2016-06-24" @default.
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• W2121855462 date "1983-02-01" @default.
• W2121855462 modified "2023-09-23" @default.
• W2121855462 title "Follicle-stimulating hormone-dependent phosphorylation of vimentin in cultures of rat Sertoli cells." @default.
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• W2121855462 doi "https://doi.org/10.1073/pnas.80.4.993" @default.
• W2121855462 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/393514" @default.
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• W2121855462 hasPublicationYear "1983" @default.
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