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. 1983 Feb;80(4):993–997. doi: 10.1073/pnas.80.4.993

Follicle-stimulating hormone-dependent phosphorylation of vimentin in cultures of rat Sertoli cells.

W A Spruill, A L Steiner, L L Tres, A L Kierszenbaum
PMCID: PMC393514  PMID: 6302679

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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