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Example sentences for: sertoli
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Androgen binding protein (ABP) is produced by Sertoli cells of the testis, secreted into the lumen of seminiferous tubules, and transported with tubular fluid to the epididymis, where it is internalized and degraded by the epithelial cells of the initial segment and the caput; it binds testosterone (T), dihydrotestosterone and estradiol with high affinity [ 9 10 11 ] . The functions of ABP have been the subject of many reviews [e.g.
1. USF1 and USF2, as well as truncated USF isoforms, bind to a consensus E-box in the RIIβ promoter in Sertoli cells.
Among genes that are stimulated by FSH/cAMP during the period of maturation of Sertoli cells (15 to 20 days of age in rats), are several subunits of cAMP-dependent protein kinase (PKA), the serine/threonine kinase mainly responsible for the downstream effects of FSH [ 15 ] . Expression of the RIIβ regulatory subunit of cAMP-dependent protein kinase is highly induced (50-fold) at the mRNA level in primary cultures of rat Sertoli cells as a late response to cAMP peaking at 12 hours [ 16 ] . We have demonstrated that expression of CAAT/Enhancer binding protein β (C/EBPβ) is induced by cAMP with rapid kinetics in Sertoli cells, and that C/EBPβ is responsible for induction of late response genes like the RIIβ-gene [ 17 ] . The RIIβ promoter contains a conserved E-box/HLH element in the basal promoter localized at -280 to -275 relative to the functional ATG [ 18 ] . This element is shown to be important for cAMP-responsiveness in granulosa cells, and it has been shown to bind both USF and Myc in CHO and NB2a cells [ 18 19 ] . In this work, we show that USF isoforms may regulate cAMP responsiveness of the RIIβ promoter by modulating the effect of C/EBP, and that the formation of USF isoforms may be regulated by cAMP in Sertoli cells.
Nuclear extract from Sertoli cells (12 × 10 6) were prepared by solubilization of nuclei in 0.4 M NaCl as described previously [ 17 ] .
C/EBP is previously reported to be an important accessory factor for transactivation by several other transcription factors [ 26 ] . C/EBPβ was shown to transactivate the α1-acid glycoprotein gene promoter even when mutated in the DNA-binding domain, and this activation appeared to depend on protein-protein interaction with glucocorticoid receptor through the leucine zipper region [ 27 ] . Recently, a conserved domain in C/EBPα and C/EBPβ was shown to mediate cAMP responsiveness, strengthening the fact that C/EBP may be characterized as a cAMP-responsive nuclear regulator [ 28 29 ] . On the COX-2 promoter in granulosa cells, cAMP-mediated regulation was shown to be mediated primarily by an E-box that bind USF1 and USF2 isoforms in a manner resembling the RIIβ E-box in Sertoli cells [ 30 ] . Transactivation of the COX-2 gene in skin carcinoma cells is highly dependent on this E-box together with a C/EBP binding site that bind C/EBPβ and C/EBPδ [ 31 ] . These data strengthens a model of formation of a cAMP-responsive unit (CRU) containing USF and C/EBP.
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