Increased expression of rat kidney-type glutaminase (KGA) during metabolic acidosis results from selective mRNA stabilization. This process is mediated by an 8-base AU-sequence that functions as a pH-response element (pHRE). LLC-PK1-FBPase+ cells, a pH-responsive porcine kidney cell line, express four distinct GA mRNAs. RNase H mapping indicated that three of the GA mRNAs are generated by use of alternative polyadenylation sites and are homologs of the rat KGA mRNA, while the fourth contains a different COOH-terminal coding and 3'-untranslated sequence. PCR cloning and sequencing established that the latter GA mRNA is the homolog of the human GAC mRNA. A rat GAC cDNA was also cloned from a rat kidney library. The 3'-untranslated regions of the GAC mRNAs, but not the porcine or human KGA mRNAs, contain identifiable pHREs. The human KGA gene spans 82 kb and is composed of 19 exons. The unique sequence from the hGAC cDNA is contained in a single exon. Thus in humans, alternative splicing of the initial transcript could produce two GA mRNAs, only one of which may be increased during acidosis.
Regulation of 9.5-kb androgen receptor mRNA concentrations in Sertoli and peritubular cells from 20-day-old rats was studied by Northern blot analysis. Treatment of cells in vitro for 1-7 days with 300 ng/ml FSH increased androgen receptor mRNA up to 4-fold in Sertoli cells but not in peritubular cells. Testosterone (100 ng/ml) had no effect or slightly decreased androgen receptor mRNA in Sertoli and peritubular cells. Androgen receptor mRNA concentrations in Sertoli and peritubular cells from rats killed 15 days after hypophysectomy were elevated 4-5-fold over those in cells from intact rats. The androgen receptor mRNA concentration was decreased in both Sertoli and peritubular cells isolated from hypophysectomized animals treated with 500 micrograms/day testosterone propionate in vivo and subsequently with 100 ng/ml testosterone in vitro. FSH treatment (100 micrograms/day in vivo, followed by 300 ng/ml in vitro) did not increase androgen receptor mRNA over that in cells from hypophysectomized controls but rather decreased its concentration to varying degrees in Sertoli and peritubular cells. The rise in androgen receptor mRNA in both Sertoli and peritubular cells isolated from hypophysectomized animals is attributable, at least in part, to the absence of the inhibitory influence of testosterone. Other data in the literature suggest positive regulation of Sertoli cell androgen receptor protein by FSH and androgens. Consequently, complex mechanisms involving transcriptional, translational, and post-translational regulation probably control androgen receptor concentrations in the cells of the rat seminiferous tubule.
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