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Physiol. Genomics 9: 157-166, 2002. First published April 16, 2002; doi:10.1152/physiolgenomics.00017.2002
1094-8341/02 $5.00
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Received 12 February 2002; accepted in final form 15 April 2002.
Physiological Genomics 9:157-166 (2002)
1094-8341/02 $5.00 © 2002 American Physiological Society

Complexity and species variation of the kidney-type glutaminase gene

L. David Porter, Hend Ibrahim, Lynn Taylor and Norman P. Curthoys

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870

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.

pH-response element; metabolic acidosis; mRNA stabilization; LLC-PK1-FBPase+ cells; COOH-terminal domains; RNase H mapping




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