Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing.

@article{Elgadi1999CloningAA,
  title={Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing.},
  author={K M Elgadi and Robert A. Meguid and Ming Qian and Wiley W. Souba and Steven F Abcouwer},
  journal={Physiological genomics},
  year={1999},
  volume={1 2},
  pages={
          51-62
        }
}
Three human glutaminase (hGA) isoforms were identified, two of which represent isoforms previously unidentified in any species. One isoform contains an open reading frame with high homology with the rat kidney-type glutaminase, suggesting that this isoform represents the human kidney-type glutaminase, hKGA. A second isoform, termed hGAC, contains an open reading frame that matches hKGA except for a unique COOH-terminal amino acid sequence. In addition, a third human glutaminase isoform was… 
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This is the first report demonstrating expression of alternative transcripts of the mammalian Gls2 gene, and transcriptional mechanisms giving rise to GLS2 variants and isolation of novel G LS2 transcripts in human, rat and mouse are presented.
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Genomic organization and transcriptional analysis of the human L-glutaminase gene 1
TLDR
The human liver-type GA (hLGA) gene has been characterized and Progressive deletion analysis of LGA promoter–luciferase constructs indicated that the core promoter is located between nt ®141 and ­410, with several potential regulatory elements : CAAT, GC, TATA-like, Ras-responsive.
The origin and evolution of human glutaminases and their atypical C-terminal ankyrin repeats
TLDR
An evolutionary model wherein the appearance of the most active enzyme isoform, glutaminase C (GAC), was a late retrotransposition event that occurred in fishes from the Chondrichthyes class, and the ankyrin repeats in the glutaminases were acquired early in their evolution.
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