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Human type II arginase: sequence analysis and tissue-specific expression

S M Morris1, D Bhamidipati, D Kepka-Lenhart

  • 1Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, PA 15261, USA. sid@hoffman.mgen.pitt.edu

Gene
|July 9, 1997
PubMed
Summary
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Human type II arginase shares evolutionary history with amphibians, unlike type I arginase found only in the liver. Differential gene expression suggests complex regulation in humans.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Arginase enzymes are crucial for the urea cycle and nitric oxide synthesis.
  • Two main arginase isoforms, type I and type II, exist with distinct tissue distributions and functions.
  • Understanding the evolutionary origins and expression patterns of arginase isoforms is key to their physiological roles.

Purpose of the Study:

  • To isolate and characterize the human type II arginase cDNA.
  • To compare the sequence of human type II arginase with other known arginases.
  • To investigate the expression patterns of type I and type II arginase mRNA in human and mouse tissues.

Main Methods:

  • Isolation of full-length cDNA encoding human type II arginase from a kidney cDNA library.

Related Experiment Videos

  • Sequence comparison of human type II arginase with vertebrate, bacterial, fungal, and plant arginases.
  • Analysis of arginase mRNA expression in human and mouse RNA samples using hybridization techniques.

    • Main Results:

    • Human type II arginase sequence shows 58% identity to human type I arginase and 71% identity to Xenopus type II arginase.
    • Seven essential active site residues are conserved across all tested arginases.
    • Type II arginase mRNA is widely expressed in human and mouse tissues, while type I arginase mRNA is liver-specific.
    • Multiple type II arginase mRNA species were detected in humans, but only one in mice.

    Conclusions:

    • Gene duplication for arginase likely predates the divergence of mammals and amphibians.
    • The ubiquitous expression of type II arginase suggests broader physiological roles compared to liver-specific type I arginase.
    • Differential mRNA processing or alternative promoter usage may explain the multiple type II arginase mRNA forms in humans.