cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase

Richard M. Wright, Gisela M. Vaitaitis, Cory M. Wilson, Thomas B. Repine, Lance S. Terada, John E. Repine

Research output: Contribution to journalArticle

79 Scopus citations

Abstract

We isolated cDNAs encoding xanthine dehydrogenase (XD; xanthine:NAD+ oxidoreductase, EC 1.1.1.204) from a human liver cDNA library. The complete nucleotide sequence of human XD was determined; the deduced amino acid sequence encoded a protein of 1336 amino acid residues of Mr 147,782. Human XD possessed many of the signature sequences typical of XDs from flies and rodents, including an unusual cysteine distribution, a potential 2Fe/2S binding site, and a putative molybdopterin cofactor binding domain. Analysis of potential NAD binding sites suggested a simple hypothesis for the conversion of human XD into the oxygen metabolite forming xanthine oxidase (XO; xanthine:oxygen oxidoreductase, EC 1.1.3.22). Using a human XD complementary RNA hybridization probe, we found a 5100-base RNA in human liver by RNA blot-hybridization analysis. This RNA exhibited tissue-specific distribution that may be pertinent to XD- and XO-mediated oxygen radical injury in ischemia/reperfusion and inflammation. A second 4500-base RNA was detected in some tissues and may arise through differential transcription termination.

Original languageEnglish (US)
Pages (from-to)10690-10694
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number22
DOIs
StatePublished - Nov 15 1993

Keywords

  • Ischemia
  • Oxidative injury
  • Oxygen radicals
  • Reperfusion

ASJC Scopus subject areas

  • General

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