Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins

Shinichiro Yoshitake, Hiroki Nanri, Mihindukulasuriya Rohan Fernando, Shigeki Minakami

Research output: Contribution to journalArticle

83 Scopus citations

Abstract

A possible involvement of thioltransferase (also known as glutaredoxin) in the regenerative reaction of proteins inactivated by oxidative stress were examined in vitro using the enzyme purified from bovine liver. Thioltransferase at physiological concentrations, together with glutathione, glutathione reductase and NADPH, regenerated the oxidatively damaged proteins with a comparable potency to that of thioredoxin. Experiments performed with protein substrates with their critical cysteine residues oxidized differently, that is, phosphofruktokinase and glyceraldehyde 3-phosphate dehydrogenase with mixed disulfide bonds and glyceraldehyde 3-phosphate dehydrogenase with sulfenyl or sulfinyl groups, indicated that thioltransferase regenerated the proteins inactivated by mixed disulfide formation more efficiently than thioredoxin, whereas thioredoxin preferentially regenerated the proteins inactivated by monothiol oxidation to sulfenic or sulfinic acid. These findings suggested that thioltransferase exerted regenerative effects on oxidatively damaged proteins like its cognate protein, thioredoxin, but with different substrate specificity, and their relative contribution to the regeneration reaction is dependent on the form of the oxidized thiols of the damaged proteins.

Original languageEnglish (US)
Pages (from-to)42-46
Number of pages5
JournalJournal of Biochemistry
Volume116
Issue number1
DOIs
StatePublished - Jul 1994

Keywords

  • Oxidative damage
  • Regeneration
  • Thioltransferase (glutaredoxin)
  • Thioredoxin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins'. Together they form a unique fingerprint.

  • Cite this