Role of copper and ceruloplasmin in oxidative mutagenesis induced by the glutathione-γ-glutamyl transpeptidase system and by other thiols

✍ Scribed by Avishay-Abraham Stark; George Allison Glass

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 196 KB
• Volume: 29
• Category: Article
• ISSN: 0893-6692
• DOI: 10.1002/(sici)1098-2280(1997)29:1<63::aid-em9>3.0.co;2-e

✦ Synopsis

Glutathione is activated to a mutagen by g-glutamyl on the type of thiol. At high Cu or CP concentrations, transpeptidase. Other thiols, such as cysteine, peni-thiol mutagenesis was inhibited. Cu also decreased cillamine, cysteine ethylester, and cysteinylglycine, the mutagenicity of H 2 O 2 . Cu-and CP-enhanced are direct mutagens in the Ames Salmonella muta-mutagenesis were inhibited by radical scavengers, genicity test. Thiol mutagenesis is oxidative in na-catalase, and peroxidase but not by superoxide disture and involves H 2 O 2 and possibly hydroxyl radi-mutase. The effects of Cu and CP on thiol-dependent cals. Transition metals are crucial for thiol autoxida-mutagenesis were similar to their effects on thioltion. The role of copper and ceruloplasmin (CP) in driven lipid peroxidation. The results indicate that thiol-dependent mutagenesis was studied in Salmothe role of Cu and CP in the enhancement of thiol nella typhimurium strain TA102. Cu and CP at low mutagenesis is the facilitation of the transfer of elecconcentrations enhanced thiol-dependent mutagen-trons from a thiol to iron, rather than in catalysis of esis in the presence, but not in the absence, of the Fenton reaction. Environ.