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PubMed · 16987024

Thioredoxin-1 and posttranslational modifications.

Judith Haendeler
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Abstract

Thioredoxin-1 is a 12 kDa protein that consists of a redox regulatory domain containing the active cysteine residues 32 and 35. These cysteines are conserved from bacteria to human. Unlike thioredoxins from lower species, mammalian thioredoxin-1 contains three additional nonactive cysteine residues at positions 62, 69, and 73 (for human thioredoxin-1). Key biological functions of thioredoxin-1 are antioxidative, anti-apoptotic, and pro-proliferative properties. Thioredoxin-1 is regulated by the ability of the thioredoxin reductase to reduce oxidized thioredoxin-1 at cysteines 32 and 35. However, posttranslational modifications of thioredoxin-1, including glutathionylation, thiol-oxidation, and S-nitros(yl)ation, at the nonactive cysteines importantly contribute to the regulation and functions of thioredoxin-1. This review focuses on the posttranslational modifications of the active and nonactive cysteines and their contribution for functional regulation of thioredoxin-1.

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AnimalsCysteineGlutathioneHumansNitric OxideOxidation-ReductionProtein Processing, Post-TranslationalS-NitrosothiolsThioredoxinsJournal ArticleResearch Support, Non-U.S. Gov'tReview

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Judith Haendeler. Thioredoxin-1 and posttranslational modifications.. https://doi.org/10.1089/ars.2006.8.1723

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