Mechanisms of liver injury. III. Role of glutathione redox status in liver injury

Derick Han, Naoko Hanawa, Behnam Saberi, Neil Kaplowitz

Research output: Contribution to journalArticlepeer-review

225 Scopus citations


GSH is the most abundant redox molecule in cells and thus the most important determinant of cellular redox status. Thiols in proteins can undergo a wide range of reversible redox modifications (e.g., S-glutathionylation, S-nitrosylation, and disulfide formation) during times of increased exposure to reactive oxygen and nitrogen species, which can affect protein activity. These reversible thiol modifications regulated by GSH may be nanoswitches to turn on and off proteins, similar to phosphorylation, in cells. In the cytoplasm, an altered redox state can activate (e.g., MAPKs and NF-E2-related factor-2) and inhibit (e.g., phosphatases and caspases) proteins, whereas in the nucleus, redox alterations can inhibit DNA binding of transcription factors (e.g., NF-κB and activator protein-1). The consequences include the promotion of expression of antioxidant genes and alterations of hepatocyte survival as well as the balance between necrotic versus apoptotic cell death. Therefore, the understanding of the redox regulation of proteins may have important clinical ramifications in understanding the pathogenesis of liver diseases.

Original languageEnglish (US)
Pages (from-to)G1-G7
JournalAmerican Journal of Physiology - Gastrointestinal and Liver Physiology
Issue number1
StatePublished - 2006
Externally publishedYes


  • Disulfide
  • S-glutathionylation
  • Thiol

ASJC Scopus subject areas

  • Physiology
  • Hepatology
  • Gastroenterology
  • Physiology (medical)


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