Protein S-nitrosylation and cancer

Cancer Lett. 2012 Jul 28;320(2):123-9. doi: 10.1016/j.canlet.2012.03.009. Epub 2012 Mar 13.

Abstract

Protein S-nitrosylation is a covalent post-translational modification through coupling of a nitric oxide (NO) moiety with the reactive thiol group of a protein cysteine residue to form an S-nitrosothiol (SNO). S-nitrosylation is a key mechanism in the transmission of NO-based cellular signals in the vital cellular processes, including transcription regulation, DNA repair, and apoptosis. Contemporary research has implicated dysregulation of S-nitrosylation in severe pathological events, including cancer onset, progression, and treatment resistance. The S-nitrosylation status may be directly linked to many cancer therapy outcomes as well as therapeutic-resistance, emphasizing the need to develop S-nitrosylation-related anti-cancer therapeutics. The role of S-nitrosylated proteins in the development and progression of cancer are varied, generating a critical need for a thorough review of the current dynamic research in this area.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Disease Progression
  • Dual Specificity Phosphatase 1 / chemistry
  • Humans
  • Neoplasms / genetics*
  • Neoplasms / metabolism
  • Nitric Oxide / metabolism*
  • Protein Processing, Post-Translational*
  • S-Nitrosothiols / metabolism

Substances

  • S-Nitrosothiols
  • Nitric Oxide
  • DUSP1 protein, human
  • Dual Specificity Phosphatase 1