Nitrosative stress in the ER: a new role for S-nitrosylation in neurodegenerative diseases.

Published

Journal Article (Review)

S-Nitrosylation, the covalent addition of a nitrogen monoxide group to a cysteine thiol, has been shown to modify the function of a broad spectrum of mammalian, plant, and microbial proteins and thereby to convey the ubiquitous influence of nitric oxide on cellular signal transduction and host defense. Accumulating evidence indicates that dysregulated, diminished, or excessive S-nitrosylation may be implicated in a wide range of pathophysiological conditions. A recent study establishes a functional relationship between inhibitory S-nitrosylation of the redox enzyme protein disulfide isomerase (PDI), defects in regulation of protein folding within the endoplasmic reticulum (ER), and neurodegeneration. Further, an examination of human brains afflicted with Parkinson's or Alzheimer's disease supports a causal role for the S-nitrosylation of PDI and consequent ER stress in these prevalent neurodegenerative disorders.

Full Text

Duke Authors

Cited Authors

  • Benhar, M; Forrester, MT; Stamler, JS

Published Date

  • July 21, 2006

Published In

Volume / Issue

  • 1 / 6

Start / End Page

  • 355 - 358

PubMed ID

  • 17163772

Pubmed Central ID

  • 17163772

Electronic International Standard Serial Number (EISSN)

  • 1554-8937

Digital Object Identifier (DOI)

  • 10.1021/cb600244c

Language

  • eng

Conference Location

  • United States