Journal
PROTEOMICS
Volume 3, Issue 1, Pages 73-77Publisher
WILEY
DOI: 10.1002/pmic.200390011
Keywords
heat shock protein; mass spectroscopy; protein oxidation; two-dimensional gel electrophoresis; vimentin
Funding
- NATIONAL CANCER INSTITUTE [P30CA054174] Funding Source: NIH RePORTER
- NCI NIH HHS [CA54174] Funding Source: Medline
Ask authors/readers for more resources
Oxidative damage to neuronal proteins appears to be central to the toxicity associated with a number of neuropathologies, including Alzheimer's disease. We have examined this by using oxidative stress to induce apoptosis in a mouse hippocampal neuronal cell line (HT-22). Oxidatively modified proteins were measured by high-resolution two-dimensional gel electrophoresis coupled with oxidation-specific immunostains. Under these conditions the oxidatively stressed cells undergo apoptosis, and specific proteins are oxidized. The three proteins that appeared to be most susceptible to oxidation were identified by mass spectrometry. Those oxidized proteins are heat shook protein 60 and vimentin, both believed to function as antiapoptotic proteins, and a third protein with sequence homology to hemoglobin a-chain. When the cells were pretreated with vitamin E, these proteins were not oxidized and the cells did not undergo apoptosis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available