Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) participates in a cell death cascade wherein a variety of stimuli activate nitric oxide (NO) synthases with NO nitrosylating GAPDH, conferring on it the ability to bind to Siah, an E3-ubiquitin-ligase, whose nuclear localization signal enables the GAPDH/Siah protein complex to translocate to the nucleus where degradation of Siah targets elicits cell death. R-(-)-Deprenyl (deprenyl) ameliorates the progression of disability in early Parkinson's disease and also has neuroprotective actions. We show that deprenyl and a related agent, TCH346, in subnanomolar concentrations, prevent S-nitrosylation of GAPDH, the binding of GAPDH to Siah, and nuclear translocation of GAPDH. In mice treated with the dopamine neuronal toxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), low doses of deprenyl prevent binding of GAPDH and Siah1 in the dopamine-enriched corpus striatum.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1450161PMC
http://dx.doi.org/10.1073/pnas.0511321103DOI Listing

Publication Analysis

Top Keywords

death cascade
8
cell death
8
binding gapdh
8
gapdh
7
neuroprotection pharmacologic
4
pharmacologic blockade
4
blockade gapdh
4
gapdh death
4
cascade glyceraldehyde-3-phosphate
4
glyceraldehyde-3-phosphate dehydrogenase
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!