Sulfhydration mediates neuroprotective actions of parkin

Increases in S-nitrosylation and inactivation of the neuroprotective ubiquitin E3 ligase, parkin, in the brains of patients with Parkinson’s Disease (PD) are thought to be pathogenic and suggest a possible mechanism linking parkin to sporadic PD. Here we demonstrate that physiologic modification of...

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Main Authors: Vandiver, M. Scott, Paul, Bindu D., Xu, Risheng, Karuppagounder, Senthilkumar, Rao, Feng, Snowman, Adele M., Ko, Han Seok, Lee, Yun Il, Dawson, Valina L., Dawson, Ted M., Sen, Nilkantha, Snyder, Solomon H.
Format: Online
Language:English
Published: 2013
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3622945/
id pubmed-3622945
recordtype oai_dc
spelling pubmed-36229452013-09-27 Sulfhydration mediates neuroprotective actions of parkin Vandiver, M. Scott Paul, Bindu D. Xu, Risheng Karuppagounder, Senthilkumar Rao, Feng Snowman, Adele M. Ko, Han Seok Lee, Yun Il Dawson, Valina L. Dawson, Ted M. Sen, Nilkantha Snyder, Solomon H. Article Increases in S-nitrosylation and inactivation of the neuroprotective ubiquitin E3 ligase, parkin, in the brains of patients with Parkinson’s Disease (PD) are thought to be pathogenic and suggest a possible mechanism linking parkin to sporadic PD. Here we demonstrate that physiologic modification of parkin by hydrogen sulfide (H2S), termed sulfhydration, enhances its catalytic activity. Sulfhydration sites are identified by mass spectrometry analysis and investigated by site directed mutagenesis. Parkin sulfhydration is markedly depleted in the brains of patients with PD, suggesting that this loss may be pathologic. This implies that H2S donors may be therapeutic. 2013 /pmc/articles/PMC3622945/ /pubmed/23535647 http://dx.doi.org/10.1038/ncomms2623 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Vandiver, M. Scott
Paul, Bindu D.
Xu, Risheng
Karuppagounder, Senthilkumar
Rao, Feng
Snowman, Adele M.
Ko, Han Seok
Lee, Yun Il
Dawson, Valina L.
Dawson, Ted M.
Sen, Nilkantha
Snyder, Solomon H.
spellingShingle Vandiver, M. Scott
Paul, Bindu D.
Xu, Risheng
Karuppagounder, Senthilkumar
Rao, Feng
Snowman, Adele M.
Ko, Han Seok
Lee, Yun Il
Dawson, Valina L.
Dawson, Ted M.
Sen, Nilkantha
Snyder, Solomon H.
Sulfhydration mediates neuroprotective actions of parkin
author_facet Vandiver, M. Scott
Paul, Bindu D.
Xu, Risheng
Karuppagounder, Senthilkumar
Rao, Feng
Snowman, Adele M.
Ko, Han Seok
Lee, Yun Il
Dawson, Valina L.
Dawson, Ted M.
Sen, Nilkantha
Snyder, Solomon H.
author_sort Vandiver, M. Scott
title Sulfhydration mediates neuroprotective actions of parkin
title_short Sulfhydration mediates neuroprotective actions of parkin
title_full Sulfhydration mediates neuroprotective actions of parkin
title_fullStr Sulfhydration mediates neuroprotective actions of parkin
title_full_unstemmed Sulfhydration mediates neuroprotective actions of parkin
title_sort sulfhydration mediates neuroprotective actions of parkin
description Increases in S-nitrosylation and inactivation of the neuroprotective ubiquitin E3 ligase, parkin, in the brains of patients with Parkinson’s Disease (PD) are thought to be pathogenic and suggest a possible mechanism linking parkin to sporadic PD. Here we demonstrate that physiologic modification of parkin by hydrogen sulfide (H2S), termed sulfhydration, enhances its catalytic activity. Sulfhydration sites are identified by mass spectrometry analysis and investigated by site directed mutagenesis. Parkin sulfhydration is markedly depleted in the brains of patients with PD, suggesting that this loss may be pathologic. This implies that H2S donors may be therapeutic.
publishDate 2013
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3622945/
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