Proteomics

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Site-specific Identification and Quantification of Protein Glutathionylation under Ischemic Stress


ABSTRACT: Ischemia or ischemic reperfusion is well-known for its contribution to heart diseases. During ischemia and reperfusion, a flux of nutrients and oxygen to cardiomyocytes is altered, which causes a burst of ROS from mitochondria and other enzymes. Elevated levels of ROS can cause oxidative modifications of cardiac proteins, such as protein glutathionylation. Despite previous extensive studies, proteomic identification of glutathionylated proteins in cardiomyocytes under altered levels of nutrients and oxygen has been relatively limited. We have applied our clickable glutathione approach to HL-1 cardiomyocyte cell line under metabolic alterations of glucose, oxygen, and fatty acids to detect and identify proteins undergoing glutathionylation.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Maheeshi Yapa Abeywardana  

LAB HEAD: Young-Hoon Ahn

PROVIDER: PXD024766 | Pride | 2021-08-13

REPOSITORIES: Pride

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Publications

Identification and Quantification of Glutathionylated Cysteines under Ischemic Stress.

Yapa Abeywardana Maheeshi M   Samarasinghe Kusal T G KTG   Munkanatta Godage Dhanushka D   Ahn Young-Hoon YH  

Journal of proteome research 20210812 9


Ischemia reperfusion injury contributes to adverse cardiovascular diseases in part by producing a burst of reactive oxygen species that induce oxidations of many muscular proteins. Glutathionylation is one of the major protein cysteine oxidations that often serve as molecular mechanisms behind the pathophysiology associated with ischemic stress. Despite the biological significance of glutathionylation in ischemia reperfusion, identification of specific glutathionylated cysteines under ischemic s  ...[more]

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