The biological significance of oxidative modifications of cysteine residues in proteins illustrated with the example of glyceraldehyde-3-phosphate dehydrogenase
Journal Title: Advances in Hygiene and Experimental Medicine - Year 2014, Vol 68, Issue
Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key redox-sensitive protein, the activity of which is largely affected by oxidative modifications at its highly reactive cysteine residue in the active site of the enzyme (Cys-152). These modifications occur as a result of S-thiolation, S-nitrosylation or disulfide bonds that lead to aggregate formation. The oxidative changes not only affect the glycolytic function but also stimulate the participation of GAPDH in numerous cellular processes. In this review we describe how thiol modification of Cys-152 in GAPDH re-routes metabolic pathways in the cell and converts a metabolic enzyme into a pro-apoptotic factor. Especially interesting issue is the participation of GAPDH in the regulation of expression of endothelin 1 and nitrosylation of nuclear proteins. In the last section we describe involvement of GAPDH in the processes associated with neurodegenerative diseases.
Authors and Affiliations
Aleksandra Rodacka, Joanna Gerszon, Mieczysław Puchała
Keywords
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