Open AccessThe biological significance of oxidative modifications of cysteine residues in proteins illustrated with the example of glyceraldehyde-3-phosphate dehydrogenase
Author(s) -
Aleksandra Rodacka,
Joanna Gerszon,
Mieczysław Puchała
Publication year - 2014
Publication title -
postępy higieny i medycyny doświadczalnej
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.275
H-Index - 34
eISSN - 1732-2693
pISSN - 0032-5449
DOI - 10.5604/17322693.1093929
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , s nitrosylation , cysteine , dehydrogenase , biochemistry , oxidative phosphorylation , nitrosylation , enzyme , chemistry , cysteine metabolism , glycolysis , organic chemistry , nitric oxide
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.