Identification of the first human glutaredoxin pseudogene localized to human chromosome 20q11.2.

Abstract

Thiol-disulfide interchange reactions are one of the most important regulatory systems in cells. Two kinds of molecules are responsible for this process: non-protein low molecular weight thiols and thiol-containing proteins of higher molecular weight (Zlieger, 1985). Among the first type, glutathione arises as the most important reductant in cell, while thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomer-ase (PDI) are the best known examples of regulatory proteins by thiol-disulfide interchange reactions (Holmgren, 1989). Thioredoxins and glutaredoxins share many common features like being small, heat-stable, globular proteins (around 12 kDa), with a similar tridimensional structure (thioredoxin fold) and both using NADPH as source of reducing equivalents (Holmgren, 1989). However, while the electron from NADPH is transferred to the flavoenzyme thioredoxin reductase that in turn reduces thioredoxin (the so-called thioredoxin system), glutaredoxin is reduced by the sequential transfer of red...