Background: Dysfunction of the cellular antioxidant system and accumulation of reactive oxygen species are involved in the pathophysiology of diseases such as cardiovascular disease, neurodegenerative disorders, tumors, male infertility and aging. Two gluthathione peroxidases play key roles in the cellular protection against oxidative damage. Glutathione peroxidase (GPx-1) removes cytosolic hydroperoxides while phospholipid-hydroperoxide glutathione peroxidase (GPx-4) is a unique enzyme that reduces phospholipid peroxides in membranes.
Methods: We cloned and sequenced the full-length cDNA for GPx-1 (GenBank: AY966403) and GPx-4 (GenBank: AY966404) from the common marmoset (Callithrix jacchus) in order to create a suitable model for studying human diseases related with oxidative stress.
Results: The cDNAs encode a 202 amino acid protein for GPx-1 and a 197 amino acid protein for GPx-4. Both proteins include selenocysteine (Sec, in Gpx-1 at position 48; in GPx-4 at position 73) and showed high homology (>90%) with other mammalian GPxs. The relative levels of mRNA expression for GPx-1 and GPx-4 were determined in different marmoset tissues by quantitative real-time reverse transcriptase-polymerase chain reaction using transcription elongation factor-2 as a reference gene. GPx-1 showed increased levels of expression in the liver, heart and kidney while the highest mRNA levels for GPx-4 were detected in the testis, followed by the liver, lung, kidney and spinal cord.
Conclusions: These findings will be of value for studies designed to assess the role of glutathione peroxidases in non-human primate models for a variety of diseases in which increased oxidative stress has been implicated.