title: Marmoset glutathione peroxidases: cDNA sequences, molecular evolution, and gene expression.
abstract: 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.
authors.affiliation: Department of Clinical Chemistry, Georg-August University, Goettingen, Germany.
authors.forename: Srebrena
authors.initials: S
authors.lastname: Atanasova
authors.forename: Nicolas
authors.initials: N
authors.lastname: von Ahsen
authors.forename: Christina
authors.initials: C
authors.lastname: Schlumbohm
authors.forename: Eberhard
authors.initials: E
authors.lastname: Wieland
authors.forename: Michael
authors.initials: M
authors.lastname: Oellerich
authors.forename: Victor
authors.initials: V
authors.lastname: Armstrong
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002144:Callithrix / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D019143:Evolution, Molecular; D015870:Gene Expression; D005979:Glutathione Peroxidase / Q000235:genetics*; D008297:Male; D008969:Molecular Sequence Data; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D010802:Phylogeny; D019105:Random Amplified Polymorphic DNA Technique / Q000662:veterinary; D016415:Sequence Alignment; D000094765:Glutathione Peroxidase GPX1
chemical_list: D018076:DNA, Complementary; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D005979:Glutathione Peroxidase; D000094765:Glutathione Peroxidase GPX1