Database: OMIM
Entry: 138320
LinkDB: 138320
MIM Entry: 138320
  Paglia and Valentine (1967) characterized red cell glutathione
  peroxidase (EC Necheles et al. (1968) observed hemolytic
  disease of the newborn with hyperbilirubinemia and Heinz bodies,
  associated with partial deficiency of red cell glutathione peroxidase.
  The clinical manifestations were self-limited; evidence of hemolysis had
  disappeared by 3 months of age, although the enzyme deficiency
  persisted. Sibs were affected in some instances and 1 parent had
  comparably depressed enzyme level and a history of neonatal jaundice.
  Necheles et al. (1969) found low levels of glutathione peroxidase in an
  18-year-old Puerto Rican male with compensated hemolytic anemia. Both
  parents and 1 sib had intermediate enzyme levels. By electrophoretic
  means, Beutler and West (1974) demonstrated polymorphism of red cell
  glutathione peroxidase in Afro-Americans. Since no male-to-male
  transmission was noted, X-linkage could not be excluded but is unlikely.
  An electrophoretic polymorphism of glutathione peroxidase was described
  by Beutler et al. (1974).
  Beutler and Matsumoto (1975) found that persons of Jewish ancestry and
  others of Mediterranean origin have a decrease in red cell GPX activity,
  but not of leukocyte or fibroblast activity. Oriental populations showed
  a significantly lower scatter in red cell enzyme levels in comparison
  with Occidental populations. The authors suggested the existence of a
  low GPX allele with a frequency of about 0.556 in the Jewish population
  and 0.181 in the U.S.-Northern European population. They recommended
  caution in assigning a cause-effect relationship to GPX deficiency and
  hemolytic anemia.
  Meera Khan et al. (1986) studied the genetics of red cell GPX1 in the
  Djuka of Suriname. This group consists of descendants of captives from
  the Gold Coast (Ghana) of Africa brought to Suriname during the 17th
  century and of others probably from a wider region of West Africa
  transported during the 18th century. During successive waves of revolt
  and following the abolition of slavery, the Djuka escaped into the
  interior of Suriname and organized themselves into groups which have
  lived since then as permanent forest dwellers with little or no
  extra-ethnic mixture. Meera Khan et al. (1986) found that the Djuka have
  a frequency of the GPX1*2 allele of 0.054 and suggested that the GPX1*2
  allele is an African marker. The only non-Africans in whom it is
  presently found are Ashkenazi Jews living in the United States and the
  Punjabis of the Indian subcontinent. It was proposed that both groups
  independently acquired the variant allele through an ancient African
  mixture. See Meera Khan et al. (1984).
  The catalytic activity of GPX1 enzyme in the 2-1 heterozygote is greater
  than that in the 1-1 homozygote. It may be that individuals with the
  higher peroxidase activity have an intraerythrocytic environment which
  is less favorable for the survival of the falciparum parasite and
  therefore that the 2-1 heterozygote enjoys a selective advantage in a
  malarious environment. Meera Khan et al. (1986) referred to the
  electrophoretic variants as electrotypes. Paglia (1989) wrote: 'To date,
  no defects in glutathione peroxidase have been unequivocally
  incriminated in the pathogenesis of hemolytic syndromes, although
  several instances of partial deficiency have been reported in patients
  with anemias of unknown etiology. This association may be coincidental,
  since there is a broad range of ethnic variation in the erythrocyte
  enzyme' (Beutler and Matsumoto, 1975).
  Perona et al. (1979) presented evidence that neonatal deficiency of the
  selenoenzyme glutathione peroxidase, with hematologic consequences, may
  result from 'selenium imbalance' during pregnancy. Glutathione
  peroxidase is involved in the detoxification of hydrogen peroxide.
  Selenium in the form of selenocysteine is part of its catalytic site. In
  experimental selenium deficiency in animals and in selenium deficiency
  that has developed in patients on long-term total parenteral
  alimentation, GSHPx activity in red blood cells, granulocytes, and
  platelets is low. Replacement with intravenous selenous acid results in
  slow recovery of GSHPx activity in red cells over a 3-month period;
  recovery occurs only in cells made in the presence of selenium (Cohen et
  al., 1985).
  Using a radioimmunoassay for GSHPx, Takahashi et al. (1986) showed that
  there is a direct relationship between enzyme activity and enzyme
  protein concentration. Thus, selenium is necessary for the synthesis of
  protein. Selenium deficiency results in a decrease not only in
  glutathione peroxidase activity but also in GSHPx protein. Only
  erythrocytes formed in the presence of selenium contain GSHPx activity.
  The possibility of confusing genetic and environmental factors is
  indicated. Takahashi et al. (1987) observed a selenium-dependent GPX in
  human plasma that is distinct from the one found in erythrocytes.
  Selenium deficiency in children with inborn errors of metabolism under
  treatment with chemically defined formulas has been reported. Yannicelli
  et al. (1992) described a child with biotin-nonresponsive propionic
  acidemia (606054) who developed erythrocyte macrocytosis and unusual
  texture of the hair with hypopigmentation. Selenium supplementation
  resulted in dramatic improvement. Vinton et al. (1987) had reported a
  child receiving long-term total parenteral nutrition who developed
  erythrocyte macrocytosis and hair and skin depigmentation (referred to
  by them as pseudoalbinism) as manifestations of selenium deficiency.
  Sukenaga et al. (1987) presented the sequence of GPX cDNA. GPX is one of
  only a few proteins known in higher vertebrates to contain
  selenocysteine. This unusual amino acid occurs at the active site of GPX
  and is coded by the nonsense (stop) codon TGA. Sequence analysis of cDNA
  clones confirmed previous findings that the unusual amino acid
  selenocysteine is encoded by the opal terminator codon UGA (Le Beau,
  1989). (Note that TGA = UGA; they represent the cDNA and mRNA code,
  respectively.) There appears to be a selenocysteyl-tRNA which donates
  selenocysteine to the growing polypeptide chain of GPX, and therefore,
  selenocysteine becomes the twenty-first naturally occurring amino acid.
  A tRNA molecule that carries selenocysteine has its own translating
  factor that delivers it to the translating ribosome (Bock et al., 1991).
  Bacterial formate dehydrogenase also contains selenocysteine.
  Glutathione peroxidase activity of red cells was found to be elevated in
  patients with trisomy 21 (Sinet et al., 1975). Although confirmation of
  the localization of the antiviral protein locus (107450) and the soluble
  superoxide dismutase locus (147450) to chromosome 21 has been provided
  by dosage effects, misleading results have been provided by this
  approach in the case of other loci. Studying nucleated cells
  (lymphocytes and polymorphs) from patients with trisomy 21 and monosomy
  21, Feaster et al. (1977) could not confirm the suggested assignment of
  this locus to that chromosome. Wijnen et al. (1978) presented evidence
  that GPX1 is on chromosome 3. Johannsmann et al. (1979) concluded that
  the GPX locus is on 3p. In situ hybridization localized the gene to
  3p13-q12. McBride et al. (1988) used a cDNA probe to study DNAs isolated
  from human-rodent somatic cell hybrids. A 609-bp probe containing the
  entire coding region hybridized to human chromosomes 3, 21, and Xp. An
  intronic probe detected only the gene on chromosome 3. The sequences on
  chromosomes X and 21 showed equal conservation of the 3-prime
  untranslated and coding sequences but did not contain introns,
  suggesting that they represent processed pseudogenes. By in situ
  hybridization of a glutathione peroxidase cDNA clone, Le Beau et al.
  (1989) sublocalized the gene to 3q11-q13 (see Chada et al., 1990).
  Combining this with previous data, the localization becomes 3q11-q12.
  Mehdizadeh et al. (1996) mapped the Gpx1 gene to mouse chromosome 9 in a
  region of known conserved homology between mouse chromosome 9 and human
  chromosome 3.
  Kiss et al. (1997) concluded that the GPX1 gene is, in fact, located on
  3p21.3; they used fluorescence in situ hybridization and PCR analysis.
  They suggested that the probes previously used were not strictly
  specific for GPX1 and could amplify other sequences on chromosome 3. The
  results were compatible with the existence of a pseudogene of GPX1 on
  Shen et al. (1994) reported variation in vivo and instability in vitro
  of an in-frame GCG trinucleotide repeat in the GPX1 gene. In a
  population study of 110 alleles from 55 unrelated persons, the allele
  frequencies for 4, 5, and 6 GCG repeats were 0.40, 0.35, and 0.25,
  respectively. No allele was associated with diminished enzyme activity.
  Current stocks of HL-60 cells, a human myeloid leukemia cell line, were
  found to be homozygous for the 6-repeat allele. The expansion of the
  repeat appears to have developed in the course of multiple passages of
  the rapidly proliferating cell line because cells frozen in 1976 showed
  a 4/6 genotype and 'intermediate' passage cells frozen in 1985 contained
  both 4/6 and 5/6 genotypes.
  Data on gene frequencies of allelic variants were tabulated by
  Roychoudhury and Nei (1988).
  Cellular antioxidant enzymes such as glutathione peroxidase-1 and
  superoxide dismutase have a central role in control of reactive oxygen
  species. In a study of 636 patients with suspected coronary artery
  disease, Blankenberg et al. (2003) found that erythrocyte GPX1 activity
  was among the strongest univariate predictors of the risk of
  cardiovascular events. An inverse relationship was found between the
  level of GPX1 activity and the risk of cardiovascular events. GPX1
  activity was affected by sex (lower in males) and smoking status.
  Blankenberg et al. (2003) found no association between risk of
  cardiovascular events and superoxide dismutase activity.
  De Haan et al. (1998) demonstrated a role for GPX1 in protection against
  oxidative stress by showing that Gpx1 -/- mice are highly sensitive to
  the oxidant paraquat. Lethality was detected within 24 hours in mice
  exposed to paraquat at 10 mg/kg(-1), approximately 1/7 of the LD50 of
  wildtype controls. The effects of paraquat were dose-related. De Haan et
  al. (1998) further demonstrated that paraquat transcriptionally
  upregulates Gpx1 in normal cells, reinforcing a role for GPX1 in
  protection against paraquat toxicity. Cortical neurons from Gpx1 -/-
  mice are more susceptible to peroxide; 30% of neurons from
  Gpx1-deficient mice were killed when exposed to 65 micromolar peroxide,
  whereas the wildtype controls were unaffected. De Haan et al. (1998)
  stated that their data established function for GPX1 in protection
  against some oxidative stressors and in protection of neurons against
  Reddy et al. (2001) studied the functional role of GPX1 activity in
  antioxidant mechanisms of lens in vivo by comparing lens changes of Gpx1
  knockout mice with age-matched control animals. Slit-lamp images showed
  increased nuclear light scattering (NLS) in Gpx1 knockout mice compared
  with control animals. Transmission electron microscopy revealed changes
  in the nucleus manifested by waviness of fiber membranes as early as 3
  weeks of age. The Gpx1 knockout mice developed mature cataracts after 15
  months. Reddy et al. (2001) concluded that their results demonstrated
  the critical role of GPX1 in antioxidant defense mechanisms of the lens
  nucleus. The increased NLS appeared to be associated with damage to
  nuclear fiber membranes, which might have been due to formation of lipid
  peroxides, which serve as substrates for GPX1. Cataract formation
  appeared to progress from focal opacities, apparent at an early age, to
  lamellar cataracts between 6 and 10 months, and finally to complete
  opacification in animals older than 15 months.
  Shiomi et al. (2004) created myocardial infarction by left coronary
  artery ligation in mice overexpressing Gpx1 in the heart and wildtype
  mice. Although infarct size was comparable, the transgenic mice had an
  increased survival rate with decreased left ventricular dilatation,
  dysfunction, and end-diastolic pressure compared to wildtype mice. The
  improvement in left ventricular function was accompanied by a decrease
  in myocyte hypertrophy, apoptosis, and interstitial fibrosis in the
  noninfarcted left ventricle. Shiomi et al. (2004) concluded that
  overexpression of Gpx1 protects the heart against post-myocardial
  infarction remodeling and heart failure in mice.
Allelic Variants:
  Forsberg et al. (1999) searched the human EST database to determine new
  polymorphisms in the antioxidant enzymes superoxide dismutase (see
  147450), glutathione peroxidases, catalase (115500), and microsomal
  glutathione transferase-1 (138330). When any mutation, indicated by the
  search, gave rise to a nonconservative amino acid change, they performed
  PCR restriction analysis and/or sequence analysis of genomic DNA from
  human subjects in order to verify these potential polymorphisms. In this
  way, they identified a pro197-to-leu substitution in the GPX1 gene,
  resulting from a C-to-T transition at nucleotide 593. The corresponding
  allele frequencies were approximately 70% for pro197 and 30% for leu197.
See Also:
  Board  (1983); Boivin et al. (1969); Golan et al. (1980); Johannsmann
  et al. (1981); Necheles et al. (1970); Nishimura et al. (1972); Steinberg
  et al. (1970); Steinberg and Necheles (1971)
  1. Beutler, E.; Matsumoto, F.: Ethnic variation in red cell glutathione
  peroxidase activity. Blood 46: 103-110, 1975.
  2. Beutler, E.; West, C.: Red cell glutathione peroxidase polymorphism
  in Afro-Americans. Am. J. Hum. Genet. 26: 255-258, 1974.
  3. Beutler, E.; West, C.; Beutler, B.: Electrophoretic polymorphism
  of glutathione peroxidase. Ann. Hum. Genet. 38: 163-169, 1974.
  4. Blankenberg, S.; Rupprecht, H. J.; Bickel, C.; Torzewski, M.; Hafner,
  G; Tiret, L.; Smieja, M.; Cambien, F.; Meyer, J.; Lackner, K. J.:
  Glutathione peroxidase 1 activity and cardiovascular events in patients
  with coronary artery disease. New Eng. J. Med. 349: 1605-1613, 2003.
  5. Board, P. G.: Further electrophoretic studies of erythrocyte glutathione
  peroxidase. Am. J. Hum. Genet. 35: 914-918, 1983.
  6. Bock, A.; Forchhammer, K.; Heider, J.; Leinfelder, W.; Sawers,
  G.; Veprek, B.; Zinoni, F.: Selenocysteine: the 21st amino acid. Molec.
  Microbiol. 5: 515-520, 1991.
  7. Boivin, P.; Galand, C.; Hakim, J.: Anemie hemolytique avec deficit
  en glutathion-peroxydase chez un adulte. Enzym. Biol. Clin. 10:
  68-80, 1969.
  8. Chada, S.; Le Beau, M. M.; Casey, L.; Newburger, P. E.: Isolation
  and chromosomal localization of the human glutathione peroxidase gene. Genomics   6:
  268-271, 1990.
  9. Cohen, H. J.; Chovaniec, M. E.; Mistretta, O.; Baker, S. S.: Selenium
  repletion and glutathione peroxidase-differential effects on plasma
  and red cell enzyme activity. Am. J. Clin. Nutr. 41: 735-747, 1985.
  10. de Haan, J. B.; Bladier, C.; Griffiths, P.; Kelner, M.; O'Shea,
  R. D.; Cheung, N. S.; Bronson, R. T.; Silvestro, M. J.; Wild, S.;
  Zheng, S. S.; Beart, P. M.; Hertzog, P. J.; Kola, I.: Mice with a
  homozygous null mutation for the most abundant glutathione peroxidase,
  Gpx1, show increased susceptibility to the oxidative stress-inducing
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  21. Am. J. Hum. Genet. 29: 563-570, 1977.
  12. Forsberg, L.; de Faire, U.; Morgenstern, R.: Low yield of polymorphisms
  from EST Blast searching: analysis of genes related to oxidative stress
  and verification of the P197L polymorphism in GPX1. Hum. Mutat. 13:
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  13. Golan, R.; Ezzer, J. B.; Szeinberg, A.: Red cell glutathione
  peroxidase in various Jewish ethnic groups in Israel. Hum. Hered. 30:
  136-141, 1980.
  14. Johannsmann, R.; Hellkuhl, B.; Grzeschik, K.-H.: Regional mapping
  of human chromosome 3: assignment of a glutathione peroxidase-1 gene
  to 3p13-3q12. Hum. Genet. 56: 361-363, 1981.
  15. Johannsmann, R.; Hellkuhl, B.; Grzeschik, K.-H.: Regional assignment
  of a gene for glutathione peroxidase on human chromosome 3. (Abstract) Cytogenet  .
  Cell Genet. 25: 167 only, 1979.
  16. Kiss, C.; Li, J.; Szeles, A.; Gizatullin, R. Z.; Kashuba, V. I.;
  Lushnikova, T.; Protopopov, A. I.; Kelve, M.; Kiss, H.; Kholodnyuk,
  I. D.; Imreh, S.; Klein, G.; Zabarovsky, E. R.: Assignment of the
  ARHA and GPX1 genes to human chromosome bands 3p21.3 by in situ hybridization
  and with somatic cell hybrids. Cytogenet. Cell Genet. 79: 228-230,
  17. Le Beau, M. M.: Personal Communication. Chicago, Ill.  1/23/1989.
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  sublocalization of the human glutathione peroxidase gene. (Abstract) Cytogenet.
  Cell Genet. 51: 1030 only, 1989.
  19. McBride, O. W.; Mitchell, A.; Lee, B. J.; Mullenbach, G.; Hatfield,
  D.: Gene for selenium-dependent glutathione peroxidase maps to human
  chromosomes 3, 21 and X. BioFactors 1: 285-292, 1988.
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  cell glutathione peroxidase (GPX1) variation in Afro-Jamaican, Asiatic
  Indian, and Dutch populations: is the GPX1*2 allele of 'Thomas' variant
  an African marker? Hum. Genet. 66: 352-355, 1984.
  21. Meera Khan, P.; Verma, C.; Wijnen, L. M. M.; Wijnen, J. T.; Prins,
  H. K.; Nijenhuis, L. E.: Electrotypes and formal genetics of red
  cell glutathione peroxidase (GPX1) in the Djuka of Surinam. Am. J.
  Hum. Genet. 38: 712-723, 1986.
  22. Mehdizadeh, S.; Warden, C. H.; Wen, P.-Z.; Xia, Y.-R.; Mehrabian,
  M.; Lusis, A. J.: The glutathione peroxidase gene, Gpx1, maps to
  mouse chromosome 9. Mammalian Genome 7: 465-466, 1996.
  23. Necheles, T. F.; Boles, T. A.; Allen, D. M.: Erythrocyte glutathione-peroxid  ase
  deficiency and hemolytic disease of the newborn infant. J. Pediat. 72:
  319-324, 1968.
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  D. M.: Homozygous erythrocyte glutathione-peroxidase deficiency:
  clinical and biochemical studies. Blood 33: 164-169, 1969.
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  deficiency. Brit. J. Haemat. 19: 605-612, 1970.
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  J.; Musch, D. C.; Boyle, D. L.; Takemoto, L. J.; Ho, Y.-S.; Knoernschild,
  T.; Juenemann, A.; Lutjen-Drecoll, E.: Glutathione peroxidase-1 deficiency
  leads to increased nuclear light scattering, membrane damage, and
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  trinucleotide repeat in the coding region of the human cellular glutathione
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  S.; Ikeuchi, M.; Wen, J.; Kubota, T.; Utsumi, H.; Takeshita, A.:
  Overexpression of glutathione peroxidase prevents left ventricular
  remodeling and failure after myocardial infarction in mice. Circulation 109:
  544-549, 2004.
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  H.: Increase in glutathione peroxidase activity in erythrocytes from
  trisomy 21 subjects. Biochem. Biophys. Res. Commun. 67: 910-915,
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  deficiency: biochemical studies on the mechanisms of drug-induced
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  coding for human glutathione peroxidase. Nucleic Acids Res. 15:
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  and characterization of human plasma glutathione peroxidase: a selenoglycoprotei  n
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  677-686, 1987.
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  protein: absence in selenium deficiency states and correlation with
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  Pediat. 111: 711-717, 1987.
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  P.: Assignment of a gene for glutathione peroxidase (GPX-1) to human
  chromosome 3. Cytogenet. Cell Genet. 22: 232-238, 1978.
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  Dis. 15: 261-268, 1992.
Clinical Synopsis:
     Hemolytic disease of the newborn;
     Compensated hemolytic anemia
     Neonatal hyperbilirubinemia
     Glutathione peroxidase deficiency;
     Heinz bodies
     Selenium deficiency interaction
     Autosomal recessive (3q11-q12)
  Marla J. F. O'Neill - updated: 11/3/2005
  Victor A. McKusick - updated: 11/3/2003
  Jane Kelly - updated: 7/2/2002
  Ada Hamosh - updated: 7/28/2000
  Victor A. McKusick - updated: 5/14/1999
  Victor A. McKusick - updated: 5/28/1998
Creation Date: 
  Victor A. McKusick: 3/9/1989
Edit Dates: 
  carol: 01/08/2010
  wwang: 12/28/2009
  wwang: 11/3/2005
  terry: 4/6/2005
  mgross: 3/17/2004
  tkritzer: 11/6/2003
  tkritzer: 11/4/2003
  terry: 11/3/2003
  mgross: 7/2/2002
  carol: 6/22/2001
  alopez: 8/1/2000
  terry: 7/28/2000
  mgross: 6/3/1999
  mgross: 5/26/1999
  terry: 5/14/1999
  terry: 4/30/1999
  terry: 6/1/1998
  terry: 5/28/1998
  joanna: 6/20/1997
  mark: 10/11/1996
  terry: 9/20/1996
  terry: 1/11/1995
  mimadm: 9/24/1994
  warfield: 4/8/1994
  pfoster: 2/18/1994
  carol: 7/8/1992
  carol: 3/31/1992
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