Glutathione peroxidase 5

Template:PBB Glutathione peroxidase 5 (GPx-5), also known as epididymal secretory glutathione peroxidase is an enzyme that in humans is encoded by the GPX5 gene.^[1]^[2]

GPx-5 belongs to the glutathione peroxidase family. It is specifically expressed in the epididymis in the mammalian male reproductive tract, and is androgen-regulated. Unlike mRNAs for other characterized glutathione peroxidases, this mRNA does not contain a selenocysteine (UGA) codon. Thus, the encoded protein is selenium-independent, and has been proposed to play a role in protecting the membranes of spermatozoa from the damaging effects of lipid peroxidation and/or preventing premature acrosome reaction. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.^[1]

References

^ ^a ^b "Entrez Gene: glutathione peroxidase 5 (epididymal androgen-related protein)".
^ Hall L, Williams K, Perry AC, Frayne J, Jury JA (July 1998). "The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract". Biochem. J. 333 (1): 5–9. PMC 1219548. PMID 9639555.{{cite journal}}: CS1 maint: multiple names: authors list (link)

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Perry AC, Jones R, Niang LS, et al. (1992). "Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon". Biochem. J. 285 (3): 863–70. PMC 1132876. PMID 1386734.
Richard MJ, Guiraud P, Didier C, et al. (2001). "Human immunodeficiency virus type 1 Tat protein impairs selenoglutathione peroxidase expression and activity by a mechanism independent of cellular selenium uptake: consequences on cellular resistance to UV-A radiation". Arch. Biochem. Biophys. 386 (2): 213–20. doi:10.1006/abbi.2000.2197. PMID 11368344.
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Rejraji H, Vernet P, Drevet JR (2002). "GPX5 is present in the mouse caput and cauda epididymidis lumen at three different locations". Mol. Reprod. Dev. 63 (1): 96–103. doi:10.1002/mrd.10136. PMID 12211066.{{cite journal}}: CS1 maint: multiple names: authors list (link)
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Choi J, Liu RM, Kundu RK, et al. (2000). "Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice". J. Biol. Chem. 275 (5): 3693–8. doi:10.1074/jbc.275.5.3693. PMID 10652368.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Vernet P, Faure J, Dufaure JP, Drevet JR (1997). "Tissue and developmental distribution, dependence upon testicular factors and attachment to spermatozoa of GPX5, a murine epididymis-specific glutathione peroxidase". Mol. Reprod. Dev. 47 (1): 87–98. doi:10.1002/(SICI)1098-2795(199705)47:1<87::AID-MRD12>3.0.CO;2-X. PMID 9110319.{{cite journal}}: CS1 maint: multiple names: authors list (link)
Price TO, Ercal N, Nakaoke R, Banks WA (2005). "HIV-1 viral proteins gp120 and Tat induce oxidative stress in brain endothelial cells". Brain Res. 1045 (1–2): 57–63. doi:10.1016/j.brainres.2005.03.031. PMID 15910762.{{cite journal}}: CS1 maint: multiple names: authors list (link)
Williams K, Frayne J, Hall L (1998). "Expression of extracellular glutathione peroxidase type 5 (GPX5) in the rat male reproductive tract". Mol. Hum. Reprod. 4 (9): 841–8. doi:10.1093/molehr/4.9.841. PMID 9783843.{{cite journal}}: CS1 maint: multiple names: authors list (link)
Bailey SD, Xie C, Do R, et al. (2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study". Diabetes Care. 33 (10): 2250–3. doi:10.2337/dc10-0452. PMC 2945168. PMID 20628086.
Moyer AM, Sun Z, Batzler AJ, et al. (2010). "Glutathione pathway genetic polymorphisms and lung cancer survival after platinum-based chemotherapy". Cancer Epidemiol. Biomarkers Prev. 19 (3): 811–21. doi:10.1158/1055-9965.EPI-09-0871. PMC 2837367. PMID 20200426.

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[entrez-1] "Entrez Gene: glutathione peroxidase 5 (epididymal androgen-related protein)".

[pmid9639555-2] Hall L, Williams K, Perry AC, Frayne J, Jury JA (July 1998). "The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract". Biochem. J. 333 (1): 5–9. PMC 1219548. PMID 9639555.{{cite journal}}: CS1 maint: multiple names: authors list (link)

[1]

[2]

v t e Oxidoreductases: peroxidases (EC 1.11)
1.11.1.1-14	NADH peroxidase NADPH peroxidase Fatty-acid peroxidase Catalase Cytochrome c peroxidase Eosinophil peroxidase Glutathione peroxidase GPX 1 2 3 4 5 6 7 8 Horseradish peroxidase Lactoperoxidase Myeloperoxidase Thyroid peroxidase Deiodinase Iodothyronine deiodinase Iodotyrosine deiodinase
1.11.1.15 (peroxiredoxin)	1 2 3 4 5 6

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

References

Further reading