Redox regulation of mammalian sperm capacitation
Capacitation is a series of morphological and metabolic changes necessary for the spermatozoon to achieve fertilizing ability. One of the earlier happenings during mammalian sperm capacitation is the production of reactive oxygen species (ROS) that will trigger and regulate a series of events includ...
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Format: | Article |
Language: | English |
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Wolters Kluwer Medknow Publications
2015-01-01
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Series: | Asian Journal of Andrology |
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Online Access: | http://www.ajandrology.com/article.asp?issn=1008-682X;year=2015;volume=17;issue=4;spage=583;epage=590;aulast=O'Flaherty |
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author | Cristian O′Flaherty |
author_facet | Cristian O′Flaherty |
author_sort | Cristian O′Flaherty |
collection | DOAJ |
description | Capacitation is a series of morphological and metabolic changes necessary for the spermatozoon to achieve fertilizing ability. One of the earlier happenings during mammalian sperm capacitation is the production of reactive oxygen species (ROS) that will trigger and regulate a series of events including protein phosphorylation, in a time-dependent fashion. The identity of the sperm oxidase responsible for the production of ROS involved in capacitation is still elusive, and several candidates are discussed in this review. Interestingly, ROS-induced ROS formation has been described during human sperm capacitation. Redox signaling during capacitation is associated with changes in thiol groups of proteins located on the plasma membrane and subcellular compartments of the spermatozoon. Both, oxidation of thiols forming disulfide bridges and the increase on thiol content are necessary to regulate different sperm proteins associated with capacitation. Reducing equivalents such as NADH and NADPH are necessary to support capacitation in many species including humans. Lactate dehydrogenase, glucose-6-phospohate dehydrogenase, and isocitrate dehydrogenase are responsible in supplying NAD (P) H for sperm capacitation. Peroxiredoxins (PRDXs) are newly described enzymes with antioxidant properties that can protect mammalian spermatozoa; however, they are also candidates for assuring the regulation of redox signaling required for sperm capacitation. The dysregulation of PRDXs and of enzymes needed for their reactivation such as thioredoxin/thioredoxin reductase system and glutathione-S-transferases impairs sperm motility, capacitation, and promotes DNA damage in spermatozoa leading to male infertility. |
first_indexed | 2024-12-11T02:53:09Z |
format | Article |
id | doaj.art-e51b183730c048c1a52a884a11fcf601 |
institution | Directory Open Access Journal |
issn | 1008-682X 1745-7262 |
language | English |
last_indexed | 2024-12-11T02:53:09Z |
publishDate | 2015-01-01 |
publisher | Wolters Kluwer Medknow Publications |
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series | Asian Journal of Andrology |
spelling | doaj.art-e51b183730c048c1a52a884a11fcf6012022-12-22T01:23:15ZengWolters Kluwer Medknow PublicationsAsian Journal of Andrology1008-682X1745-72622015-01-0117458359010.4103/1008-682X.153303Redox regulation of mammalian sperm capacitationCristian O′FlahertyCapacitation is a series of morphological and metabolic changes necessary for the spermatozoon to achieve fertilizing ability. One of the earlier happenings during mammalian sperm capacitation is the production of reactive oxygen species (ROS) that will trigger and regulate a series of events including protein phosphorylation, in a time-dependent fashion. The identity of the sperm oxidase responsible for the production of ROS involved in capacitation is still elusive, and several candidates are discussed in this review. Interestingly, ROS-induced ROS formation has been described during human sperm capacitation. Redox signaling during capacitation is associated with changes in thiol groups of proteins located on the plasma membrane and subcellular compartments of the spermatozoon. Both, oxidation of thiols forming disulfide bridges and the increase on thiol content are necessary to regulate different sperm proteins associated with capacitation. Reducing equivalents such as NADH and NADPH are necessary to support capacitation in many species including humans. Lactate dehydrogenase, glucose-6-phospohate dehydrogenase, and isocitrate dehydrogenase are responsible in supplying NAD (P) H for sperm capacitation. Peroxiredoxins (PRDXs) are newly described enzymes with antioxidant properties that can protect mammalian spermatozoa; however, they are also candidates for assuring the regulation of redox signaling required for sperm capacitation. The dysregulation of PRDXs and of enzymes needed for their reactivation such as thioredoxin/thioredoxin reductase system and glutathione-S-transferases impairs sperm motility, capacitation, and promotes DNA damage in spermatozoa leading to male infertility.http://www.ajandrology.com/article.asp?issn=1008-682X;year=2015;volume=17;issue=4;spage=583;epage=590;aulast=O'Flahertygene regulationMusashiMusashi-1Musashi-2posttranscriptional controlRNA binding proteinsspermatogenesissplicingtestistranslationcell fatecell stressimportinkaryopherinnucleocytoplasmic transportspermatidspermatocytespermatogenesisartificial inseminationbiomarkerfertilityfertilizationflow cytometryinfertilitynanotechnologyoocyte activationPostacrosomal Sheath WWI Domain Binding ProteinspermSPTRX3thioredoxinubiquitinATP binding cassette transportersalbuminhigh-density lipoproteinlipid raftsmembrane fluiditymembrane microdomainsmembrane packingoxysterolsreverse cholesterol transportsterol transporterseggfertilizationheat shock protein A2molecular chaperonespermsperm-egg interactionsdehydrogenasesoxidasesperoxiredoxinsreactive oxygen speciesspermatozoathiolsthioredoxins |
spellingShingle | Cristian O′Flaherty Redox regulation of mammalian sperm capacitation Asian Journal of Andrology gene regulation Musashi Musashi-1 Musashi-2 posttranscriptional control RNA binding proteins spermatogenesis splicing testis translation cell fate cell stress importin karyopherin nucleocytoplasmic transport spermatid spermatocyte spermatogenesis artificial insemination biomarker fertility fertilization flow cytometry infertility nanotechnology oocyte activation Postacrosomal Sheath WWI Domain Binding Protein sperm SPTRX3 thioredoxin ubiquitin ATP binding cassette transporters albumin high-density lipoprotein lipid rafts membrane fluidity membrane microdomains membrane packing oxysterols reverse cholesterol transport sterol transporters egg fertilization heat shock protein A2 molecular chaperone sperm sperm-egg interactions dehydrogenases oxidases peroxiredoxins reactive oxygen species spermatozoa thiols thioredoxins |
title | Redox regulation of mammalian sperm capacitation |
title_full | Redox regulation of mammalian sperm capacitation |
title_fullStr | Redox regulation of mammalian sperm capacitation |
title_full_unstemmed | Redox regulation of mammalian sperm capacitation |
title_short | Redox regulation of mammalian sperm capacitation |
title_sort | redox regulation of mammalian sperm capacitation |
topic | gene regulation Musashi Musashi-1 Musashi-2 posttranscriptional control RNA binding proteins spermatogenesis splicing testis translation cell fate cell stress importin karyopherin nucleocytoplasmic transport spermatid spermatocyte spermatogenesis artificial insemination biomarker fertility fertilization flow cytometry infertility nanotechnology oocyte activation Postacrosomal Sheath WWI Domain Binding Protein sperm SPTRX3 thioredoxin ubiquitin ATP binding cassette transporters albumin high-density lipoprotein lipid rafts membrane fluidity membrane microdomains membrane packing oxysterols reverse cholesterol transport sterol transporters egg fertilization heat shock protein A2 molecular chaperone sperm sperm-egg interactions dehydrogenases oxidases peroxiredoxins reactive oxygen species spermatozoa thiols thioredoxins |
url | http://www.ajandrology.com/article.asp?issn=1008-682X;year=2015;volume=17;issue=4;spage=583;epage=590;aulast=O'Flaherty |
work_keys_str_mv | AT cristianoflaherty redoxregulationofmammalianspermcapacitation |