Thiol-disulfide proteins of stallion epididymal spermatozoa

Universidade Estadual do Norte Fluminense (UENF). Centro de Biociências e Biotecnologia. Laboratório de Biologia Celular e Tecidual. Campos dos Goytacases, RJ, Brasil.

Detalles Bibliográficos
Autores: Dias, G. M., Lopez, M. L., Ferreira, A. T. S., Chapeaurouge, D. A., Rodrigues, A., Perales, J., Retamal, C. A.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:Brasil
Institución:Fundação Oswaldo Cruz (FIOCRUZ)
Repositorio:Repositório Institucional da FIOCRUZ (ARCA)
Idioma:inglés
OAI Identifier:oai:arca.fiocruz.br:icict/10767
Acceso en línea:https://arca.fiocruz.br/handle/icict/10767
Access Level:acceso abierto
Palabra clave:Maturação do Esperma
Espermatozoides
Reagentes de Sulfidrila
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dc.title.none.fl_str_mv Thiol-disulfide proteins of stallion epididymal spermatozoa
title Thiol-disulfide proteins of stallion epididymal spermatozoa
spellingShingle Thiol-disulfide proteins of stallion epididymal spermatozoa
Dias, G. M.
Maturação do Esperma
Espermatozoides
Reagentes de Sulfidrila
title_short Thiol-disulfide proteins of stallion epididymal spermatozoa
title_full Thiol-disulfide proteins of stallion epididymal spermatozoa
title_fullStr Thiol-disulfide proteins of stallion epididymal spermatozoa
title_full_unstemmed Thiol-disulfide proteins of stallion epididymal spermatozoa
title_sort Thiol-disulfide proteins of stallion epididymal spermatozoa
dc.creator.none.fl_str_mv Dias, G. M.
Lopez, M. L.
Ferreira, A. T. S.
Chapeaurouge, D. A.
Rodrigues, A.
Perales, J.
Retamal, C. A.
author Dias, G. M.
author_facet Dias, G. M.
Lopez, M. L.
Ferreira, A. T. S.
Chapeaurouge, D. A.
Rodrigues, A.
Perales, J.
Retamal, C. A.
author_role author
author2 Lopez, M. L.
Ferreira, A. T. S.
Chapeaurouge, D. A.
Rodrigues, A.
Perales, J.
Retamal, C. A.
author2_role author
author
author
author
author
author
dc.subject.decs.none.fl_str_mv Maturação do Esperma
Espermatozoides
Reagentes de Sulfidrila
topic Maturação do Esperma
Espermatozoides
Reagentes de Sulfidrila
description Universidade Estadual do Norte Fluminense (UENF). Centro de Biociências e Biotecnologia. Laboratório de Biologia Celular e Tecidual. Campos dos Goytacases, RJ, Brasil.
publishDate 2014
dc.date.issued.fl_str_mv 2014
dc.date.accessioned.fl_str_mv 2015-06-10T13:55:20Z
dc.date.available.fl_str_mv 2015-06-10T13:55:20Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.citation.fl_str_mv DIAS, G. M. et al. Thiol-disulfide proteins of stallion epididymal spermatozoa. Animal Reproduction Science, v.145, n.1-2, p.29-39, 2014.
dc.identifier.uri.fl_str_mv https://arca.fiocruz.br/handle/icict/10767
dc.identifier.issn.none.fl_str_mv 0378-4320
dc.identifier.doi.none.fl_str_mv 10.1016/j.anireprosci.2013.12.007
identifier_str_mv DIAS, G. M. et al. Thiol-disulfide proteins of stallion epididymal spermatozoa. Animal Reproduction Science, v.145, n.1-2, p.29-39, 2014.
0378-4320
10.1016/j.anireprosci.2013.12.007
url https://arca.fiocruz.br/handle/icict/10767
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Institucional da FIOCRUZ (ARCA)
instname:Fundação Oswaldo Cruz (FIOCRUZ)
instacron:FIOCRUZ
instname_str Fundação Oswaldo Cruz (FIOCRUZ)
instacron_str FIOCRUZ
institution FIOCRUZ
reponame_str Repositório Institucional da FIOCRUZ (ARCA)
collection Repositório Institucional da FIOCRUZ (ARCA)
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spelling 2015-06-10T13:55:20Z2015-06-10T13:55:20Z2014DIAS, G. M. et al. Thiol-disulfide proteins of stallion epididymal spermatozoa. Animal Reproduction Science, v.145, n.1-2, p.29-39, 2014.0378-4320https://arca.fiocruz.br/handle/icict/1076710.1016/j.anireprosci.2013.12.007engElsevierThiol-disulfide proteins of stallion epididymal spermatozoainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleUniversidade Estadual do Norte Fluminense (UENF). Centro de Biociências e Biotecnologia. Laboratório de Biologia Celular e Tecidual. Campos dos Goytacases, RJ, Brasil.Universidade Estadual do Norte Fluminense (UENF). Centro de Biociências e Biotecnologia. Laboratório de Biologia Celular e Tecidual. Campos dos Goytacases, RJ, Brasil.Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil.Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil.Universidade Estadual do Norte Fluminense (UENF). Centro de Biociências e Biotecnologia. Laboratório de Biologia Celular e Tecidual. Campos dos Goytacases, RJ, Brasil.undação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil.Universidade Estadual do Norte Fluminense (UENF). Centro de Biociências e Biotecnologia. Laboratório de Biologia Celular e Tecidual. Campos dos Goytacases, RJ, Brasil.Thiol groups of cysteine residues represent redox centers involved in multiple biological functions. It has been postulated that changes in the redox status of mammalian epididymal spermatozoa contribute to the sperm maturation process. The present work shows the thiol-disulfide protein profile of stallion epididymal spermatozoa achieved by twodimension electrophoresis and MALDI-TOF/TOF mass spectrometry of proteins labeled with a thiol-reactive fluorescent tag, monobromobimane. Our results have shown the formation of disulfide bonds in several sperm protein fractions during the epididymal maturation process. The majority of the oxidized thiol sperm proteins identified correspond to structural molecules of the flagellum (as the outer dense fiber-1 protein – ODF1), followed by glycolytic enzymes (as glyceraldehyde-3-phosphate dehydrogenase spermatogenic), antioxidant protectors (as glutathione S-transferase and phospholipid hydroperoxide glutathione peroxidase – PHGPx). The magnitude of the thiol oxidation differs between proteins, and was more drastic in polypeptides with molecular weights of up to 33 kDa, identified as ODF1 and PHGPx. A kinase anchor protein, a voltage-dependent anion channel protein and a zona pellucida-binding protein were also found in the polypeptide samples that contained oxidized SH groups. These proteins may be modified or controlled by the mechanisms involved in the cysteine-redox changes, corroborating the belief that a correct degree of protein oxidation is required for the stabilization of sperm structure, protection against oxidative damage, induction of progressive sperm motility and fertilization.Maturação do EspermaEspermatozoidesReagentes de Sulfidrilainfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZDias, G. M.Lopez, M. L.Ferreira, A. T. S.Chapeaurouge, D. A.Rodrigues, A.Perales, J.Retamal, C. 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