Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa

Autores
Romanato, M.; Regueira, E.; Cameo, M.S.; Baldini, C.; Calvo, L.; Calvo, J.C.
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background: Human spermatozoa decondense in vitro upon exposure to heparin and glutathione. Glutathione is also the disulfide bond reducer in vivo, and heparan sulfate, a functional analogue of heparin, has been proposed as the protamine acceptor. The aim of this study was to evaluate the decondensing ability of chemically modified heparins and different glycosaminoglycans (GAGs) on isolated sperm nuclei in vitro, and to analyse the possible role of different GAGs as protamine acceptors. Methods: Capacitated spermatozoa and isolated sperm nuclei from normospermic semen samples were decondensed in the presence of heparin (or its equivalent) and glutathione. After fixation with glutaraldehyde, the percentage of decondensed spermatozoa and nuclei was determined under phase-contrast. Proteins were extracted from sperm nuclei previously incubated in the presence of gluhathione and different GAGs by incubation with urea-β-meracptoethanol-NaCl, and analysed by acid polyacrylamide gel electrophoresis. Results: The ability of desulfated heparins and other GAGs to decondense isolated nuclei mirrored exactly the decondensation of capacitated spermatozoa, the only difference being the level of maximum decondensation achieved. Heparan sulfate and heparin, but not other GAGs, were able to release protamines from sperm chromatin. Conclusions: Heparan sulfate could be functioning as protamine acceptor in vivo during human sperm nuclear decondensation. © The Author 2005. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.
Fil:Romanato, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Regueira, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Calvo, J.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Hum. Reprod. 2005;20(10):2784-2789
Materia
Heparan sulfate
Protamine
Sperm nuclear decondensation
glutaraldehyde
glutathione
glycosaminoglycan
heparan sulfate
heparin
protamine
article
carbohydrate analysis
cell isolation
chromatin condensation
drug activity
human
human cell
immunocytochemistry
in vitro study
male
phase contrast microscopy
polyacrylamide gel electrophoresis
protein analysis
protein isolation
protein secretion
semen analysis
spermatozoon capacitation
spermatozoon density
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_02681161_v20_n10_p2784_Romanato

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oai_identifier_str paperaa:paper_02681161_v20_n10_p2784_Romanato
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoaRomanato, M.Regueira, E.Cameo, M.S.Baldini, C.Calvo, L.Calvo, J.C.Heparan sulfateProtamineSperm nuclear decondensationglutaraldehydeglutathioneglycosaminoglycanheparan sulfateheparinprotaminearticlecarbohydrate analysiscell isolationchromatin condensationdrug activityhumanhuman cellimmunocytochemistryin vitro studymalephase contrast microscopypolyacrylamide gel electrophoresisprotein analysisprotein isolationprotein secretionsemen analysisspermatozoon capacitationspermatozoon densityBackground: Human spermatozoa decondense in vitro upon exposure to heparin and glutathione. Glutathione is also the disulfide bond reducer in vivo, and heparan sulfate, a functional analogue of heparin, has been proposed as the protamine acceptor. The aim of this study was to evaluate the decondensing ability of chemically modified heparins and different glycosaminoglycans (GAGs) on isolated sperm nuclei in vitro, and to analyse the possible role of different GAGs as protamine acceptors. Methods: Capacitated spermatozoa and isolated sperm nuclei from normospermic semen samples were decondensed in the presence of heparin (or its equivalent) and glutathione. After fixation with glutaraldehyde, the percentage of decondensed spermatozoa and nuclei was determined under phase-contrast. Proteins were extracted from sperm nuclei previously incubated in the presence of gluhathione and different GAGs by incubation with urea-β-meracptoethanol-NaCl, and analysed by acid polyacrylamide gel electrophoresis. Results: The ability of desulfated heparins and other GAGs to decondense isolated nuclei mirrored exactly the decondensation of capacitated spermatozoa, the only difference being the level of maximum decondensation achieved. Heparan sulfate and heparin, but not other GAGs, were able to release protamines from sperm chromatin. Conclusions: Heparan sulfate could be functioning as protamine acceptor in vivo during human sperm nuclear decondensation. © The Author 2005. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.Fil:Romanato, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Regueira, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Calvo, J.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2005info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_02681161_v20_n10_p2784_RomanatoHum. Reprod. 2005;20(10):2784-2789reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-04T09:48:21Zpaperaa:paper_02681161_v20_n10_p2784_RomanatoInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-04 09:48:22.651Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa
title Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa
spellingShingle Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa
Romanato, M.
Heparan sulfate
Protamine
Sperm nuclear decondensation
glutaraldehyde
glutathione
glycosaminoglycan
heparan sulfate
heparin
protamine
article
carbohydrate analysis
cell isolation
chromatin condensation
drug activity
human
human cell
immunocytochemistry
in vitro study
male
phase contrast microscopy
polyacrylamide gel electrophoresis
protein analysis
protein isolation
protein secretion
semen analysis
spermatozoon capacitation
spermatozoon density
title_short Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa
title_full Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa
title_fullStr Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa
title_full_unstemmed Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa
title_sort Further evidence on the role of heparan sulfate as protamine acceptor during the decondensation of human spermatozoa
dc.creator.none.fl_str_mv Romanato, M.
Regueira, E.
Cameo, M.S.
Baldini, C.
Calvo, L.
Calvo, J.C.
author Romanato, M.
author_facet Romanato, M.
Regueira, E.
Cameo, M.S.
Baldini, C.
Calvo, L.
Calvo, J.C.
author_role author
author2 Regueira, E.
Cameo, M.S.
Baldini, C.
Calvo, L.
Calvo, J.C.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Heparan sulfate
Protamine
Sperm nuclear decondensation
glutaraldehyde
glutathione
glycosaminoglycan
heparan sulfate
heparin
protamine
article
carbohydrate analysis
cell isolation
chromatin condensation
drug activity
human
human cell
immunocytochemistry
in vitro study
male
phase contrast microscopy
polyacrylamide gel electrophoresis
protein analysis
protein isolation
protein secretion
semen analysis
spermatozoon capacitation
spermatozoon density
topic Heparan sulfate
Protamine
Sperm nuclear decondensation
glutaraldehyde
glutathione
glycosaminoglycan
heparan sulfate
heparin
protamine
article
carbohydrate analysis
cell isolation
chromatin condensation
drug activity
human
human cell
immunocytochemistry
in vitro study
male
phase contrast microscopy
polyacrylamide gel electrophoresis
protein analysis
protein isolation
protein secretion
semen analysis
spermatozoon capacitation
spermatozoon density
dc.description.none.fl_txt_mv Background: Human spermatozoa decondense in vitro upon exposure to heparin and glutathione. Glutathione is also the disulfide bond reducer in vivo, and heparan sulfate, a functional analogue of heparin, has been proposed as the protamine acceptor. The aim of this study was to evaluate the decondensing ability of chemically modified heparins and different glycosaminoglycans (GAGs) on isolated sperm nuclei in vitro, and to analyse the possible role of different GAGs as protamine acceptors. Methods: Capacitated spermatozoa and isolated sperm nuclei from normospermic semen samples were decondensed in the presence of heparin (or its equivalent) and glutathione. After fixation with glutaraldehyde, the percentage of decondensed spermatozoa and nuclei was determined under phase-contrast. Proteins were extracted from sperm nuclei previously incubated in the presence of gluhathione and different GAGs by incubation with urea-β-meracptoethanol-NaCl, and analysed by acid polyacrylamide gel electrophoresis. Results: The ability of desulfated heparins and other GAGs to decondense isolated nuclei mirrored exactly the decondensation of capacitated spermatozoa, the only difference being the level of maximum decondensation achieved. Heparan sulfate and heparin, but not other GAGs, were able to release protamines from sperm chromatin. Conclusions: Heparan sulfate could be functioning as protamine acceptor in vivo during human sperm nuclear decondensation. © The Author 2005. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.
Fil:Romanato, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Regueira, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Calvo, J.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Background: Human spermatozoa decondense in vitro upon exposure to heparin and glutathione. Glutathione is also the disulfide bond reducer in vivo, and heparan sulfate, a functional analogue of heparin, has been proposed as the protamine acceptor. The aim of this study was to evaluate the decondensing ability of chemically modified heparins and different glycosaminoglycans (GAGs) on isolated sperm nuclei in vitro, and to analyse the possible role of different GAGs as protamine acceptors. Methods: Capacitated spermatozoa and isolated sperm nuclei from normospermic semen samples were decondensed in the presence of heparin (or its equivalent) and glutathione. After fixation with glutaraldehyde, the percentage of decondensed spermatozoa and nuclei was determined under phase-contrast. Proteins were extracted from sperm nuclei previously incubated in the presence of gluhathione and different GAGs by incubation with urea-β-meracptoethanol-NaCl, and analysed by acid polyacrylamide gel electrophoresis. Results: The ability of desulfated heparins and other GAGs to decondense isolated nuclei mirrored exactly the decondensation of capacitated spermatozoa, the only difference being the level of maximum decondensation achieved. Heparan sulfate and heparin, but not other GAGs, were able to release protamines from sperm chromatin. Conclusions: Heparan sulfate could be functioning as protamine acceptor in vivo during human sperm nuclear decondensation. © The Author 2005. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.
publishDate 2005
dc.date.none.fl_str_mv 2005
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_02681161_v20_n10_p2784_Romanato
url http://hdl.handle.net/20.500.12110/paper_02681161_v20_n10_p2784_Romanato
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Hum. Reprod. 2005;20(10):2784-2789
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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