Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation
- Autores
- Sanchez, M.C.; Alvarez Sedo, C.; Julianelli, V.L.; Romanato, M.; Calvo, L.; Calvo, J.C.; Fontana, V.A.
- Año de publicación
- 2013
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The mammalian sperm nucleus contains an unusually condensed chromatin, due to replacement of the majority of histones by protamines. However, soon after the spermatozoon penetrates the ooplasm at fertilization, decondensation of this densely packed chromatin must occur to allow formation of the male pronucleus and syngamy. Decondensation is accomplished by protamine disulfide bond reduction by oocyte glutathione and replacement of protamines by oocyte histones with the aid of an acceptor molecule. Previous results from our laboratory have demonstrated that heparan sulfate (HS) present in the ooplasm functions as protamine acceptor during human sperm decondensation in vivo. In the present paper, we analyze the role of heparin, structural analogue of HS, and dermatan sulfate (DS) in murine sperm chromatin decondensation in vitro, including the possibility of a synergistic effect between both glycosaminoglycans. Decondensation was assessed under phase contrast microscopy following incubation of murine spermatozoa with glutathione and either heparin, DS, or a combination of both. Ultrastructural changes taking place during decondensation were analyzed by transmission electron microscopy. Both glycosaminoglycans were able to promote the decondensation of murine spermatozoa in vitro but the decondensing ability of heparin was significantly higher. Use of both glycosaminoglycans together revealed the existence of a synergistic effect. Transmission electron microscopy analysis of decondensing spermatozoa supported these findings. Synergism between heparin and DS was observed both in capacitated and non-capacitated spermatozoa but decondensation kinetics was faster in the former. The results obtained indicate a new potential role for dermatan sulfate in murine sperm decondensation at fertilization and provide evidence of differences in the degree of chromatin condensation throughout the murine sperm nucleus. © 2013 Informa Healthcare USA, Inc.
Fil:Julianelli, V.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Romanato, M. 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.
Fil:Fontana, V.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. - Fuente
- Syst. Biology Reprod. Med. 2013;59(2):82-90
- Materia
-
Chromatin decondensation
Dermatan sulfate
Heparin
Murine spermatozoa
Synergism
dermatan sulfate
glutathione
glycosaminoglycan
heparin
animal cell
article
chromatin
chromatin decondensation'
controlled study
dose response
in vitro study
male
mouse
nonhuman
phase contrast microscopy
priority journal
spermatozoon
transmission electron microscopy
Animals
Chromatin
Dermatan Sulfate
Dose-Response Relationship, Drug
Heparin
Male
Mice
Microscopy, Electron
Spermatozoa - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/2.5/ar
- Repositorio
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_19396368_v59_n2_p82_Sanchez
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Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensationSanchez, M.C.Alvarez Sedo, C.Julianelli, V.L.Romanato, M.Calvo, L.Calvo, J.C.Fontana, V.A.Chromatin decondensationDermatan sulfateHeparinMurine spermatozoaSynergismdermatan sulfateglutathioneglycosaminoglycanheparinanimal cellarticlechromatinchromatin decondensation'controlled studydose responsein vitro studymalemousenonhumanphase contrast microscopypriority journalspermatozoontransmission electron microscopyAnimalsChromatinDermatan SulfateDose-Response Relationship, DrugHeparinMaleMiceMicroscopy, ElectronSpermatozoaThe mammalian sperm nucleus contains an unusually condensed chromatin, due to replacement of the majority of histones by protamines. However, soon after the spermatozoon penetrates the ooplasm at fertilization, decondensation of this densely packed chromatin must occur to allow formation of the male pronucleus and syngamy. Decondensation is accomplished by protamine disulfide bond reduction by oocyte glutathione and replacement of protamines by oocyte histones with the aid of an acceptor molecule. Previous results from our laboratory have demonstrated that heparan sulfate (HS) present in the ooplasm functions as protamine acceptor during human sperm decondensation in vivo. In the present paper, we analyze the role of heparin, structural analogue of HS, and dermatan sulfate (DS) in murine sperm chromatin decondensation in vitro, including the possibility of a synergistic effect between both glycosaminoglycans. Decondensation was assessed under phase contrast microscopy following incubation of murine spermatozoa with glutathione and either heparin, DS, or a combination of both. Ultrastructural changes taking place during decondensation were analyzed by transmission electron microscopy. Both glycosaminoglycans were able to promote the decondensation of murine spermatozoa in vitro but the decondensing ability of heparin was significantly higher. Use of both glycosaminoglycans together revealed the existence of a synergistic effect. Transmission electron microscopy analysis of decondensing spermatozoa supported these findings. Synergism between heparin and DS was observed both in capacitated and non-capacitated spermatozoa but decondensation kinetics was faster in the former. The results obtained indicate a new potential role for dermatan sulfate in murine sperm decondensation at fertilization and provide evidence of differences in the degree of chromatin condensation throughout the murine sperm nucleus. © 2013 Informa Healthcare USA, Inc.Fil:Julianelli, V.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Romanato, M. 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.Fil:Fontana, V.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2013info: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_19396368_v59_n2_p82_SanchezSyst. Biology Reprod. Med. 2013;59(2):82-90reponame: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/ar2025-09-04T09:48:24Zpaperaa:paper_19396368_v59_n2_p82_SanchezInstitucionalhttps://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 09:48:25.967Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse |
dc.title.none.fl_str_mv |
Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation |
title |
Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation |
spellingShingle |
Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation Sanchez, M.C. Chromatin decondensation Dermatan sulfate Heparin Murine spermatozoa Synergism dermatan sulfate glutathione glycosaminoglycan heparin animal cell article chromatin chromatin decondensation' controlled study dose response in vitro study male mouse nonhuman phase contrast microscopy priority journal spermatozoon transmission electron microscopy Animals Chromatin Dermatan Sulfate Dose-Response Relationship, Drug Heparin Male Mice Microscopy, Electron Spermatozoa |
title_short |
Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation |
title_full |
Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation |
title_fullStr |
Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation |
title_full_unstemmed |
Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation |
title_sort |
Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation |
dc.creator.none.fl_str_mv |
Sanchez, M.C. Alvarez Sedo, C. Julianelli, V.L. Romanato, M. Calvo, L. Calvo, J.C. Fontana, V.A. |
author |
Sanchez, M.C. |
author_facet |
Sanchez, M.C. Alvarez Sedo, C. Julianelli, V.L. Romanato, M. Calvo, L. Calvo, J.C. Fontana, V.A. |
author_role |
author |
author2 |
Alvarez Sedo, C. Julianelli, V.L. Romanato, M. Calvo, L. Calvo, J.C. Fontana, V.A. |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
Chromatin decondensation Dermatan sulfate Heparin Murine spermatozoa Synergism dermatan sulfate glutathione glycosaminoglycan heparin animal cell article chromatin chromatin decondensation' controlled study dose response in vitro study male mouse nonhuman phase contrast microscopy priority journal spermatozoon transmission electron microscopy Animals Chromatin Dermatan Sulfate Dose-Response Relationship, Drug Heparin Male Mice Microscopy, Electron Spermatozoa |
topic |
Chromatin decondensation Dermatan sulfate Heparin Murine spermatozoa Synergism dermatan sulfate glutathione glycosaminoglycan heparin animal cell article chromatin chromatin decondensation' controlled study dose response in vitro study male mouse nonhuman phase contrast microscopy priority journal spermatozoon transmission electron microscopy Animals Chromatin Dermatan Sulfate Dose-Response Relationship, Drug Heparin Male Mice Microscopy, Electron Spermatozoa |
dc.description.none.fl_txt_mv |
The mammalian sperm nucleus contains an unusually condensed chromatin, due to replacement of the majority of histones by protamines. However, soon after the spermatozoon penetrates the ooplasm at fertilization, decondensation of this densely packed chromatin must occur to allow formation of the male pronucleus and syngamy. Decondensation is accomplished by protamine disulfide bond reduction by oocyte glutathione and replacement of protamines by oocyte histones with the aid of an acceptor molecule. Previous results from our laboratory have demonstrated that heparan sulfate (HS) present in the ooplasm functions as protamine acceptor during human sperm decondensation in vivo. In the present paper, we analyze the role of heparin, structural analogue of HS, and dermatan sulfate (DS) in murine sperm chromatin decondensation in vitro, including the possibility of a synergistic effect between both glycosaminoglycans. Decondensation was assessed under phase contrast microscopy following incubation of murine spermatozoa with glutathione and either heparin, DS, or a combination of both. Ultrastructural changes taking place during decondensation were analyzed by transmission electron microscopy. Both glycosaminoglycans were able to promote the decondensation of murine spermatozoa in vitro but the decondensing ability of heparin was significantly higher. Use of both glycosaminoglycans together revealed the existence of a synergistic effect. Transmission electron microscopy analysis of decondensing spermatozoa supported these findings. Synergism between heparin and DS was observed both in capacitated and non-capacitated spermatozoa but decondensation kinetics was faster in the former. The results obtained indicate a new potential role for dermatan sulfate in murine sperm decondensation at fertilization and provide evidence of differences in the degree of chromatin condensation throughout the murine sperm nucleus. © 2013 Informa Healthcare USA, Inc. Fil:Julianelli, V.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Romanato, M. 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. Fil:Fontana, V.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. |
description |
The mammalian sperm nucleus contains an unusually condensed chromatin, due to replacement of the majority of histones by protamines. However, soon after the spermatozoon penetrates the ooplasm at fertilization, decondensation of this densely packed chromatin must occur to allow formation of the male pronucleus and syngamy. Decondensation is accomplished by protamine disulfide bond reduction by oocyte glutathione and replacement of protamines by oocyte histones with the aid of an acceptor molecule. Previous results from our laboratory have demonstrated that heparan sulfate (HS) present in the ooplasm functions as protamine acceptor during human sperm decondensation in vivo. In the present paper, we analyze the role of heparin, structural analogue of HS, and dermatan sulfate (DS) in murine sperm chromatin decondensation in vitro, including the possibility of a synergistic effect between both glycosaminoglycans. Decondensation was assessed under phase contrast microscopy following incubation of murine spermatozoa with glutathione and either heparin, DS, or a combination of both. Ultrastructural changes taking place during decondensation were analyzed by transmission electron microscopy. Both glycosaminoglycans were able to promote the decondensation of murine spermatozoa in vitro but the decondensing ability of heparin was significantly higher. Use of both glycosaminoglycans together revealed the existence of a synergistic effect. Transmission electron microscopy analysis of decondensing spermatozoa supported these findings. Synergism between heparin and DS was observed both in capacitated and non-capacitated spermatozoa but decondensation kinetics was faster in the former. The results obtained indicate a new potential role for dermatan sulfate in murine sperm decondensation at fertilization and provide evidence of differences in the degree of chromatin condensation throughout the murine sperm nucleus. © 2013 Informa Healthcare USA, Inc. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013 |
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_19396368_v59_n2_p82_Sanchez |
url |
http://hdl.handle.net/20.500.12110/paper_19396368_v59_n2_p82_Sanchez |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar |
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 |
Syst. Biology Reprod. Med. 2013;59(2):82-90 reponame:Biblioteca Digital (UBA-FCEN) instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales instacron:UBA-FCEN |
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repository.name.fl_str_mv |
Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
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