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
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_19396368_v59_n2_p82_Sanchez

id BDUBAFCEN_4e787681ade4002126fef77d2e4cd32a
oai_identifier_str paperaa:paper_19396368_v59_n2_p82_Sanchez
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling 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
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
_version_ 1842340702461100032
score 12.623145