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Article: Effects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa
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TitleEffects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa
 
AuthorsChiu, PCN1
Wong, BST1
Chung, MK1
Lam, KKW1
Pang, RTK1
Lee, KF1
Sumitro, SB3
Gupta, SK2
Yeung, WSB1
 
KeywordsAcrosome reaction
Fertilization
Sperm
Zona pellucida
 
Issue Date2008
 
PublisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/
 
CitationBiology Of Reproduction, 2008, v. 79 n. 5, p. 869-877 [How to Cite?]
DOI: http://dx.doi.org/10.1095/biolreprod.108.069344
 
AbstractAcrosome reaction is crucial to the penetration of spermatozoa through the zona pellucida (ZP). Glycosylation of ZP glycoproteins is important in spermatozoa-ZP interaction. Human ZP glycoprotein-3 (ZP3) is believed to initiate acrosome reaction. Recently, human ZP4 was also implicated in inducing acrosome reaction. These studies were based on recombinant human ZP proteins with glycosylation different from their native counterparts. In the present study, the effects of native human ZP3 and ZP4 on acrosome reaction and spermatozoa-ZP binding were investigated. Native human ZP3 and ZP4 were immunoaffinity-purified. They induced acrosome reaction and inhibited spermatozoa-ZP binding time- and dose-dependently to different extents. These biological activities of human ZP3 and ZP4 depended partly on their glycosylation, with N-linked glycosylation contributing much more significantly than O-linked glycosylation. Studies with inhibitors showed that both human ZP3- and ZP4-induced acrosome reactions were protein kinase-C, protein tyrosine kinase, T-type Ca2+ channels, and extracellular Ca2+ dependent. G-protein also participated in human ZP3- but not in ZP4-induced acrosome reaction. On the other hand, protein kinase-A and L-type Ca 2+ channels took part only in human ZP4-induced acrosome reaction. This manuscript describes for the first time the actions of purified native human ZP3 and ZP4 on acrosome reaction and spermatozoa-ZP binding. © 2008 by the Society for the Study of Reproduction, Inc.
 
ISSN0006-3363
2013 Impact Factor: 3.451
 
DOIhttp://dx.doi.org/10.1095/biolreprod.108.069344
 
ISI Accession Number IDWOS:000260321300010
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorChiu, PCN
 
dc.contributor.authorWong, BST
 
dc.contributor.authorChung, MK
 
dc.contributor.authorLam, KKW
 
dc.contributor.authorPang, RTK
 
dc.contributor.authorLee, KF
 
dc.contributor.authorSumitro, SB
 
dc.contributor.authorGupta, SK
 
dc.contributor.authorYeung, WSB
 
dc.date.accessioned2010-05-31T04:09:45Z
 
dc.date.available2010-05-31T04:09:45Z
 
dc.date.issued2008
 
dc.description.abstractAcrosome reaction is crucial to the penetration of spermatozoa through the zona pellucida (ZP). Glycosylation of ZP glycoproteins is important in spermatozoa-ZP interaction. Human ZP glycoprotein-3 (ZP3) is believed to initiate acrosome reaction. Recently, human ZP4 was also implicated in inducing acrosome reaction. These studies were based on recombinant human ZP proteins with glycosylation different from their native counterparts. In the present study, the effects of native human ZP3 and ZP4 on acrosome reaction and spermatozoa-ZP binding were investigated. Native human ZP3 and ZP4 were immunoaffinity-purified. They induced acrosome reaction and inhibited spermatozoa-ZP binding time- and dose-dependently to different extents. These biological activities of human ZP3 and ZP4 depended partly on their glycosylation, with N-linked glycosylation contributing much more significantly than O-linked glycosylation. Studies with inhibitors showed that both human ZP3- and ZP4-induced acrosome reactions were protein kinase-C, protein tyrosine kinase, T-type Ca2+ channels, and extracellular Ca2+ dependent. G-protein also participated in human ZP3- but not in ZP4-induced acrosome reaction. On the other hand, protein kinase-A and L-type Ca 2+ channels took part only in human ZP4-induced acrosome reaction. This manuscript describes for the first time the actions of purified native human ZP3 and ZP4 on acrosome reaction and spermatozoa-ZP binding. © 2008 by the Society for the Study of Reproduction, Inc.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationBiology Of Reproduction, 2008, v. 79 n. 5, p. 869-877 [How to Cite?]
DOI: http://dx.doi.org/10.1095/biolreprod.108.069344
 
dc.identifier.citeulike3181284
 
dc.identifier.doihttp://dx.doi.org/10.1095/biolreprod.108.069344
 
dc.identifier.epage877
 
dc.identifier.hkuros154738
 
dc.identifier.isiWOS:000260321300010
 
dc.identifier.issn0006-3363
2013 Impact Factor: 3.451
 
dc.identifier.issue5
 
dc.identifier.openurl
 
dc.identifier.pmid18667750
 
dc.identifier.scopuseid_2-s2.0-55549122993
 
dc.identifier.spage869
 
dc.identifier.urihttp://hdl.handle.net/10722/60394
 
dc.identifier.volume79
 
dc.languageeng
 
dc.publisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofBiology of Reproduction
 
dc.relation.referencesReferences in Scopus
 
dc.subjectAcrosome reaction
 
dc.subjectFertilization
 
dc.subjectSperm
 
dc.subjectZona pellucida
 
dc.titleEffects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. National Institute of Immunology India
  3. Brawijaya University