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Article: Native human zona pellucida glycoproteins: Purification and binding properties

TitleNative human zona pellucida glycoproteins: Purification and binding properties
Authors
KeywordsAcrosome
Antibody
Glycoprotein
Spermatozoa
Zona pellucida
Issue Date2008
PublisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/
Citation
Human Reproduction, 2008, v. 23 n. 6, p. 1385-1393 How to Cite?
AbstractBACKGROUND: Fertilization starts with the binding of the spermatozoa to the zona pellucida (ZP) of the oocyte. Such binding is a carbohydrate-mediated event and consists of a series of tightly regulated events. Molecular interactions between spermatozoon and ZP in human are not well characterized due to limited availability of oocytes for research. Our current technology cannot generate recombinant human ZP (hZP) glycoproteins with native glycosylation. METHODS AND RESULTS: In this study, hZP glycoproteins, hZP2 (∼120 kDa), hZP3 (∼58 kDa) and hZP4 (∼65 kDa) were purified from ZP (purity >88%) by immunoaffinity columns. The binding sites of the purified native hZP3 and hZP4 were localized to the acrosome region of the capacitated human spermatozoa, and were lost after acrosome reaction. Purified human hZP2 bound to this region only in acrosome-reacted spermatozoa. Differential binding of the three glycoproteins to the post-acrosomal region and the midpiece of the spermatozoa was observed. In addition, hZP3, but not hZP2 and hZP4, induced hyperactivation. The stimulatory activity was dependent partly on N-linked glycosylation of hZP3. CONCLUSIONS: This manuscript describes the biological activities of purified hZP glycoproteins from the native source for the first time. © The Author 2008. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/87443
ISSN
2015 Impact Factor: 4.621
2015 SCImago Journal Rankings: 2.271
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChiu, PCNen_HK
dc.contributor.authorWong, BSTen_HK
dc.contributor.authorLee, CLen_HK
dc.contributor.authorPang, RTKen_HK
dc.contributor.authorLee, KFen_HK
dc.contributor.authorSumitro, SBen_HK
dc.contributor.authorGupta, SKen_HK
dc.contributor.authorYeung, WSBen_HK
dc.date.accessioned2010-09-06T09:29:43Z-
dc.date.available2010-09-06T09:29:43Z-
dc.date.issued2008en_HK
dc.identifier.citationHuman Reproduction, 2008, v. 23 n. 6, p. 1385-1393en_HK
dc.identifier.issn0268-1161en_HK
dc.identifier.urihttp://hdl.handle.net/10722/87443-
dc.description.abstractBACKGROUND: Fertilization starts with the binding of the spermatozoa to the zona pellucida (ZP) of the oocyte. Such binding is a carbohydrate-mediated event and consists of a series of tightly regulated events. Molecular interactions between spermatozoon and ZP in human are not well characterized due to limited availability of oocytes for research. Our current technology cannot generate recombinant human ZP (hZP) glycoproteins with native glycosylation. METHODS AND RESULTS: In this study, hZP glycoproteins, hZP2 (∼120 kDa), hZP3 (∼58 kDa) and hZP4 (∼65 kDa) were purified from ZP (purity >88%) by immunoaffinity columns. The binding sites of the purified native hZP3 and hZP4 were localized to the acrosome region of the capacitated human spermatozoa, and were lost after acrosome reaction. Purified human hZP2 bound to this region only in acrosome-reacted spermatozoa. Differential binding of the three glycoproteins to the post-acrosomal region and the midpiece of the spermatozoa was observed. In addition, hZP3, but not hZP2 and hZP4, induced hyperactivation. The stimulatory activity was dependent partly on N-linked glycosylation of hZP3. CONCLUSIONS: This manuscript describes the biological activities of purified hZP glycoproteins from the native source for the first time. © The Author 2008. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/en_HK
dc.relation.ispartofHuman Reproductionen_HK
dc.rightsHuman Reproduction. Copyright © Oxford University Press.en_HK
dc.subjectAcrosomeen_HK
dc.subjectAntibodyen_HK
dc.subjectGlycoproteinen_HK
dc.subjectSpermatozoaen_HK
dc.subjectZona pellucidaen_HK
dc.titleNative human zona pellucida glycoproteins: Purification and binding propertiesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0268-1161&volume=23&spage=1385&epage=&date=2008&atitle=Native+human+zona+pellucida+glycoproteins:+purification+and+binding+propertiesen_HK
dc.identifier.emailChiu, PCN: pchiucn@hku.hken_HK
dc.identifier.emailPang, RTK: rtkpang@hku.hken_HK
dc.identifier.emailLee, KF: ckflee@hku.hken_HK
dc.identifier.authorityChiu, PCN=rp00424en_HK
dc.identifier.authorityPang, RTK=rp01761en_HK
dc.identifier.authorityLee, KF=rp00458en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1093/humrep/den047en_HK
dc.identifier.pmid18332087-
dc.identifier.scopuseid_2-s2.0-44449178422en_HK
dc.identifier.hkuros144468en_HK
dc.identifier.hkuros171464-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-44449178422&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume23en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1385en_HK
dc.identifier.epage1393en_HK
dc.identifier.isiWOS:000256171000022-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridChiu, PCN=25959969200en_HK
dc.identifier.scopusauthoridWong, BST=24337009700en_HK
dc.identifier.scopusauthoridLee, CL=9277221100en_HK
dc.identifier.scopusauthoridPang, RTK=7004376636en_HK
dc.identifier.scopusauthoridLee, KF=26643097500en_HK
dc.identifier.scopusauthoridSumitro, SB=55218596400en_HK
dc.identifier.scopusauthoridGupta, SK=55495151900en_HK
dc.identifier.scopusauthoridYeung, WSB=55763794856en_HK
dc.identifier.citeulike2812916-

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