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Article: The role of galectin-3 in spermatozoa-zona pellucida binding and its association with fertilization in vitro

TitleThe role of galectin-3 in spermatozoa-zona pellucida binding and its association with fertilization in vitro
Authors
KeywordsCapacitation
Extracellular vesicles
Fertilization
Galectin-3
Human spermatozoa
Issue Date2019
PublisherOxford University Press. The Journal's web site is located at http://molehr.oxfordjournals.org/
Citation
Molecular Human Reproduction, 2019, v. 25 n. 8, p. 458-470 How to Cite?
AbstractHuman spermatozoa can fertilize an oocyte only after post-testicular maturation and capacitation. These processes involve dynamic modification and reorganization of the sperm plasma membrane, which allow them to bind to the zona pellucida (ZP) of the oocyte. Defective sperm-ZP binding is one of the major causes of male subfertility. Galectin-3 is a secretory lectin in human seminal plasma well known for its action on cell adhesion. The aim of this study was to determine the role of galectin-3 in spermatozoa-ZP interaction and its association with fertilization rate in clinical assisted reproduction. Our studies revealed that the acrosomal region of ejaculated and capacitated spermatozoa possess strong galectin-3 immunoreactivity, which is much stronger than that of epididymal spermatozoa. Expression of galectin-3 can also be detected on seminal plasma-derived extracellular vesicles (EVs) and can be transferred to the sperm surface. Blocking of sperm surface galectin-3 function by antibody or carbohydrate substrate reduced the ZP-binding capacity of spermatozoa. Purified galectin-3 is capable of binding to ZP, indicating that galectin-3 may serve as a cross-linking bridge between ZP glycans and sperm surface glycoproteins. Galectin-3 levels in seminal plasma-derived EVs were positively associated with fertilization rates. These results suggest that galectin-3 in EVs is transferred to the sperm surface during post-testicular maturation and plays a crucial role in spermatozoa-ZP binding after capacitation. Reduced galectin-3 expression in seminal plasma-derived EVs may be a cause behind a low fertilization rate. Further studies with more clinical samples are required to confirm the relationship between galectin-3 levels and IVF outcomes.
Persistent Identifierhttp://hdl.handle.net/10722/288205
ISSN
2018 Impact Factor: 3.396
2015 SCImago Journal Rankings: 1.611
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMEI, S-
dc.contributor.authorChen, P-
dc.contributor.authorLee, CL-
dc.contributor.authorZhao, W-
dc.contributor.authorWang, Y-
dc.contributor.authorLam, KKW-
dc.contributor.authorHo, PC-
dc.contributor.authorYeung, WSB-
dc.contributor.authorFang, C-
dc.contributor.authorChiu, PCN-
dc.date.accessioned2020-10-05T12:09:24Z-
dc.date.available2020-10-05T12:09:24Z-
dc.date.issued2019-
dc.identifier.citationMolecular Human Reproduction, 2019, v. 25 n. 8, p. 458-470-
dc.identifier.issn1360-9947-
dc.identifier.urihttp://hdl.handle.net/10722/288205-
dc.description.abstractHuman spermatozoa can fertilize an oocyte only after post-testicular maturation and capacitation. These processes involve dynamic modification and reorganization of the sperm plasma membrane, which allow them to bind to the zona pellucida (ZP) of the oocyte. Defective sperm-ZP binding is one of the major causes of male subfertility. Galectin-3 is a secretory lectin in human seminal plasma well known for its action on cell adhesion. The aim of this study was to determine the role of galectin-3 in spermatozoa-ZP interaction and its association with fertilization rate in clinical assisted reproduction. Our studies revealed that the acrosomal region of ejaculated and capacitated spermatozoa possess strong galectin-3 immunoreactivity, which is much stronger than that of epididymal spermatozoa. Expression of galectin-3 can also be detected on seminal plasma-derived extracellular vesicles (EVs) and can be transferred to the sperm surface. Blocking of sperm surface galectin-3 function by antibody or carbohydrate substrate reduced the ZP-binding capacity of spermatozoa. Purified galectin-3 is capable of binding to ZP, indicating that galectin-3 may serve as a cross-linking bridge between ZP glycans and sperm surface glycoproteins. Galectin-3 levels in seminal plasma-derived EVs were positively associated with fertilization rates. These results suggest that galectin-3 in EVs is transferred to the sperm surface during post-testicular maturation and plays a crucial role in spermatozoa-ZP binding after capacitation. Reduced galectin-3 expression in seminal plasma-derived EVs may be a cause behind a low fertilization rate. Further studies with more clinical samples are required to confirm the relationship between galectin-3 levels and IVF outcomes.-
dc.languageeng-
dc.publisherOxford University Press. The Journal's web site is located at http://molehr.oxfordjournals.org/-
dc.relation.ispartofMolecular Human Reproduction-
dc.rightsPre-print: Journal Title] ©: [year] [owner as specified on the article] Published by Oxford University Press [on behalf of xxxxxx]. All rights reserved. Pre-print (Once an article is published, preprint notice should be amended to): This is an electronic version of an article published in [include the complete citation information for the final version of the Article as published in the print edition of the Journal.] Post-print: This is a pre-copy-editing, author-produced PDF of an article accepted for publication in [insert journal title] following peer review. The definitive publisher-authenticated version [insert complete citation information here] is available online at: xxxxxxx [insert URL that the author will receive upon publication here].-
dc.subjectCapacitation-
dc.subjectExtracellular vesicles-
dc.subjectFertilization-
dc.subjectGalectin-3-
dc.subjectHuman spermatozoa-
dc.titleThe role of galectin-3 in spermatozoa-zona pellucida binding and its association with fertilization in vitro-
dc.typeArticle-
dc.identifier.emailLee, CL: kcllee@hku.hk-
dc.identifier.emailLam, KKW: kkwlam@hku.hk-
dc.identifier.emailHo, PC: pcho@hku.hk-
dc.identifier.emailYeung, WSB: wsbyeung@hku.hk-
dc.identifier.emailChiu, PCN: pchiucn@hku.hk-
dc.identifier.authorityLee, CL=rp02515-
dc.identifier.authorityHo, PC=rp00325-
dc.identifier.authorityYeung, WSB=rp00331-
dc.identifier.authorityChiu, PCN=rp00424-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1093/molehr/gaz030-
dc.identifier.pmid31194867-
dc.identifier.scopuseid_2-s2.0-85072058912-
dc.identifier.scopuseid_2-s2.0-85072058912-
dc.identifier.hkuros314955-
dc.identifier.volume25-
dc.identifier.issue8-
dc.identifier.spage458-
dc.identifier.epage470-
dc.identifier.isiWOS:000493181200004-
dc.publisher.placeUnited Kingdom-
dc.identifier.issnl1360-9947-

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