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Adhesion to oviduct glycans regulates porcine sperm Ca(2+) influx and viability

Before fertilization, sperm bind to epithelial cells of the oviduct isthmus to form a reservoir that regulates sperm viability and capacitation. The sperm reservoir maintains optimum fertility in species, like swine, in which semen deposition and ovulation may not be well synchronized. We demonstrat...

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Autores principales: Machado, Sergio A., Sharif, Momal, Kadirvel, Govindasamy, Bovin, Nicolai, Miller, David J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7442259/
https://www.ncbi.nlm.nih.gov/pubmed/32822385
http://dx.doi.org/10.1371/journal.pone.0237666
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author Machado, Sergio A.
Sharif, Momal
Kadirvel, Govindasamy
Bovin, Nicolai
Miller, David J.
author_facet Machado, Sergio A.
Sharif, Momal
Kadirvel, Govindasamy
Bovin, Nicolai
Miller, David J.
author_sort Machado, Sergio A.
collection PubMed
description Before fertilization, sperm bind to epithelial cells of the oviduct isthmus to form a reservoir that regulates sperm viability and capacitation. The sperm reservoir maintains optimum fertility in species, like swine, in which semen deposition and ovulation may not be well synchronized. We demonstrated previously that porcine sperm bind to two oviductal glycan motifs, a biantennary 6-sialylated N-acetyllactosamine (bi-SiaLN) oligosaccharide and 3-O-sulfated Lewis X trisaccharide (suLe(X)). Here, we assessed the ability of these glycans to regulate sperm Ca(2+) influx, capacitation and affect sperm lifespan. After 24 h, the viability of sperm bound to immobilized bi-SiaLN and suLe(X) was higher (46% and 41% respectively) compared to viability of free-swimming sperm (10–12%). Ca(2+) is a central regulator of sperm function so we assessed whether oviduct glycans could affect the Ca(2+) influx that occurs during capacitation. Using a fluorescent intracellular Ca(2+) probe, we observed that both oviduct glycans suppressed the Ca(2+) increase that occurs during capacitation. Thus, specific oviduct glycans can regulate intracellular Ca(2+). Because the increase in intracellular Ca(2+) was suppressed by oviduct glycans, we examined whether glycans affected capacitation, as determined by protein tyrosine phosphorylation and the ability to undergo a Ca(2+) ionophore-induced acrosome reaction. We found no discernable suppression of capacitation in sperm bound to oviduct glycans. We also detected no effect of oviduct glycans on sperm motility during capacitation. In summary, Le(X) and bi-SiaLN glycan motifs found on oviduct oligosaccharides suppress the Ca(2+) influx that occurs during capacitation and extend sperm lifespan but do not affect sperm capacitation or motility.
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spelling pubmed-74422592020-08-26 Adhesion to oviduct glycans regulates porcine sperm Ca(2+) influx and viability Machado, Sergio A. Sharif, Momal Kadirvel, Govindasamy Bovin, Nicolai Miller, David J. PLoS One Research Article Before fertilization, sperm bind to epithelial cells of the oviduct isthmus to form a reservoir that regulates sperm viability and capacitation. The sperm reservoir maintains optimum fertility in species, like swine, in which semen deposition and ovulation may not be well synchronized. We demonstrated previously that porcine sperm bind to two oviductal glycan motifs, a biantennary 6-sialylated N-acetyllactosamine (bi-SiaLN) oligosaccharide and 3-O-sulfated Lewis X trisaccharide (suLe(X)). Here, we assessed the ability of these glycans to regulate sperm Ca(2+) influx, capacitation and affect sperm lifespan. After 24 h, the viability of sperm bound to immobilized bi-SiaLN and suLe(X) was higher (46% and 41% respectively) compared to viability of free-swimming sperm (10–12%). Ca(2+) is a central regulator of sperm function so we assessed whether oviduct glycans could affect the Ca(2+) influx that occurs during capacitation. Using a fluorescent intracellular Ca(2+) probe, we observed that both oviduct glycans suppressed the Ca(2+) increase that occurs during capacitation. Thus, specific oviduct glycans can regulate intracellular Ca(2+). Because the increase in intracellular Ca(2+) was suppressed by oviduct glycans, we examined whether glycans affected capacitation, as determined by protein tyrosine phosphorylation and the ability to undergo a Ca(2+) ionophore-induced acrosome reaction. We found no discernable suppression of capacitation in sperm bound to oviduct glycans. We also detected no effect of oviduct glycans on sperm motility during capacitation. In summary, Le(X) and bi-SiaLN glycan motifs found on oviduct oligosaccharides suppress the Ca(2+) influx that occurs during capacitation and extend sperm lifespan but do not affect sperm capacitation or motility. Public Library of Science 2020-08-21 /pmc/articles/PMC7442259/ /pubmed/32822385 http://dx.doi.org/10.1371/journal.pone.0237666 Text en © 2020 Machado et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Machado, Sergio A.
Sharif, Momal
Kadirvel, Govindasamy
Bovin, Nicolai
Miller, David J.
Adhesion to oviduct glycans regulates porcine sperm Ca(2+) influx and viability
title Adhesion to oviduct glycans regulates porcine sperm Ca(2+) influx and viability
title_full Adhesion to oviduct glycans regulates porcine sperm Ca(2+) influx and viability
title_fullStr Adhesion to oviduct glycans regulates porcine sperm Ca(2+) influx and viability
title_full_unstemmed Adhesion to oviduct glycans regulates porcine sperm Ca(2+) influx and viability
title_short Adhesion to oviduct glycans regulates porcine sperm Ca(2+) influx and viability
title_sort adhesion to oviduct glycans regulates porcine sperm ca(2+) influx and viability
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7442259/
https://www.ncbi.nlm.nih.gov/pubmed/32822385
http://dx.doi.org/10.1371/journal.pone.0237666
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