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Combined albumin and bicarbonate induces head-to-head sperm agglutination which physically prevents equine sperm-oviduct binding

(2016) REPRODUCTION. 151(4). p.313-330
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Abstract
In many species, sperm binding to oviduct epithelium is believed to be an essential step in generating a highly fertile capacitated sperm population primed for fertilization. In several mammalian species, this interaction is based on carbohydrate-lectin recognition. D-galactose has previously been characterized as a key molecule that facilitates sperm-oviduct binding in the horse. We used oviduct explant and oviduct apical plasma membrane (APM) assays to investigate the effects of various carbohydrates; glycosaminoglycans; lectins; S-S reductants; and the capacitating factors albumin, Ca2+ and HCO3- on sperm-oviduct binding in the horse. Carbohydrate-specific lectin staining indicated that N-acetylgalactosamine, N-acetylneuraminic acid (sialic acid) and D-mannose or D-glucose were the most abundant carbohydrates on equine oviduct epithelia, whereas D-galactose moieties were not detected. However, in a competitive binding assay, sperm-oviduct binding density was not influenced by any tested carbohydrates, glycosaminoglycans, lectins or D-penicillamine, nor did the glycosaminoglycans induce sperm tail-associated protein tyrosine phosphorylation. Furthermore, N-glycosidase F (PNGase) pretreatment of oviduct explants and APM did not alter sperm-oviduct binding density. By contrast, a combination of the sperm-capacitating factors albumin and HCO3- severely reduced (>10-fold) equine sperm-oviduct binding density by inducing rapid head-to-head agglutination, both of which events were independent of Ca2+ and an elevated pH (7.9). Conversely, neither albumin and HCO3- nor any other capacitating factor could induce release of oviduct-bound sperm. In conclusion, a combination of albumin and HCO3- markedly induced sperm head-to-head agglutination which physically prevented stallion sperm to bind to oviduct epithelium.
Keywords
sperm-oviduct binding, bicarbonate, albumin, carbohydrates, equine, BULL SPERM, ANTI-AGGLUTININ, STALLION SPERM, EPITHELIAL-CELLS, BOVINE SPERM, APICAL PLASMA-MEMBRANES, EJACULATED BOAR SPERMATOZOA, INTRACELLULAR CALCIUM-CONCENTRATION, CELLS IN-VITRO, PROTEIN-TYROSINE PHOSPHORYLATION

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Citation

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Chicago
Leemans, Bart, Bart M Gadella, Tom AE Stout, Edita Sostaric, Catharina De Schauwer, Hilde Nelis, Maarten Hoogewijs, and Ann Van Soom. 2016. “Combined Albumin and Bicarbonate Induces Head-to-head Sperm Agglutination Which Physically Prevents Equine Sperm-oviduct Binding.” Reproduction 151 (4): 313–330.
APA
Leemans, B., Gadella, B. M., Stout, T. A., Sostaric, E., De Schauwer, C., Nelis, H., Hoogewijs, M., et al. (2016). Combined albumin and bicarbonate induces head-to-head sperm agglutination which physically prevents equine sperm-oviduct binding. REPRODUCTION, 151(4), 313–330.
Vancouver
1.
Leemans B, Gadella BM, Stout TA, Sostaric E, De Schauwer C, Nelis H, et al. Combined albumin and bicarbonate induces head-to-head sperm agglutination which physically prevents equine sperm-oviduct binding. REPRODUCTION. 2016;151(4):313–30.
MLA
Leemans, Bart, Bart M Gadella, Tom AE Stout, et al. “Combined Albumin and Bicarbonate Induces Head-to-head Sperm Agglutination Which Physically Prevents Equine Sperm-oviduct Binding.” REPRODUCTION 151.4 (2016): 313–330. Print.
@article{7035798,
  abstract     = {In many species, sperm binding to oviduct epithelium is believed to be an essential step in generating a highly fertile capacitated sperm population primed for fertilization. In several mammalian species, this interaction is based on carbohydrate-lectin recognition. D-galactose has previously been characterized as a key molecule that facilitates sperm-oviduct binding in the horse. We used oviduct explant and oviduct apical plasma membrane (APM) assays to investigate the effects of various carbohydrates; glycosaminoglycans; lectins; S-S reductants; and the capacitating factors albumin, Ca2+ and HCO3- on sperm-oviduct binding in the horse. Carbohydrate-specific lectin staining indicated that N-acetylgalactosamine, N-acetylneuraminic acid (sialic acid) and D-mannose or D-glucose were the most abundant carbohydrates on equine oviduct epithelia, whereas D-galactose moieties were not detected. However, in a competitive binding assay, sperm-oviduct binding density was not influenced by any tested carbohydrates, glycosaminoglycans, lectins or D-penicillamine, nor did the glycosaminoglycans induce sperm tail-associated protein tyrosine phosphorylation. Furthermore, N-glycosidase F (PNGase) pretreatment of oviduct explants and APM did not alter sperm-oviduct binding density. By contrast, a combination of the sperm-capacitating factors albumin and HCO3- severely reduced ({\textrangle}10-fold) equine sperm-oviduct binding density by inducing rapid head-to-head agglutination, both of which events were independent of Ca2+ and an elevated pH (7.9). Conversely, neither albumin and HCO3- nor any other capacitating factor could induce release of oviduct-bound sperm. In conclusion, a combination of albumin and HCO3- markedly induced sperm head-to-head agglutination which physically prevented stallion sperm to bind to oviduct epithelium.},
  author       = {Leemans, Bart and Gadella, Bart M and Stout, Tom AE and Sostaric, Edita and De Schauwer, Catharina and Nelis, Hilde and Hoogewijs, Maarten and Van Soom, Ann},
  issn         = {1470-1626},
  journal      = {REPRODUCTION},
  keyword      = {sperm-oviduct binding,bicarbonate,albumin,carbohydrates,equine,BULL SPERM,ANTI-AGGLUTININ,STALLION SPERM,EPITHELIAL-CELLS,BOVINE SPERM,APICAL PLASMA-MEMBRANES,EJACULATED BOAR SPERMATOZOA,INTRACELLULAR CALCIUM-CONCENTRATION,CELLS IN-VITRO,PROTEIN-TYROSINE PHOSPHORYLATION},
  language     = {eng},
  number       = {4},
  pages        = {313--330},
  title        = {Combined albumin and bicarbonate induces head-to-head sperm agglutination which physically prevents equine sperm-oviduct binding},
  url          = {http://dx.doi.org/10.1530/REP-15-0471},
  volume       = {151},
  year         = {2016},
}

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