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The incorporation of cystine by the soluble carrier family 7 member 11 (SLC7A11) is a component of the redox regulatory mechanism in stallion spermatozoa
Univ Extremadura, Spain.
Univ Extremadura, Spain.
Univ Extremadura, Spain.
Univ Extremadura, Spain.
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2019 (English)In: Biology of Reproduction, ISSN 0006-3363, E-ISSN 1529-7268, Vol. 101, no 1, p. 208-222Article in journal (Refereed) Published
Abstract [en]

Oxidative stress is considered amajor mechanism causing sperm damage during cryopreservation and storage, and underlies male factor infertility. Currently, oxidative stress is no longer believed to be caused only by the overproduction of reactive oxygen species, but rather by the deregulation of redox signaling and control mechanisms. With this concept in mind, here, we describe for the first time the presence of the soluble carrier family 7 member 11 (SLC7A11) antiporter, which exchanges extracellular cystine (Cyss) for intracellular glutamate, in stallion spermatozoa, as well as its impact on sperm function using the specific inhibitor sulfasalazine. Spermatozoa incubated with Cyss exhibited an increased intracellular GSH content compared with controls (P amp;lt; 0.01): 50% in fresh extended stallion spermatozoa and 30% in frozen-thawed spermatozoa. This effect was prevented by the addition of sulfasalazine to the media. Cystine supplementation also reduced the oxidation-reduction potential of spermatozoa, with sulfasalazine only preventing this effect on fresh spermatozoa that were incubated for 3 h at 37 degrees C, but not in frozen-thawed spermatozoa. While sulfasalazine reduced the motility of frozen-thawed spermatozoa, it increased motility in fresh samples. The present findings provide new and relevant data on the mechanism regulating the redox status of spermatozoa and suggest that a different redox regulatory mechanism exists in cryopreserved spermatozoa, thus providing new clues to improve current cryopreservation technologies and treat male factor infertility. Summary Sentence The SLC7A11 antiporter that exchanges cystine by intracellular glutamate is present and functional in stallion spermatozoa, but cryopreserved spermatozoa may present altered functionality.

Place, publisher, year, edition, pages
OXFORD UNIV PRESS INC , 2019. Vol. 101, no 1, p. 208-222
Keywords [en]
stallion; spermatozoa; GSH; flow cytometry; cysteine; cystine; oxidation; reduction
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:liu:diva-162085DOI: 10.1093/biolre/ioz069ISI: 000492974800018PubMedID: 30998234OAI: oai:DiVA.org:liu-162085DiVA, id: diva2:1371320
Note

Funding Agencies|Ministerio de Economia y CompetitividadEuropean Regional Development Fund (FEDER), Madrid, Spain [AGL2017-83149-R]; Junta de Extremadura-FEDEREuropean Union (EU) [IB16030, GR18008]; Swedish Research councils VRSwedish Research Council [521-2011-6553]; FORMAS, StockholmSwedish Research Council Formas [2017-00946]; Valhondo Calaaf Foundation, Caceres, Spain

Available from: 2019-11-19 Created: 2019-11-19 Last updated: 2019-11-19

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Rodriguez-Martinez, Heriberto
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Division of Children's and Women's healthFaculty of Medicine and Health Sciences
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Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

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