Sperm fucosyltransferase-5 mediates spermatozoa-oviductal epithelial cell interaction to protect human spermatozoa from oxidative damage

Oxidative damage by reactive oxygen species (ROS) is a major cause of sperm dysfunction. Excessive ROS generation reduces fertilization and enhances DNA damage of spermatozoa. Interaction between spermatozoa and oviductal epithelial cells improves the fertilizing ability of and reduces chromatin dam...

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Bibliographic Details
Published in:Molecular human reproduction 2015-06, Vol.21 (6), p.516-526
Main Authors: Huang, Venus Wenxin, Lee, Cheuk-Lun, Lee, Yin-Lau, Lam, Kevin K W, Ko, Jennifer K Y, Yeung, William S B, Ho, Pak-Chung, Chiu, Philip C N
Format: Article
Language:English
Subjects:
Cell Communication
Cryopreservation
DNA Fragmentation
Epithelial Cells - enzymology
Fallopian Tubes - enzymology
Female
Fucosyltransferases - physiology
Humans
Male
Oxidative Stress
Reactive Oxygen Species
Semen Preservation
Sperm Motility
Spermatozoa - cytology
Spermatozoa - enzymology
Spermatozoa - physiology
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Summary:Oxidative damage by reactive oxygen species (ROS) is a major cause of sperm dysfunction. Excessive ROS generation reduces fertilization and enhances DNA damage of spermatozoa. Interaction between spermatozoa and oviductal epithelial cells improves the fertilizing ability of and reduces chromatin damage in spermatozoa. Our previous data showed that oviductal epithelial cell membrane proteins interact with the human spermatozoa and protect them from ROS-induced reduction in sperm motility, membrane integrity and DNA integrity. Sperm fucosyltransferase-5 (sFUT5) is a membrane carbohydrate-binding protein on human spermatozoa. In this study, we demonstrate for the first time that sFUT5 is involved in human spermatozoa-oviduct interaction and the beneficial effects of such interaction on the fertilizing ability of human spermatozoa. Anti-sFUT5 antibody-treated spermatozoa had reduced binding to oviductal membrane proteins. It is consistent with the result that affinity-purified sFUT5 is bound to the epithelial lining of human oviduct and to the immortalized human oviductal epithelial cell line, OE-E6/E7. Pretreatment of spermatozoa with anti-sFUT5 antibody and oviductal membrane proteins with sFUT5 suppressed the protective action of oviductal membrane proteins against ROS/cryopreservation-induced oxidative damage in spermatozoa. Asialofetuin, a reported sFUT5 substrate, can partly mimic the protective effect of oviductal epithelial cell membrane proteins on sperm motility, membrane and DNA integrity. The results enhance our understanding on the protective mechanism of oviduct on sperm functions.
ISSN:1360-9947
1460-2407
DOI:10.1093/molehr/gav015