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Polysialic acid is present in mammalian semen as a post-translational modification of the neural cell adhesion molecule NCAM and the polysialyltransferase ST8SiaII.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2013 Jun 28; Vol. 288 (26), pp. 18825-33. Date of Electronic Publication: 2013 May 13. - Publication Year :
- 2013
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Abstract
- Fertilization in animals is a complex sequence of several biochemical events beginning with the insemination into the female reproductive tract and, finally, leading to embryogenesis. Studies by Kitajima and co-workers (Miyata, S., Sato, C., and Kitajima, K. (2007) Trends Glycosci. Glyc, 19, 85-98) demonstrated the presence of polysialic acid (polySia) on sea urchin sperm. Based on these results, we became interested in the potential involvement of sialic acid polymers in mammalian fertilization. Therefore, we isolated human sperm and performed analyses, including Western blotting and mild 1,2-diamino-4,5-methylenedioxybenzene-HPLC, that revealed the presence α2,8-linked polySia chains. Further analysis by a glyco-proteomics approach led to the identification of two polySia carriers. Interestingly, besides the neural cell adhesion molecule, the polysialyltransferase ST8SiaII has also been found to be a target for polysialylation. Further analysis of testis and epididymis tissue sections demonstrated that only epithelial cells of the caput were polySia-positive. During the epididymal transit, polySia carriers were partially integrated into the sperm membrane of the postacrosomal region. Because polySia is known to counteract histone as well as neutrophil extracellular trap-mediated cytotoxicity against host cells, which plays a role after insemination, we propose that polySia in semen represents a cytoprotective element to increase the number of vital sperm.
- Subjects :
- Amino Acid Motifs
Animals
Chromatography, High Pressure Liquid
Epididymis metabolism
Female
Fertilization
Humans
Male
Mice
Microscopy, Fluorescence
Proteomics methods
Rats
Spermatozoa metabolism
Neural Cell Adhesion Molecules metabolism
Protein Processing, Post-Translational
Semen metabolism
Sialic Acids metabolism
Sialyltransferases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 288
- Issue :
- 26
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 23671285
- Full Text :
- https://doi.org/10.1074/jbc.M113.451112