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Immunolocalization and quantitation of acidic seminal fluid protein (aSFP) in ejaculated, swim-up, and capacitated bull spermatozoa.

Authors
Type
Published Article
Journal
Biological chemistry Hoppe-Seyler
Publication Date
Volume
375
Issue
7
Pages
457–461
Identifiers
PMID: 7945995
Source
Medline
License
Unknown

Abstract

Acidic seminal fluid protein (aSFP, 12.9 kDa), a major protein of bull seminal plasma, belongs to the spermadhesin protein family. Boar spermadhesins become bound to the sperm head's surface at ejaculation and are thought to play a role as capacitation factors and/or in gamete recognition and binding. Here, we have investigated the topographical distribution and fate of bovine spermadhesin aSFP during sperm capacitation in order to assess whether aSFP could be involved in similar aspects of the fertilization process as its boar homologous proteins. 5.7 +/- 2.1 x 10(6) molecules/spermatozoa were quantitated on the surface of fresh ejaculated and washed sperm. The binding site of aSFP was restricted to a thin coat at the apical part of the acrosomal cap. The amount of aSFP in swim-up sperm was 1.8 +/- 1.0 x 10(6) molecules/spermatozoa, but decreased dramatically to 22 +/- 10 x 10(3) and to undetectable levels after incubation of sperm for 1.5 h and 18 h, respectively, in capacitation medium. This indicates that the bull spermatozoa surface may be completely depleted of spermadhesin aSFP before spermatozoa reach the surroundings of the investing egg. Therefore, our results suggest that aSFP may act as a decapacitation factor on bull spermatozoa rather than as a zona pellucida binding molecule.

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