C. Gaudreault et al., Hamster sperm protein, P26h: A member of the short-chain dehydrogenase reductase superfamily, BIOL REPROD, 61(1), 1999, pp. 264-273
For successful fertilization to occur,mammalian spermatozoa must undergo a
series of modifications in order to reach and penetrate the oocyte. Some of
these modifications occur during passage through the epididymis, the site
where spermatozoa acquire their fertilizing ability. We have previously des
cribed hamster sperm protein, P26h, which is acquired by spermatozoa during
epididymal transit, and have proposed that this protein is involved in spe
rm-egg binding. In the present study, we report the cloning and characteriz
ation of the full-length cDNA encoding hamster P26h. A database search usin
g the predicted hamster P26h amino acid sequence revealed 85% identity with
mouse AP27 protein and porcine carbonyl reductase, members of the short-ch
ain dehydrogenase/reductase (SDR) family of proteins. Northern blot analysi
s revealed a major P26h 1-kilobase transcript in the testis. No signal was
detected in other somatic tissues of the hamster. In situ hybridization exp
eriments revealed that the P26h gene was predominantly transcribed in semin
iferous tubules of the testis and at a lower level in the corpus epididymid
is. The identity of the cloned P26h was confirmed by immunoprecipitating in
vitro-translated P26h using polyclonal antiserum raised against purified h
amster sperm P26h. Taken together, these results identify P26h as a new mem
ber of the SDR family of proteins involved in the processes of mammalian ga
mete interactions.