[Androgen-dependent protein secreted by mouse caput epididymis shows high homologies with different glutathione peroxidases].
Principal cells of the mouse caput epididymidis synthesize and secrete a 24 kDa protein able to bind to the head of the spermatozoa. Sequencing of several clones selected from cDNA and genomic libraries, combined with the microsequencing of the NH2 terminus of the protein allowed to reconstitute the entire primary structure of the mature 24 kDa protein. It revealed 81% homology with a human plasma glutathione peroxidase and 61% homology with a mouse erythrocyte glutathione peroxidase. This enzyme, once secreted in the epididymal fluid, might protect sperm membrane lipids, particularly those of the acrosomal part, against peroxidation.
Ghyselinck
N B
NB
Laboratoire de Biologie cellulaire, Université Blaise-Pascal, Aubière.
Rigaudière
N
N
Dufaure
J P
JP
D000728:Androgens / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D004822:Epididymis / Q000737:chemistry* / Q000378:metabolism; D015698:Genomic Library; D005979:Glutathione Peroxidase / Q000097:blood / Q000737:chemistry*; D006801:Humans; D008297:Male; D051379:Mice; D010443:Peptide Chain Termination, Translational; D016415:Sequence Alignment
D000728:Androgens; D005979:Glutathione Peroxidase
Une protéine androgéno-dépendante sécrétée par la tête de l'épididyme de souris présente des homologies élevées avec différentes glutathion peroxydases.