title: Fertilization-promoting peptide in reproductive tissues and semen of the male marmoset (Callithrix jacchus).
abstract: Fertilization-promoting peptide (FPP) is present in the prostate gland and semen of some mammals, and has been shown to enhance the fertilizing ability of both epididymal mouse and ejaculated human spermatozoa. The novel peptide may prove of importance for the treatment of some cases of male infertility, and a suitable animal model would be useful to test this hypothesis. To this end, we examined reproductive tissues and semen of the male marmoset for the presence of FPP. Peptides were extracted from seminal plasma, testes, prostate, and bulbourethral glands of intact and castrated male marmosets. The peptides were identified by ion-exchange chromatography followed by radioimmunoassay. The mean concentration of FPP immunoreactivity in semen from intact males was 58.7 nM (SE +/- 9.9 nM, n = 10), and anion-exchange chromatography revealed FPP as the only immunoreactive peptide present. Analysis of tissues revealed that FPP in semen was likely to be derived from the prostate gland, which contained this peptide as the major source of immunoreactivity (10.86 pmol/gland; SE +/- 4.39 pmol/gland, n = 4). Only low concentrations of FPP were detectable in the bulbourethral glands, and the peptide was undetectable in the testis. Surprisingly, FPP was readily detectable in the seminal plasma from one castrated marmoset and was present in the prostate gland from 3 castrates at levels which did not differ significantly from those in intact animals (5.47 pmol/gland, SE +/- 1.64 pmol/gland, n = 3). Plasma testosterone measurements indicated that residual circulatory androgens remained after castration, which may be consistent both with the maintenance of mating behavior and the presence of prostatic FPP. We conclude that FPP is present within the prostate gland and seminal plasma of the marmoset at concentrations consistent with a role in male fertility in this species.
authors.affiliation: School of Animal and Microbial Sciences, University of Reading, UK.
authors.forename: A M
authors.initials: AM
authors.lastname: Kennedy
authors.forename: J M
authors.initials: JM
authors.lastname: Morrell
authors.forename: R J
authors.initials: RJ
authors.lastname: Siviter
authors.forename: S M
authors.initials: SM
authors.lastname: Cockle
mesh_terms: D000818:Animals; D002030:Bulbourethral Glands / Q000737:chemistry; D002144:Callithrix / Q000378:metabolism*; D002369:Castration; D002852:Chromatography, Ion Exchange; D008297:Male; D000085822:Prolyl Oligopeptidases; D011467:Prostate / Q000737:chemistry*; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives; D011863:Radioimmunoassay; D012661:Semen / Q000737:chemistry* / Q000201:enzymology; D012697:Serine Endopeptidases / Q000378:metabolism; D013737:Testis / Q000737:chemistry; D013739:Testosterone / Q000097:blood; D013973:Thyrotropin-Releasing Hormone / Q000031:analogs & derivatives* / Q000032:analysis / Q000302:isolation & purification / Q000627:therapeutic use
chemical_list: D013739:Testosterone; D013973:Thyrotropin-Releasing Hormone; C059697:pyroglutamyl-glutamyl-proline amide; D012697:Serine Endopeptidases; C000705287:PREPL protein, human; D000085822:Prolyl Oligopeptidases; D011761:Pyrrolidonecarboxylic Acid