β 2-Inhibin contains the active core of human seminal plasma β-inhibin: synthesis and bioactivity

• Published in: FEBS letters 1985-02, Vol.181 (1), p.57-63
• Main Authors: Arbatti, N.J., Seidah, N.G., Rochemont, J., Escher, E., Sheth, A.R., Chrétien, M.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Chemical synthesis; Chromatography, High Pressure Liquid; Follicle Stimulating Hormone - metabolism; Gonadotropin-Releasing Hormone - pharmacology; Human seminal plasma; Humans; Inhibins; Luteinizing Hormone - metabolism; Peptide Fragments; Peptides - chemical synthesis; Peptides - pharmacology; Pituitary FSH release; Pituitary Gland - drug effects; Prostatic Secretory Proteins; Semen - analysis; β 2-Inhibin
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(85)81113-3

The complete synthesis of the C-terminal 28 residues segment 67–94 of human seminal plasma jS-Inhibin, called β 2-Inhibin, is reported. The Inhibin-like activity of the native 94 amino acids β-Inhibin is compared to that of the synthetic replica of β 2-Inhibin. In all assays used both peptides effectively suppress the FSH release induced by LHRH but have little effect on the LH release. In the mouse both peptides are equipotent on a mole basis. In the rat the synthetic β 2-Inhibin is 3–10 times more potent than β-Inhibin. Both peptides are active in rat anterior pituitary primary culture assays where maximum suppression of FSH release induced by LHRH occurs around 300 pmol ml of β 2-Inhibin. In contrast, maximum suppression of FSH release in the mouse pituitary assay occurs at 10–15 pmol ml of either Inhibin.