Dl. Russell et Jk. Findlay, THE N-TERMINAL PEPTIDE OF THE INHIBIN ALPHA-SUBUNIT - WHAT ARE ITS ENDOCRINE AND PARACRINE ROLES, Trends in endocrinology and metabolism, 6(9-10), 1995, pp. 305-311
alpha N inhibin (molecular mass 23/24 kD) is present in the pro-alpha
N-alpha C subunit of inhibin and can be released by cleavage at the fl
anking arginine residues during posttranslational processing. Although
the alpha N protein isolated from bovine follicular fluid has no inhi
binlike (FSH suppressing) activity, alpha N is present in high molecul
ar weight forms of biologically active inhibin found in follicular flu
id and plasma. alpha N may modify the biological activity of inhibin b
y influencing its half-life or access to ifs receptor. alpha N may als
o play a role in regulating fertility through a local action on ovulat
ion by the ovary that is independent of the actions of inhibin. The ev
idence suggests a unique physiological significance for the precursor
peptides of the inhibin-alpha subunit in both the endocrine and paracr
ine control of fertility.