Beta-microseminoprotein (beta-MSP) is not an inhibin.

Beta-microseminoprotein (beta-MSP), a sperm-coating antigen isolated from human seminal plasma, has apparent structural identity with "beta-inhibin" isolated from the same source. Publication of the amino acid sequence of beta-MSP revealed a greater than 96% homology with "beta-inhibin," with only a proline-threonine substitution at positions 39 and 40, and the omission of a glycine at position 93. Due to the nearly identical sequences of "beta-inhibin" and beta-MSP, we examined the ability of beta-MSP and its tryptic peptides to inhibit basal follicle-stimulating hormone (FSH) secretion from rat pituitary cells in culture, the inhibin bioassay. Whole pituitaries collected from 250- to 300-g male rats were dispersed enzymatically and plated onto 24-well culture dishes for 3 days. beta-MSP and its tryptic peptides were dissolved in cell culture medium, applied to the pituitary monolayer cell cultures, and incubated for an additional 3 days. FSH levels in the medium were determined by radioimmunoassay. A partially purified preparation of inhibin and our in-house inhibin standard, both prepared from porcine follicular fluid (pFFl), were included in the same assay. Whereas the partially purified inhibin from pFFl showed a dose-dependent inhibition of FSH secretion, with a 50% inhibitory dose (ID50) of 50 ng, which paralleled that of the standard, beta-MSP and its tryptic peptides failed to depress FSH levels in the medium at any of the doses tested (10-10,000 ng/ml). We conclude that beta-MSP is not an inhibin under our assay conditions.