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Published online by Cambridge University Press:  02 March 2009

Henry G Burger*
Prince Henry's Institute of Medical Research, Melbourne, Australia
Henry G Burger, Director, Prince Henry's Institute of Medical Research, Clayton, Victoria 3168, Australia.
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Inhibin is a glycoprotein hormone, consisting of two dissimilar, disulphide-linked subunits, termed α (MW 20kD) and β (MW 3-15kD), which inhibits the production and/or secretion of pituitary gonadotrophins, preferentially follicle stimulating hormone (FSH). The most widely studied inhibin molecule has a molecular weight of 31-32kD, as purified and cloned from bovine, porcine, ovine, rat and human sources. Higher molecular weight forms have been identified in ovarian follicular fluids and in culture media of granulosa and Sertoli cells, and generally differ from the 31kD form in having larger α-subunits, designated by their molecular weights, e.g. α44 in 58kD inhibin. There are two forms of the β-subunit, named βA and βB and the corresponding inhibin dimers have been named inhibin A and inhibin B. Dimers of the β-subunit, which have been shown to have FSH stimulating activity, are termed activins and are designated activin A, B or AB depending on whether the dimer is a homodimer of βA or βB or a heterodimer of βA and βB (Figure 1). The major gonadal source of inhibin is the granulosa cell in the female and the Sertoli cell in the male. Other potential cellular sites of origin will be discussed below.

Copyright © Cambridge University Press 1992

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