The family of inhibin-related proteins has been investigated extensively in the last decade. It is composed of three members: inhibin, activin and follistatin. Inhibin and activin are chemically related, while follistatin acts as an activin-binding protein. Initially identified as regulators of pituitary follice stimulating hormone (FSH) secretion, inhibin, activin and follistatin have more recently been characterized as growth factors, embryo modulators and immune factors. Human placenta, amnion, chorion and maternal decidua express mRNAs for inhibin, activin and follistatin, and the presence of both immunoreactive and bioactive proteins has been demonstrated. The proteins are present in maternal and fetal circulation, and are measurable in amniotic fluid with changes related to gestational age and to the occurrence of gestational diseases. Various biological actions have been described in embryo and intrauterine tissues, which suggest a role for these proteins in the development of the gestational unit. However, several questions remain to be elucidated. The chemical forms of inhibin, activin and follistatin produced by human placenta and the mechanisms involved in the regulation of their secretion are largely unknown. The nature of the receptors for these proteins and the physiological implications of receptor activation have not yet been elucidated and this will require further investigation.