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.

It is 130 years since the first description of endometriosis and yet this enigmatic disease still continues to confound gynaecologists. In the last five years there has been evidence which suggests that endometriosis is a much more common finding in the pelvis than previously recognized and this has created conflict over the precise definition of the disease. Currently it is difficult for clinicians to be certain what constitutes endometriosis and what is the clinical and pathological significance of the visual diagnosis of the disease. This article will review the evidence about the pathological significance of the visual diagnosis of endometriosis. It will analyze the aetiological factors that predispose to the disease and evidence concerning its pathogenesis. Finally, it will discuss the evidence that points to a particular epithelium being the origin of endometriosis.

Human endometrium is composed of three layers: stratum compactum, stratum spongiosum and stratum basale. Stratum compactum is the superficial layer made up of openings of the uterine glands and some stromal cells. Stratum spongiosum is the middle layer containing mainly dilated glands and little stroma. Stratum basale is the deepest layer adjoining the muscularis. It consists of primordial glands and compact stroma. Stratum compactum and stratum spongiosum form stratum functionale which is subject to cyclic changes and is removed during menstruation.

Spermatozoa binding to the zona pellucida is an early, critical event leading to fertilization and early pre-embryo development. Fertilization involves a complex and orderly sequence of events that is completed at syngamy, which is defined as the union of the two sets of haploid chromosomes to form a new diploid fertilized ovum (zygote). In order to be able to fertilize an oocyte, spermatozoa need to undergo a process called ‘capacitation’, which is usually defined as a series of changes that renders the sperm cells capable of undergoing the acrosome reaction. This process that naturally occurs within the female genital tract is possible under in vitro conditions. However, capacitation is not the only process spermatozoa must undergo to fertilize the oocytes successfully. To fertilize an oocyte, spermatozoa must also be at least highly motile, as well as being capable of undergoing the acrosome reaction timely, penetrating through the oocyte investments and fusing with the oocyte plasma membrane properly.

Uterine growth factors appear to play a role in the regulation of pregnancy. One of these, colony stimulating factor-1 (CSF-1), synthesized by the uterine epithelium under the control of female sex steroids, has been shown to have important functions both before implantation and during the formation of the placenta. In the female reproductive tract the CSF-1 receptor, the product of the c-fms proto-oncogene, is expressed in decidual cells, trophoblasts and macrophages, indicating that these cells are the primary targets for CSF-1. This article reviews the biology of CSF-1 during gestation as well as the possible involvement of CSF-1 and its receptor in the aetiology of gynaecological tumours.

Endothelin-1 (ET-1) is a 21 amino acid peptide, first isolated in 1988 from porcine aortic endothelial cells in tissue culture (Figure 1). The peptide was shown to be the most potent known vasoconstrictor of porcine coronary arteries. A powerful endothelium-derived vasoconstrictor had been predicted for some time, but it was when Yanagisawa and his colleagues elucidated the structure, and provided information about the molecular biology and mode of action of the peptide that an unprecedented interest was stimulated in the endothelins.