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Downloaded from Bioscientifica.Com at 10/02/2021 09:03:44AM Via Free Access Pepsin-Related Molecules Secreted by Trophoblast 63 Reviews of Reproduction (1998) 3, 62–69 Pepsin-related molecules secreted by trophoblast Jonathan A. Green, Sancai Xie and R. Michael Roberts Departments of Animal Sciences, Biochemistry, and Veterinary Pathobiology, University of Missouri–Columbia, Columbia, MO 65211–0001, USA The pregnancy-associated glycoproteins (PAGs) were first described as placental antigens of cattle that were also present in the blood serum of the mother after implantation. Molecular cloning studies have shown that they are members of the aspartic proteinase gene family and closely related to the pepsinogens. An enzymatic role seems unlikely, as at least some of them have mutations likely to render them enzymatically inactive. Nevertheless, these molecules have retained the substrate-binding cleft of the pepsins and are expressed abundantly in trophectoderm, particularly in the invasive binucleate cell component. There may be as many as 100 PAG genes in cattle and sheep, many of which are transcribed. PAGs are also products of the placenta of the pig, a species whose progenitors diverged from the ruminants at least 55 million years ago. There is even evidence for PAG-like molecules outside the Artiodactyla. Although their function remains elusive, it seems unlikely that these placentally expressed mol- ecules are simply oddities in view of their long-term evolutionary survival and conspicuous presence at the fetal–maternal interface. The placentation that occurs in ruminant ungulate species, such Identification of placental-specific antigens in ruminants as cattle, sheep and goats, is superficial, relatively noninvasive, and can be referred to as synepitheliochorial cotyledonary In 1982, Sasser and coworkers (Butler et al., 1982) injected ex- (Wooding, 1992). ‘Synepitheliochorial’ describes the fetal– tracts of homogenized bovine cotyledons into rabbits with the maternal syncytium formed by the fusion of trophoblast binu- aim of raising antisera with placental specificity. Antibodies cleate cells and uterine epithelial cells, whereas ‘cotyledonary’ that were not directed against placenta were adsorbed out with describes the gross structure of the placenta and specifically the tissue extracts from nonpregnant animals. The cleared anti- tufts of villous trophoblast (cotyledons) that insinuate them- serum was then used to monitor the partial purification of selves into the crypts of the maternal caruncles. These regions two pregnancy-specific antigens, pregnancy-specific protein A of fused fetal and maternal tissue are referred to as placentomes (PSP-A) and pregnancy-specific protein B (PSP-B). The former and are the main sites for nutrient and gas exchange in the was α-fetoprotein; however, PSP-B represented a novel antigen. placenta. Subsequent studies indicated that PSP-B probably represented The trophectodermal (chorionic) epithelium of the ruminant a mixture of related proteins since multiple molecular weight placenta contains two distinct cell populations: binucleate cells, forms (47 000–90 000) and isoelectric variants (pI 3.7–4.4) were which represent 15–20% of the total cell population within the reported (Butler et al., 1982; Sasser et al., 1989). The placental ex- mature placenta, and mononucleate cells, which comprise pression of PSP-B was restricted to the binucleate cells described the rest (Wooding, 1983). Binucleate cells have two unique above (Eckblad et al., 1985). The antigen was also detectable in characteristics. First, they migrate from the trophectoderm and maternal blood (Sasser et al., 1986), probably as a result of dis- fuse with uterine epithelial cells to form a syncytium. In sheep, charge from secretory granules subsequent to trinucleated cell the syncytium is rather extensive and persists throughout preg- formation. The radioimmunoassay with the anti-PSP-B anti- nancy. However, in cattle, the syncytium that is formed during serum developed by Sasser and his colleagues provided an ac- implantation is subsequently replaced by an intact epithelium curate pregnancy test for cattle as early as 30–35 days after by day 40. After this, the migration and fusion of binucleate insemination (Humblot et al., 1988). In some animals, PSP-B cells is limited to the generation of short-lived trinucleated cells could even be detected in maternal serum before day 20 of preg- (Fig. 1; Wooding, 1992). This fusion event is the extent of in- nancy. Antigens related immunologically to PSP-B were also vasive implantation in these species, but it allows the conceptus found in the blood of pregnant sheep (Ruder et al.,1988), mule to establish a more direct endocrinological, and presumably deer, white tail deer (Wood et al., 1986), and muskoxen (Rowell immunological, dialogue with the mother than is observed in et al., 1989) and appear to be characteristic of all ruminants. species such as the pig, where no erosion of the uterine epi- Zoli et al. (1991) reported the purification of a pregnancy- thelium occurs. Indeed, the second unique characteristic of the specific antigen they named pregnancy-associated glycoprotein binucleate cells is their ability to deliver their secretory products, or PAG. Again, antisera were raised against antigens specific to which are concentrated in dense granules, directly to the ma- fetal cotyledons and used to monitor the purification steps of ternal system. Within these dense secretory granules are the PAG. PAG is an acidic glycoprotein (pI 4.4–5.4) with a mol- placental lactogens (Duello et al., 1986) as well as many of the ecular weight of 67 000. Like PSP-B, it was first detectable in the pregnancy-associated glycoproteins, the subject of this review. maternal circulation of some cows at around the time that © 1998 Journals of Reproduction and Fertility 1359-6004/98 $12.50 Downloaded from Bioscientifica.com at 10/02/2021 09:03:44AM via free access Pepsin-related molecules secreted by trophoblast 63 (b) Dividing cell Tight junctions 1 Trophectoderm 2 Microvillar junction 3 4 Uterine Fetal villi cryptal epithelium (a) Maternal capillary Sheep, goat Exocytosis (c) Cow 1 5 Maternal crypt Trophectoderm 2 Trinucleate 4 3 cells Uterine cryptal epithelium Exocytosis Maternal capillary Fig. 1. The binucleate cell, its contribution to the definitive ruminant placenta and its endocrine characteristics. (a) Part of a mature placentome showing the cotyledonary fetal villi penetrating the crypts of the maternal caruncle. The region is heavily vascularized on both sides of the junction. (b) In sheep and goats, a fetomaternal syncytium is formed as the result of binucleate cell migration (stages 1 and 2) and fusion (stages 3 and 4); secretory granules release their contents basolaterally. After day 40 of pregnancy, bovine binucleate cell migration (c) pro- duces short-lived trinucleate cells (stage 3) which, after exocytosis, are resorbed by the trophectoderm (stages 4 and 5). The granules of binu- cleate cells contain placental lactogens and PAGs that can gain access to maternal capillaries. Presumably, PAGs expressed by mononucleate cells are secreted at the maternal–fetal interface. (Diagram adapted from Wooding, 1992.) the trophoblast formed definitive attachment to the uterine wall. active site that would likely interfere with the catalytic mechan- Concentrations increased gradually thereafter, and reached peak ism, bovine and ovine PAG-1 are probably not capable of acting values just before parturition at about 1 µg ml–1 (Zoli et al., 1992). as enzymes. This feature is discussed in greater detail below. Soon after, PAG and PSP-B were determined to be similar in The expression of PAG-1 is restricted to binucleate cells amino acid sequence (Lynch et al., 1992). within the outer epithelial layer of the placenta (Xie et al., 1991), Xie et al. (1991) cloned PAG (now known as PAG-1) from where it colocalizes with a placental lactogen, and also with late bovine and ovine placenta by screening cDNA libraries another antigen recognized by the monoclonal antibody, SBU-3 with an anti-PAG antiserum. The bovine and ovine cDNAs en- (Fig. 2). The latter recognizes a carbohydrate epitope restricted coding PAG-1 shared 86% nucleotide sequence identity with to binucleate cells (Lee et al., 1986). one another and encoded proteins of 380 and 382 amino acids, respectively, including a 15 amino acid signal sequence. Aspartic proteinases However, protein sequence data already showed that the first amino acid of bovine PAG-1 was an arginine that corresponded The aspartic proteinases, to which the PAGs are related in to one at position 39, downstream of the site of signal sequence structure, are an ancient family of enzymes. Those from higher cleavage, indicating that PAG-1 undergoes post-translational organisms, such as the digestive enzyme, pepsin, or the more processing from a pro-form. specialized hormone-processing proteinase, renin, consist of a The most surprising feature of bovine and ovine PAG-1 re- single polypeptide chain folded to form a bilobed structure vealed by the cloning experiments was that they belonged to a (Davies, 1990). In contrast, the retroviral forms are dimers of family of proteolytic enzymes known as aspartic proteinases. In two identical subunits. Consequently, the eukaryotic enzymes particular, they had greatest sequence identity with pepsino- probably arose by a duplication of a progenitor gene (Tang and gens (Table 1). However, owing to mutations in and around the Wong, 1987). In these enzymes, a pair of essential aspartic acid Downloaded from Bioscientifica.com at 10/02/2021 09:03:44AM via free access 64 J. A. Green et al. Table
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