Early pregnancy detection and the hormonal characterization of embryonic-fetal mortality in fallow deer (Dama dama)

Willard, Scott T.; Sasser, R.G.; Jaques, John T.; White, D. R.; Neuendorff, D. A.; Randel, R.D.

doi:10.1016/s0093-691x(98)00035-1

Cited by 23 publications

(11 citation statements)

References 28 publications

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“…Moreover, heterologous PAG tests were also useful for pregnancy diagnoses in wild ruminants, i.e. wood bison [107], moose [108], rocky mountain elk [109], white-tailed deer [110,111], mule deer [111], red deer [112], sika deer [113], fallow deer [114,115], mountain goat [116] and Alpine goats [117][118][119]. The measurement of PAG protein concentrations in maternal blood or milk of ruminants allow for 76.6-100% accuracy rates for early pregnancy diagnoses [120,121] and provide an alternative method to ultrasonography for determining late embryonic mortality [96,122].…”

Section: Pregnancy Diagnostic Pag Testsmentioning

confidence: 99%

Biodiversity of multiple Pregnancy-Associated Glycoprotein (PAG) family: gene cloning and chorionic protein purification in domestic and wild eutherians (Placentalia) – a review

2006

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-This review presents a broad overview of chorionic glycoproteins encoded by the Pregnancy-Associated Glycoprotein (PAG) gene family and also serves to illustrate how the recent discovery of the PAG family has contributed to our general knowledge of genome evolution, placental transcription and placental protein expression. The complex and large PAG family is restricted to the Artiodactyla order, although single PAG-like genes have also been identified in species outside the Artiodactyla. The PAGs are members of the aspartic proteinase (AP) superfamily. Unexpectedly, however, some members of the PAG family possess amino acid substitutions within and around the active site that likely render them unable to act as proteinases. This paper summarises the available information regarding biodiversity of PAG gene expression based on cDNA cloning, mRNA localisation studies and the structural organisation of the PAG genes with a particular emphasis on PAG promoters. It also compares available data regarding PAG protein purifications, sequencing and their N-glycodiversity. Finally, it discusses the scientific relevance, possible functional roles of the PAGs and describes possible profitable applications related to the detection of PAG proteins in the blood of pregnant domestic and wild species. chorionic glycoproteins / eutherian PAG family / diagnostic PAG markers

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Section: Pregnancy Diagnostic Pag Testsmentioning

confidence: 99%

Biodiversity of multiple Pregnancy-Associated Glycoprotein (PAG) family: gene cloning and chorionic protein purification in domestic and wild eutherians (Placentalia) – a review

2006

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“…Antigens serologically similar to PSPB and PAG1 have been found in other ruminants, including mule and whitetailed deer [23,24], mountain goats [25], red deer [26], French alpine goats [27], bison [28], moose [29], elk [30], fallow deer [31], and sika deer [32].…”

Section: Introductionmentioning

confidence: 99%

Isolation and Partial Characterization of a Pregnancy-Associated Glycoprotein Family from the Goat Placenta1

Garbayo

Rémy

Alabart³

et al. 1998

Biology of Reproduction

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Antigen(s) immunologically related to pregnancy-associated glycoproteins (PAGs) have previously been detected in the serum of pregnant goats. In this work, we describe a partial characterization of a family of PAGs isolated from the placenta of the goat. The procedure, monitored by RIA, included extraction of proteins at neutral pH, acidic, and ammonium sulfate precipitations; and gel filtration and ion exchange chromatographies. Immunoreactivity, initially located in the acidic supernatant and in the 40-80% ammonium sulfate fractions, was equally apportioned between the 0.04 and 0.08 M NaCl DEAE fractions. After further purification of both DEAE fractions, the preparations were subjected to one- and two-dimensional electrophoresis, and individual polypeptides were analyzed by amino acid sequencing. Three PAGs, which differed in amino acid sequence and apparent molecular masses (62, 59, and 55 kDa), were detected, each containing several isoforms with different pls: caprine (c) PAG62 (pl: 5.1, 4.8), cPAG59 (pl: 6.2, 5.9, 5.6), and cPAG55 (pl: 5.3, 5.1, 4.9). These proteins had high sequence identities to each other and to PAGs purified from other species. Each had two putative N-glycosylation sites within the 27 amino terminal residues sequenced. This work demonstrates that PAGs are present in goat placenta and that multiple forms are expressed.

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“…But, only two micro-sequence fragments of native PAG-like proteins, oPAG (65 kDa) and pBP (43 kDa), corresponded to the sequences of PAG precursors: oPAG3 or oPAG7 and the pPAG2-like subfamily, respectively. However, the purified native PAG proteins, mostly bovine and ovine PAG, have been applied with different cross-reacting anti-PAG sera for radioimmunologic assays (RIA) as routine diagnostic tests of pregnancy in domestic ruminants [25,28,49,50], as well as in various wild ruminants, including the bison [51], moose [52], elk [53], Alpine goat [54] and several deers [55][56][57]. These RIA tests were also used to recognise twins or single pregnancy [58] and the sex of the fetus [59].…”

Section: Discussionmentioning

confidence: 99%

Chorionic expression of heterogeneous products of the PAG (Pregnancy-Associated Glycoprotein) gene family secreted in vitro throughout embryonic and foetal development in the pig

et al. 2003

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-Porcine PAG (pPAG) are placental products of a multigene family that is strongly expressed in the chorionic epithelium (trophoblast and trophectoderm). The objective of this study was to define a pattern of the pPAG proteins, secreted in vitro by chorionic explants harvested on 16-77 days of pregnancy. Trophoblastic and trophectodermal explants were collected from pregnant (PR) gilts (n = 27) and used for protein in vitro production (8-261 h). Endometrial explants of luteal-phase gilts (E10, n = 4) and pseudopregnant gilts (PsE, n = 2) were used as negative controls for protein immunoblotting. Proteins (PR, E10, PsE) were isolated mainly from incubation media, fractionated, dialysed and separated by SDS-PAGE. Heterogeneous Western blotting with various polyclonal anti-PAG sera raised against bovine or ovine antigens (anti-bPAG, or anti-oPAG) initially identified the pPAG proteins. Such blotting of fractionated chorionic proteins allowed for the isolation of porcine antigens that were employed as immunogens to raise several homologous antisera (anti-pPAG). Crude antisera were adsorbed on endometrial extracts or proteins of non-PR pigs, to remove non-relevant antibodies. The patterns of pPAG proteins secreted in vitro varied throughout pregnancy (35-72 kDa). During implantation,~43 kDa (Day 16) or~68.1 kDa (Days 17-25) pPAG proteins were detected. During placentation and as pregnancy advanced (Days 31-77), 72.3 kDa pPAG proteins were observed. The secretions of parallel multiple smaller proteins (35.4-47.2 kDa), presumably, as forms of processed pPAG precursors, increased with the progress of gestation. In conclusion, the pPAG protein family plays a very important role during implantation, placenta formation and embryonic/foetal development in the pig. chorionic glycoproteins / placenta / pPAG gene family / pig / pregnancy / trophectoderm

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Early pregnancy detection and the hormonal characterization of embryonic-fetal mortality in fallow deer (Dama dama)

Cited by 23 publications

References 28 publications

Biodiversity of multiple Pregnancy-Associated Glycoprotein (PAG) family: gene cloning and chorionic protein purification in domestic and wild eutherians (Placentalia) – a review

Biodiversity of multiple Pregnancy-Associated Glycoprotein (PAG) family: gene cloning and chorionic protein purification in domestic and wild eutherians (Placentalia) – a review

Isolation and Partial Characterization of a Pregnancy-Associated Glycoprotein Family from the Goat Placenta1

Chorionic expression of heterogeneous products of the PAG (Pregnancy-Associated Glycoprotein) gene family secreted in vitro throughout embryonic and foetal development in the pig

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