Chorionic mRNA expression and N-glycodiversity of pregnancy-associated glycoprotein family (PAG) of the European bison (Bison bonasus)

Szafrańska, Bożena; Panasiewicz, Grzegorz; Dąbrowski, Maciej; Majewska, Marta; Giżejewski, Zygmunt; Beckers, Jean‐François

doi:10.1016/j.anireprosci.2004.12.013

Cited by 14 publications

(7 citation statements)

References 59 publications

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“…In goats, cPAG2 has been detected only during early pregnancy (18-19 dpc) throughout TRD, cPAG8 is expressed during the entire pregnancy, but 9 distinct transcripts (cPAG1, cPAG3-7 and cPAG9-11) start expression from 45 dpc [15]. The PAG mRNA family expression was also identified in European bison and camelids by hybridisation with the use of porcine PAG probes [45,52].…”

Section: Pregnancy-stage Dependentmentioning

confidence: 99%

“…different number and length of the PAG amplicons in various species, including the pig, wild boar, cattle, sheep, goat, elk, beaver [40][41][42][43], Carnivora species [44] and European bison (Eb) -classified as an endangered species: EN A2ce, C2a, IUCN [45,46]. These produced gDNA amplicons suggest that some PAG genes in these species can have shortened introns E, G and H, which are between exons 5-6, 7-8 and 8-9, respectively.…”

Section: Exon-intron Structure Of the Pag Genes Promoters And Gene Nmentioning

confidence: 99%

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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-stage Dependentmentioning

confidence: 99%

Section: Exon-intron Structure Of the Pag Genes Promoters And Gene Nmentioning

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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“…Thus, the variety of the PAGs may reflect different functions as pregnancy advances, as a local suppressive factor influencing the feto-maternal barrier by modulation of the maternal immune system [ 10 ] and as chorionic ligands for the luteal and uterine gonadotrophin receptors of cycling and pregnant animals [ 13 , 14 , 41 ]. Previously, diversified profiles of the PAGs (e.g., in pigs and European bison) were an effect of multiple glycosylation [ 12 , 42 ]. In this study, diversified pep/PAG-L profiles were also identified, although only one site of potential glycosylation was predicted within the amino acid sequence of the pep/PAG-L precursor.…”

Section: Discussionmentioning

confidence: 99%

“…This may suggest that pep/PAG-L can be secreted directly into the maternal blood space. To date, the PAGs have been localized only within epitheliochorial placentas [ 12 , 28 , 40 , 44 , 46 , 47 ]. In ruminants, multiple granules of binucleated cells are released close to the maternal circulation, while the trophectodermal barrier to other feto-maternal exchange is maintained [ 43 , 48 ].…”

Section: Discussionmentioning

confidence: 99%

“…All members of the AP superfamily possess a bilobed structure with a cleft capable of binding short peptides. In vitro studies also revealed multiple secretory PAG isoforms produced by chorionic explants of domestic and wild species [ 11 , 12 ]. Radio-receptor studies revealed the potential physiological importance of PAG family products as various chorionic signaling ligands interacting with gonadal and extra-gonadal gonadotropin receptors of cycling pigs and cows [ 13 ] or early pregnant pigs [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

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Identification of Placental Aspartic Proteinase in the Eurasian Beaver (Castor fiber L.)

Lipka

Panasiewicz

Majewska

et al. 2018

IJMS

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Aspartic proteinases (AP) form a multigenic group widely distributed in various organisms and includes pepsins (pep), cathepsins D and E, pregnancy associated glycoproteins (PAGs) as well as plant, fungal, and retroviral proteinases. This study describes the transcript identification and expression localization of the AP within the discoid placenta of the Castor fiber. We identified 1257 bp of the AP cDNA sequence, encoding 391 amino acids (aa) of the polypeptide precursor composed of 16 aa signal peptide, 46 aa pro-piece, and 329 aa of the mature protein. Within the AP precursor, one site of potential N-glycosylation (NPS119–121) and two Asp residues (D) specific for the catalytic cleft of AP were identified (VLFDTGSSNLWV91–102 and GIVDTGTSLLTV277–288). The highest homology of the identified placental AP nucleotide and aa sequence was to mouse pepsinogen C (75.8% and 70.1%, respectively). Identified AP also shared high homology with other superfamily members: PAGs, cathepsins, and napsins. The AP identified in this study was named as pepsinogen/PAG-Like (pep/PAG-L). Diversified pep/PAG-L protein profiles with a dominant 58 kDa isoform were identified. Immune reactive signals of the pep/PAG-L were localized within the trophectodermal cells of the beaver placenta. This is the first report describing the placental AP (pep/PAG-L) in the C. fiber.

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Pregnancy-associated glycoprotein (PAG) family localized in chorionic cells within the epitheliochorial/diffuse placenta of the alpaca (Lama pacos)

2011

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Chorionic mRNA expression and N-glycodiversity of pregnancy-associated glycoprotein family (PAG) of the European bison (Bison bonasus)

Cited by 14 publications

References 59 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

Identification of Placental Aspartic Proteinase in the Eurasian Beaver (Castor fiber L.)

Pregnancy-associated glycoprotein (PAG) family localized in chorionic cells within the epitheliochorial/diffuse placenta of the alpaca (Lama pacos)

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