Reference : Glycoproteins of the aspartyl proteinase gene family secreted by the developing placenta
Scientific journals : Article
Life sciences : Veterinary medicine & animal health
Glycoproteins of the aspartyl proteinase gene family secreted by the developing placenta
Roberts, R. M. [University of Missouri - MU > Department of Animal Science > > >]
Xie, S. [University of Missouri - MU > Department of Biochemistry > > >]
Nagel, R. J. [University of Missouri - MU > Department of Biochemistry > > >]
Low, B. [University of Missouri - MU > Department of Biochemistry > > >]
Green, J. [University of Missouri - MU > Department of Bichemistry > > >]
Beckers, Jean-François mailto [Université de Liège - ULiège > Département de sciences fonctionnelles > Physiologie de la reproduction >]
Advances in Experimental Medicine and Biology
Kluwer Academic/Plenum Publishers
Yes (verified by ORBi)
New York
[en] Pregnancy in cattle and sheep can be diagnosed by the presence of placentally-derived antigens (pregnancy-associated glycoproteins or PAG-1) in maternal serum soon after implantation begins at about Day 20 following conception. Molecular cloning of their cDNA has revealed that PAG-1 belong to the aspartic proteinase gene family and have about 50% amino acid sequence identity to pepsin. However, critical amino acid substitutions at the active site regions suggest that both bovine and ovine PAG-1 are enzymatically inactive. PAG-1 expression has been shown by in situ hybridization and immunocytochemistry to be localized to the trophoblast binucleate cells, which invade maternal uterine endometrium during implantation. The glycoproteins are concentrated in dense cytoplasmic granules that are discharged after the binucleate cells have migrated to the maternal side of the placental barrier. We suggest, therefore, that the PAG-1 might have an endocrine function either as carriers of other bioactive peptides or by acting as hormones themselves. Recently screening of placental libraries with nucleic acid probes has identified additional cDNA that are very abundant and code for polypeptides (PAG-2 and PAG-3) related to, but antigenically and structurally distinct from PAG-1 described above. These molecules have sequences of amino acids at their catalytic centers that are consistent with their being potentially functional proteinases but their role during pregnancy, like that of PAG-1, is unclear.
Researchers ; Professionals

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