An aspartic proteinase expressed in the equine placenta.
Abstract: This manuscript describes the cloning of a novel aspartic proteinase expressed in the placenta of the horse (order Perrisodactyla). Evidence for similar genes in the cat (Carnivora) and ruminants (Artiodactyla), indicates that these molecules have been conserved within widely divergent species with distinct types of placentation. Since ePAG is produced by the outer cell layer (trophoblast) of the placenta, it can tentatively be grouped with the pregnancy-associated glycoproteins (PAG) of cattle, sheep, and pig. The high sequence identity that ePAG shares with pepsinogens as well as the PAG, indicates that ePAG may be the evolutionary bridge that links these two groups of aspartic proteinases.
Publication Date: 1998-04-30 PubMed ID: 9561214DOI: 10.1007/978-1-4615-5373-1_22Google Scholar: Lookup
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- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The researchers discovered a new type of protein- an aspartic proteinase- within horse placenta that appears to be present within different species of animals. The similarities between these proteins suggest that they have been conserved throughout evolution and may play a crucial in the function of the placenta during pregnancy.
Introduction to the Research
- This study focuses on the discovery and cloning of a specific kind of protein called aspartic proteinase found in the placenta of horses.
- The aspartic proteinase is expressed in different types of species with distinct forms of placentation, including cats and ruminants.
- This protein holds potentially significant implications for the understanding of the evolutionary processes the placentation undergoes throughout different species.
Key Findings
- The aspartic proteinase discovered, tentatively classified as ePAG (equine Pregnancy-associated glycoproteins), is produced by the outermost layer of cells in the placenta, called the trophoblast.
- This indicates that ePAG may be associated with other similar glycoproteins found in cattle, sheep, and pigs, known as Pregnancy-associated glycoproteins (PAGs).
- The high sequence identity shared between ePAG and two groups of aspartic proteinases, namely the pepsinogens and PAGs, suggests that ePAG could be an evolutionary bridge connecting these two groups.
Implications of Findings
- Understanding the function and evolutionary significance of ePAG could provide crucial insights into reproductive biology, particularly regarding pregnancy.
- Considering the conservation of these proteins across largely different species, this could highlight the importance the protein has in the process of placental development and function.
- Further research and comparative studies among different species will allow a more precise comprehension of the importance and specificity of these types of proteins in reproductive processes.
Cite This Article
APA
Green J, Xie S, Gan X, Roberts RM.
(1998).
An aspartic proteinase expressed in the equine placenta.
Adv Exp Med Biol, 436, 163-167.
https://doi.org/10.1007/978-1-4615-5373-1_22 Publication
Researcher Affiliations
- Department of Animal Sciences, University of Missouri, Columbia 65211, USA.
MeSH Terms
- Animals
- Aspartic Acid Endopeptidases / genetics
- Cats
- Cattle
- DNA, Complementary
- Gene Expression
- Glycoproteins / genetics
- Horses
- Placenta / enzymology
- Pregnancy Proteins / genetics
- RNA, Messenger
Grant Funding
- HD29483 / NICHD NIH HHS
Citations
This article has been cited 3 times.- Srinivasan SV, Ghosh J, Nazar SB, Roy KS. Buffalo early pregnancy biomarker coding sequence cloning and partial length expression in E. coli after codon optimization. Heliyon 2019 Nov;5(11):e02863.
- Wiedemann I, Krebs T, Momberg N, Knorr C, Tetens J. mRNA expression profiling in cotyledons reveals significant up-regulation of the two bovine pregnancy-associated glycoprotein genes boPAG-8 and boPAG-11 in early gestation. Vet Med Sci 2018 Nov;4(4):341-350.
- Majewska M, Lipka A, Panasiewicz G, Gowkielewicz M, Jozwik M, Majewski MK, Szafranska B. Identification of Novel Placentally Expressed Aspartic Proteinase in Humans. Int J Mol Sci 2017 Jun 8;18(6).
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