Comparison of pregnant mare serum gonadotropin products with surprising differences in protein content
Abstract Equine chorionic gonadotropin (eCG) is a widely used hormone that synchronizes the female cycle and induces estrus in livestock. eCG is a heterodimeric glycoprotein composed of non-covalently linked α- and β-chains whose glycosylation profiles determine the in vivo activity of the hormone....
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Nature Portfolio
2025-02-01
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| Series: | Scientific Reports |
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| Online Access: | https://doi.org/10.1038/s41598-025-90833-3 |
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| author | Martina Lösle Chia-Wei Lin Jane Beil-Wagner Markus Aebi Thorsten Buch |
| author_facet | Martina Lösle Chia-Wei Lin Jane Beil-Wagner Markus Aebi Thorsten Buch |
| author_sort | Martina Lösle |
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| description | Abstract Equine chorionic gonadotropin (eCG) is a widely used hormone that synchronizes the female cycle and induces estrus in livestock. eCG is a heterodimeric glycoprotein composed of non-covalently linked α- and β-chains whose glycosylation profiles determine the in vivo activity of the hormone. The commercially available eCG products are crudely purified from the serum of pregnant mares, hence called pregnant mare serum gonadotropin (PMSG). Appropriate glycosylation of the protein is crucial for the correct binding to the receptor, receptor activation, and its half-life. The exact protein composition of the various commercial PMSG products and their specific glycosylation pattern have not been characterized so far. Therefore, we used proteomic approaches to analyse and compare four commercial PMSG products. Here we show that the examined PMSGs share a surprisingly low level of commonalities (5.5%) in protein composition among the four tested products, with serum proteins as the primary variable. Analysing the site-specific N-glycosylation, we confirmed the presence of O-acetylation of sialic acids at the structure of the glycans of eCG, which we could not find in significant amounts on human CG, suggesting that this modification is species-specific. It remains to be tested whether the O-acetylation plays an important role in the function of PMSG. However, this modification shall be considered while recombinant eCG are produced. |
| format | Article |
| id | doaj-art-06e185724bca42eb8991cf8d87cf1096 |
| institution | DOAJ |
| issn | 2045-2322 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Nature Portfolio |
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| spelling | doaj-art-06e185724bca42eb8991cf8d87cf10962025-08-20T03:04:11ZengNature PortfolioScientific Reports2045-23222025-02-0115111310.1038/s41598-025-90833-3Comparison of pregnant mare serum gonadotropin products with surprising differences in protein contentMartina Lösle0Chia-Wei Lin1Jane Beil-Wagner2Markus Aebi3Thorsten Buch4Institute of Laboratory Animal Science, University of ZurichFunctional Genomics Center Zürich, ETH ZürichInstitute of Laboratory Animal Science, University of ZurichInstitute of Microbiology, Department of Biology, ETH ZürichInstitute of Laboratory Animal Science, University of ZurichAbstract Equine chorionic gonadotropin (eCG) is a widely used hormone that synchronizes the female cycle and induces estrus in livestock. eCG is a heterodimeric glycoprotein composed of non-covalently linked α- and β-chains whose glycosylation profiles determine the in vivo activity of the hormone. The commercially available eCG products are crudely purified from the serum of pregnant mares, hence called pregnant mare serum gonadotropin (PMSG). Appropriate glycosylation of the protein is crucial for the correct binding to the receptor, receptor activation, and its half-life. The exact protein composition of the various commercial PMSG products and their specific glycosylation pattern have not been characterized so far. Therefore, we used proteomic approaches to analyse and compare four commercial PMSG products. Here we show that the examined PMSGs share a surprisingly low level of commonalities (5.5%) in protein composition among the four tested products, with serum proteins as the primary variable. Analysing the site-specific N-glycosylation, we confirmed the presence of O-acetylation of sialic acids at the structure of the glycans of eCG, which we could not find in significant amounts on human CG, suggesting that this modification is species-specific. It remains to be tested whether the O-acetylation plays an important role in the function of PMSG. However, this modification shall be considered while recombinant eCG are produced.https://doi.org/10.1038/s41598-025-90833-3Equine chorionic gonadotropin (eCG)Lutropin/Luteinizing hormone (LH)O-acetylationPregnant mare serum gonadotropin (PMSG)Sulfation |
| spellingShingle | Martina Lösle Chia-Wei Lin Jane Beil-Wagner Markus Aebi Thorsten Buch Comparison of pregnant mare serum gonadotropin products with surprising differences in protein content Scientific Reports Equine chorionic gonadotropin (eCG) Lutropin/Luteinizing hormone (LH) O-acetylation Pregnant mare serum gonadotropin (PMSG) Sulfation |
| title | Comparison of pregnant mare serum gonadotropin products with surprising differences in protein content |
| title_full | Comparison of pregnant mare serum gonadotropin products with surprising differences in protein content |
| title_fullStr | Comparison of pregnant mare serum gonadotropin products with surprising differences in protein content |
| title_full_unstemmed | Comparison of pregnant mare serum gonadotropin products with surprising differences in protein content |
| title_short | Comparison of pregnant mare serum gonadotropin products with surprising differences in protein content |
| title_sort | comparison of pregnant mare serum gonadotropin products with surprising differences in protein content |
| topic | Equine chorionic gonadotropin (eCG) Lutropin/Luteinizing hormone (LH) O-acetylation Pregnant mare serum gonadotropin (PMSG) Sulfation |
| url | https://doi.org/10.1038/s41598-025-90833-3 |
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