The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues
Abstract Non-enzymatic modification of proteins by carbohydrates, known as glycation, leads to generation of advanced glycation end-products (AGEs). In our study we used in vitro generated AGEs to model glycation in vivo. We discovered in vivo analogs of unusual melibiose-adducts designated MAGEs (m...
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Nature Portfolio
2021
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oai:doaj.org-article:5e928347233642c5a6d161c60deb78d82021-12-02T10:44:14ZThe melibiose-derived glycation product mimics a unique epitope present in human and animal tissues10.1038/s41598-021-82585-72045-2322https://doaj.org/article/5e928347233642c5a6d161c60deb78d82021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-82585-7https://doaj.org/toc/2045-2322Abstract Non-enzymatic modification of proteins by carbohydrates, known as glycation, leads to generation of advanced glycation end-products (AGEs). In our study we used in vitro generated AGEs to model glycation in vivo. We discovered in vivo analogs of unusual melibiose-adducts designated MAGEs (mel-derived AGEs) synthesized in vitro under anhydrous conditions with bovine serum albumin and myoglobin. Using nuclear magnetic resonance spectroscopy we have identified MAGEs as a set of isomers, with open-chain and cyclic structures, of the fructosamine moiety. We generated a mouse anti-MAGE monoclonal antibody and show for the first time that the native and previously undescribed analogous glycation product exists in living organisms and is naturally present in tissues of both invertebrates and vertebrates, including humans. We also report MAGE cross-reactive auto-antibodies in patients with diabetes. We anticipate our approach for modeling glycation in vivo will be a foundational methodology in cell biology. Further studies relevant to the discovery of MAGE may contribute to clarifying disease mechanisms and to the development of novel therapeutic options for diabetic complications, neuropathology, and cancer.Magdalena StaniszewskaAgnieszka Bronowicka-SzydełkoKinga Gostomska-PampuchJerzy SzkudlarekArkadiusz BartyśTadeusz BiegElżbieta GamianAgata KochmanBolesław PicurJadwiga PietkiewiczPiotr KuropkaWiesław SzejaJerzy WiśniewskiPiotr ZiółkowskiAndrzej GamianNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021) |
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Medicine R Science Q Magdalena Staniszewska Agnieszka Bronowicka-Szydełko Kinga Gostomska-Pampuch Jerzy Szkudlarek Arkadiusz Bartyś Tadeusz Bieg Elżbieta Gamian Agata Kochman Bolesław Picur Jadwiga Pietkiewicz Piotr Kuropka Wiesław Szeja Jerzy Wiśniewski Piotr Ziółkowski Andrzej Gamian The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues |
| description |
Abstract Non-enzymatic modification of proteins by carbohydrates, known as glycation, leads to generation of advanced glycation end-products (AGEs). In our study we used in vitro generated AGEs to model glycation in vivo. We discovered in vivo analogs of unusual melibiose-adducts designated MAGEs (mel-derived AGEs) synthesized in vitro under anhydrous conditions with bovine serum albumin and myoglobin. Using nuclear magnetic resonance spectroscopy we have identified MAGEs as a set of isomers, with open-chain and cyclic structures, of the fructosamine moiety. We generated a mouse anti-MAGE monoclonal antibody and show for the first time that the native and previously undescribed analogous glycation product exists in living organisms and is naturally present in tissues of both invertebrates and vertebrates, including humans. We also report MAGE cross-reactive auto-antibodies in patients with diabetes. We anticipate our approach for modeling glycation in vivo will be a foundational methodology in cell biology. Further studies relevant to the discovery of MAGE may contribute to clarifying disease mechanisms and to the development of novel therapeutic options for diabetic complications, neuropathology, and cancer. |
| format |
article |
| author |
Magdalena Staniszewska Agnieszka Bronowicka-Szydełko Kinga Gostomska-Pampuch Jerzy Szkudlarek Arkadiusz Bartyś Tadeusz Bieg Elżbieta Gamian Agata Kochman Bolesław Picur Jadwiga Pietkiewicz Piotr Kuropka Wiesław Szeja Jerzy Wiśniewski Piotr Ziółkowski Andrzej Gamian |
| author_facet |
Magdalena Staniszewska Agnieszka Bronowicka-Szydełko Kinga Gostomska-Pampuch Jerzy Szkudlarek Arkadiusz Bartyś Tadeusz Bieg Elżbieta Gamian Agata Kochman Bolesław Picur Jadwiga Pietkiewicz Piotr Kuropka Wiesław Szeja Jerzy Wiśniewski Piotr Ziółkowski Andrzej Gamian |
| author_sort |
Magdalena Staniszewska |
| title |
The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues |
| title_short |
The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues |
| title_full |
The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues |
| title_fullStr |
The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues |
| title_full_unstemmed |
The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues |
| title_sort |
melibiose-derived glycation product mimics a unique epitope present in human and animal tissues |
| publisher |
Nature Portfolio |
| publishDate |
2021 |
| url |
https://doaj.org/article/5e928347233642c5a6d161c60deb78d8 |
| work_keys_str_mv |
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