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The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues

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-derive...

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Autores principales: Staniszewska, Magdalena, Bronowicka-Szydełko, Agnieszka, Gostomska-Pampuch, Kinga, Szkudlarek, Jerzy, Bartyś, Arkadiusz, Bieg, Tadeusz, Gamian, Elżbieta, Kochman, Agata, Picur, Bolesław, Pietkiewicz, Jadwiga, Kuropka, Piotr, Szeja, Wiesław, Wiśniewski, Jerzy, Ziółkowski, Piotr, Gamian, Andrzej
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7859244/
https://www.ncbi.nlm.nih.gov/pubmed/33536563
http://dx.doi.org/10.1038/s41598-021-82585-7
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author Staniszewska, Magdalena
Bronowicka-Szydełko, Agnieszka
Gostomska-Pampuch, Kinga
Szkudlarek, Jerzy
Bartyś, Arkadiusz
Bieg, Tadeusz
Gamian, Elżbieta
Kochman, Agata
Picur, Bolesław
Pietkiewicz, Jadwiga
Kuropka, Piotr
Szeja, Wiesław
Wiśniewski, Jerzy
Ziółkowski, Piotr
Gamian, Andrzej
author_facet Staniszewska, Magdalena
Bronowicka-Szydełko, Agnieszka
Gostomska-Pampuch, Kinga
Szkudlarek, Jerzy
Bartyś, Arkadiusz
Bieg, Tadeusz
Gamian, Elżbieta
Kochman, Agata
Picur, Bolesław
Pietkiewicz, Jadwiga
Kuropka, Piotr
Szeja, Wiesław
Wiśniewski, Jerzy
Ziółkowski, Piotr
Gamian, Andrzej
author_sort Staniszewska, Magdalena
collection PubMed
description 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.
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spelling pubmed-78592442021-02-04 The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues Staniszewska, Magdalena Bronowicka-Szydełko, Agnieszka Gostomska-Pampuch, Kinga Szkudlarek, Jerzy Bartyś, Arkadiusz Bieg, Tadeusz Gamian, Elżbieta Kochman, Agata Picur, Bolesław Pietkiewicz, Jadwiga Kuropka, Piotr Szeja, Wiesław Wiśniewski, Jerzy Ziółkowski, Piotr Gamian, Andrzej Sci Rep Article 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. Nature Publishing Group UK 2021-02-03 /pmc/articles/PMC7859244/ /pubmed/33536563 http://dx.doi.org/10.1038/s41598-021-82585-7 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Staniszewska, Magdalena
Bronowicka-Szydełko, Agnieszka
Gostomska-Pampuch, Kinga
Szkudlarek, Jerzy
Bartyś, Arkadiusz
Bieg, Tadeusz
Gamian, Elżbieta
Kochman, Agata
Picur, Bolesław
Pietkiewicz, Jadwiga
Kuropka, Piotr
Szeja, Wiesław
Wiśniewski, Jerzy
Ziółkowski, Piotr
Gamian, Andrzej
The melibiose-derived glycation product mimics a unique epitope present in human and animal tissues
title 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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7859244/
https://www.ncbi.nlm.nih.gov/pubmed/33536563
http://dx.doi.org/10.1038/s41598-021-82585-7
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