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3-Deoxyglucosone: A Potential Glycating Agent Accountable for Structural Alteration in H3 Histone Protein through Generation of Different AGEs

Advanced glycation end-products (AGEs) are heterogeneous group of compounds, known to be implicated in diabetic complications. One of the consequences of the Maillard reaction is attributed to the production of reactive intermediate products such as α-oxoaldehydes. 3-deoxyglucosone (3-DG), an α-oxoa...

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Autores principales: Ashraf, Jalaluddin M., Ahmad, Saheem, Rabbani, Gulam, Hasan, Qambar, Jan, Arif Tasleem, Lee, Eun Ju, Khan, Rizwan Hasan, Alam, Khursheed, Choi, Inho
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4331494/
https://www.ncbi.nlm.nih.gov/pubmed/25689368
http://dx.doi.org/10.1371/journal.pone.0116804
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author Ashraf, Jalaluddin M.
Ahmad, Saheem
Rabbani, Gulam
Hasan, Qambar
Jan, Arif Tasleem
Lee, Eun Ju
Khan, Rizwan Hasan
Alam, Khursheed
Choi, Inho
author_facet Ashraf, Jalaluddin M.
Ahmad, Saheem
Rabbani, Gulam
Hasan, Qambar
Jan, Arif Tasleem
Lee, Eun Ju
Khan, Rizwan Hasan
Alam, Khursheed
Choi, Inho
author_sort Ashraf, Jalaluddin M.
collection PubMed
description Advanced glycation end-products (AGEs) are heterogeneous group of compounds, known to be implicated in diabetic complications. One of the consequences of the Maillard reaction is attributed to the production of reactive intermediate products such as α-oxoaldehydes. 3-deoxyglucosone (3-DG), an α-oxoaldehyde has been found to be involved in accelerating vascular damage during diabetes. In the present study, calf thymus histone H3 was treated with 3-deoxyglucosone to investigate the generation of AGEs (N(ε)-carboxymethyllysine, pentosidine), by examining the degree of side chain modifications and formation of different intermediates and employing various physicochemical techniques. The results clearly indicate the formation of AGEs and structural changes upon glycation of H3 by 3-deoxyglucosone, which may hamper the normal functioning of H3 histone, that may compromise the veracity of chromatin structures and function in secondary complications of diabetes.
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spelling pubmed-43314942015-02-24 3-Deoxyglucosone: A Potential Glycating Agent Accountable for Structural Alteration in H3 Histone Protein through Generation of Different AGEs Ashraf, Jalaluddin M. Ahmad, Saheem Rabbani, Gulam Hasan, Qambar Jan, Arif Tasleem Lee, Eun Ju Khan, Rizwan Hasan Alam, Khursheed Choi, Inho PLoS One Research Article Advanced glycation end-products (AGEs) are heterogeneous group of compounds, known to be implicated in diabetic complications. One of the consequences of the Maillard reaction is attributed to the production of reactive intermediate products such as α-oxoaldehydes. 3-deoxyglucosone (3-DG), an α-oxoaldehyde has been found to be involved in accelerating vascular damage during diabetes. In the present study, calf thymus histone H3 was treated with 3-deoxyglucosone to investigate the generation of AGEs (N(ε)-carboxymethyllysine, pentosidine), by examining the degree of side chain modifications and formation of different intermediates and employing various physicochemical techniques. The results clearly indicate the formation of AGEs and structural changes upon glycation of H3 by 3-deoxyglucosone, which may hamper the normal functioning of H3 histone, that may compromise the veracity of chromatin structures and function in secondary complications of diabetes. Public Library of Science 2015-02-17 /pmc/articles/PMC4331494/ /pubmed/25689368 http://dx.doi.org/10.1371/journal.pone.0116804 Text en © 2015 Ashraf et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Ashraf, Jalaluddin M.
Ahmad, Saheem
Rabbani, Gulam
Hasan, Qambar
Jan, Arif Tasleem
Lee, Eun Ju
Khan, Rizwan Hasan
Alam, Khursheed
Choi, Inho
3-Deoxyglucosone: A Potential Glycating Agent Accountable for Structural Alteration in H3 Histone Protein through Generation of Different AGEs
title 3-Deoxyglucosone: A Potential Glycating Agent Accountable for Structural Alteration in H3 Histone Protein through Generation of Different AGEs
title_full 3-Deoxyglucosone: A Potential Glycating Agent Accountable for Structural Alteration in H3 Histone Protein through Generation of Different AGEs
title_fullStr 3-Deoxyglucosone: A Potential Glycating Agent Accountable for Structural Alteration in H3 Histone Protein through Generation of Different AGEs
title_full_unstemmed 3-Deoxyglucosone: A Potential Glycating Agent Accountable for Structural Alteration in H3 Histone Protein through Generation of Different AGEs
title_short 3-Deoxyglucosone: A Potential Glycating Agent Accountable for Structural Alteration in H3 Histone Protein through Generation of Different AGEs
title_sort 3-deoxyglucosone: a potential glycating agent accountable for structural alteration in h3 histone protein through generation of different ages
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4331494/
https://www.ncbi.nlm.nih.gov/pubmed/25689368
http://dx.doi.org/10.1371/journal.pone.0116804
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