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      Role of Advanced Glycation End Products in Carcinogenesis and their Therapeutic Implications

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          Abstract

          Aging is one of the biggest risk factors for the major prevalent diseases such as cardiovascular diseases, neurodegeneration and cancer, but due to the complex and multifactorial nature of the aging process, the molecular mechanisms underlying age-related diseases are not yet fully understood. Research has been intensive in the last years aiming to characterize the pathophysiology of aging and develop therapies to fight age-related diseases. In this context advanced glycation end products (AGEs) have received attention. AGEs, when accumulated in tissues, significantly increase the level of inflammation in the body which has long been associated with the development of cancer. Here we discuss the classical settings promoting AGE formation, as well as reduction strategies, occurrence and relevance of AGEs in cancer tissues and the role of AGE-interaction with the receptor for advanced glycation end products (RAGE) in cancer initiation and progression.

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          Role of advanced glycation end products in cellular signaling☆

          Christiane Ott, Kathleen Jacobs, Elisa Haucke … (2014)
          Improvements in health care and lifestyle have led to an elevated lifespan and increased focus on age-associated diseases, such as neurodegeneration, cardiovascular disease, frailty and arteriosclerosis. In all these chronic diseases protein, lipid or nucleic acid modifications are involved, including cross-linked and non-degradable aggregates, such as advanced glycation end products (AGEs). Formation of endogenous or uptake of dietary AGEs can lead to further protein modifications and activation of several inflammatory signaling pathways. This review will give an overview of the most prominent AGE-mediated signaling cascades, AGE receptor interactions, prevention of AGE formation and the impact of AGEs during pathophysiological processes.
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            Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging.

            Richard Morimoto (2008)
            The long-term health of the cell is inextricably linked to protein quality control. Under optimal conditions this is accomplished by protein homeostasis, a highly complex network of molecular interactions that balances protein biosynthesis, folding, translocation, assembly/disassembly, and clearance. This review will examine the consequences of an imbalance in homeostasis on the flux of misfolded proteins that, if unattended, can result in severe molecular damage to the cell. Adaptation and survival requires the ability to sense damaged proteins and to coordinate the activities of protective stress response pathways and chaperone networks. Yet, despite the abundance and apparent capacity of chaperones and other components of homeostasis to restore folding equilibrium, the cell appears poorly adapted for chronic proteotoxic stress when conformationally challenged aggregation-prone proteins are expressed in cancer, metabolic disease, and neurodegenerative disease. The decline in biosynthetic and repair activities that compromises the integrity of the proteome is influenced strongly by genes that control aging, thus linking stress and protein homeostasis with the health and life span of the organism.
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              The Metabolism of Carcinoma Cells

              O WARBURG (1925)
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                Author and article information

                Journal
                Journal ID (nlm-ta): Curr Pharm Des
                Journal ID (iso-abbrev): Curr. Pharm. Des
                Journal ID (publisher-id): CPD
                Title: Current Pharmaceutical Design
                Publisher: Bentham Science Publishers
                ISSN (Print): 1381-6128
                ISSN (Electronic): 1873-4286
                Publication date (Electronic): December 2018
                Publication date (Print): December 2018
                Volume: 24
                Issue: 44
                Pages: 5245-5241
                Affiliations
                Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany;

                German Center for Diabetes Research (DZD), 85764 Muenchen- Neuherberg, , Germany;

                Leibniz Institute of Vegetable and Ornamental Crops Grossbeeren e.V. (IGZ), 14979 Grossbeeren;

                Institute of Food Chemistry, Hamburg School of Food Science, University of Hamburg , 20146, Hamburg , Germany
                Author notes
                [* ]Address correspondence to this author at the German Institute of Human Nutrition, Potsdam-Rehbruecke, Arthur-Scheunert-Allee 114-116, 14558 Nuthetal, Germany; Tel: 0049-3320088-2354;, E-mail: annika.hoehn@ 123456dife.de
                Article
                Publisher ID: CPD-24-5245
                DOI: 10.2174/1381612825666190130145549
                PMC ID: 6635609
                PubMed ID: 30706806
                SO-VID: 8782f2ae-f138-43ce-a2c9-78c45955fe68
                Copyright © © 2018 Bentham Science Publishers
                License:

                This is an open access article licensed under the terms of the Creative Commons Attribution-Non-Commercial 4.0 International Public License (CC BY-NC 4.0) ( https://creativecommons.org/licenses/by-nc/4.0/legalcode), which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

                History
                Date received : 21 December 2018
                Date accepted : 24 January 2019
                Categories
                Subject: Article

                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: advanced glycation end products,cancer,aging,inflammation,rage,cardiovascular diseases
                Data availability:
                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: advanced glycation end products, cancer, aging, inflammation, rage, cardiovascular diseases

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