Cytotoxic Effect of Advanced Glycation end Products

Boyanova, Maya; Huppertz, Berthold

doi:10.1080/13102818.2009.10817615

Cited by 8 publications

(9 citation statements)

References 39 publications

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“…The observed effects included: Condensation of chromatin, formation of apoptotic bodies and elevated expression of cytokeratin 18 and Caspase 3. It was concluded that BSA-AGE had a direct toxic effect on the cell viability in a time and dose-dependent manner, and that some pregnancy complications may arise due to the formation of AGEs ( 5 ).…”

Section: Cytotoxicity Of Agesmentioning

confidence: 99%

“…Incubation of proteins with lipid peroxidation products is an alternative method of generating AGEs. The polyol pathway leads to the conversion of glucose into fructose, and also promotes glycation; fructose may further be converted to 3-deoxyglucose and fructose-3-phosphate, both of which are very potent nonenzymatic glycation agents (5)(6)(7). Detailed information on AGE formation is reviewed elsewhere (8)(9)(10)(11).…”

Section: Introductionmentioning

confidence: 99%

“…Upon binding to receptors, AGEs activate several signalling pathways, including NF-κB, MAPKs, and Jun N-terminal kinase, which regulate the transcription of proteins, such as cytokines, chemokines, growth factors, adhesion molecules and extracellular matrix proteins. In doing so, AGEs can result alter chemotaxis, angiogenesis, oxidative stress, cell proliferation and programmed cell death ( 5 , 7 ).…”

Section: Introductionmentioning

confidence: 99%

“…AGE molecules (free, peptide-bound and protein-bound) are found in the blood plasma in high concentrations, particularly in diabetic patients. This is explained by their high concentration of the substrates; glucose and its derivatives in blood ( 5 ). AGEs are also found in aging patients and those with degenerative diseases, where AGEs accumulate in cells and tissues, such as arteries, neurons and hepatocytes ( 6 ).…”

Section: Introductionmentioning

confidence: 99%

“…AGEs may also be considered glycotoxins, due to their toxic effects on certain cells and tissues ( 5 ). The term ‘TAGE’ is the abbreviation for toxic advanced glycation end-products, which applies to some (AGE-2, AGE-3 and AA-AGE), but not all AGEs.…”

Section: Introductionmentioning

confidence: 99%

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Toxicity of advanced glycation end products (Review)

Kuzan

2021

Biomed Rep

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Advanced glycation end-products (AGEs) are proteins or lipids glycated nonenzymatically by glucose, or other reducing sugars and their derivatives, such as glyceraldehyde, glycolaldehyde, methyloglyoxal and acetaldehyde. There are three different means of AGE formation: i) Maillard reactions, the polyol pathway and lipid peroxidation. AGEs participate in the pathological mechanisms underlying the development of several diseases, such as diabetes and its complications, retinopathy or neuropathy, neurological disorders (for example, Parkinson's disease and Alzheimer's disease), atherosclerosis, hypertension and several types of cancer. AGE levels are increased in patients with hyperglycaemia, and is likely the result of the high concentration of glycation substrates circulating in the blood. The present review summarises the formation and nomenclature of advanced glycation end-products, with an emphasis on the role of AGEs in the development of diabetes, neurological disorders, as well as in cancer and other pathologies. A particular focus is placed on the functions of toxic AGEs. Additionally, studies which have shown the cytotoxicity of glycated albumin and other AGEs are also discussed. Finally, the diagnostic relevance of AGEs as well as for targeting in therapeutic strategies are highlighted.

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Section: Cytotoxicity Of Agesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Toxicity of advanced glycation end products (Review)

Kuzan

2021

Biomed Rep

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Glycation promotes the formation of genotoxic aggregates in glucose oxidase

2011

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This study investigates the effect of pentose sugars (ribose and arabinose) on the structural and chemical modifications in glucose oxidase (GOD) as well as genotoxic potential of this modified form. An intermediate state of GOD was observed on day 12 of incubation having CD minima peaks at 222 and 208 nm, characteristic of α-helix and a few tertiary contacts with altered tryptophan environment and high ANS binding. All these features indicate the existence of molten globule state of the GOD with ribose and arabinose on day 12. GOD on day 15 of incubation forms β structures as revealed by CD and FTIR which may be due to its aggregation. Furthermore, GOD on day 15 showed a remarkable increase in Thioflavin T fluorescence at 485 nm. Comet assay of lymphocytes and plasmid nicking assay in presence of glycated GOD show DNA damage which confirmed the genotoxicity of advance glycated end products. Hence, our study suggests that glycated GOD results in the formation of aggregates and the advanced glycated end products, which are genotoxic in nature.

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Effect of Non-Enzymatic Glycation on Cystatin: A Spectroscopic Study

et al. 2014

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The study shows the effect of nonenzymatic glycation on conformation and inhibitory activity of chick pea cystatin (CPC). CPC was incubated with different reducing sugars, pentose (D-Ribose), hexoses (D-Glucose, D-Fructose) at 37 °C for 5 weeks. To evaluate the modification of CPC by these different sugars during the glycation process the extent of the Maillard reaction, conformational, structural and functional changes were investigated. The behaviour of glycated CPC was monitored by the techniques of UV and fluorescence spectroscopies. Specific fluorescence was employed to characterise the glycation and AGEs. The anti-papain activity of glycated CPC was found to be significantly lower as compared to its non-glycated form. Glycation with ribose led to maximum loss in inhibitory activity. It was found that the incubation of CPC with all the mentioned sugars led to a parallel increase in tryptophan fluorescence as well as in Maillard and other AGEs specific fluorescence values and hyperchromicity in the UV-region. Among the sugars studied comparatively ribose was found to be the most active in inducing structural and conformational alterations in the protein suggesting its high reactivity with protein amino groups.

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Cytotoxic Effect of Advanced Glycation end Products

Cited by 8 publications

References 39 publications

Toxicity of advanced glycation end products (Review)

Toxicity of advanced glycation end products (Review)

Glycation promotes the formation of genotoxic aggregates in glucose oxidase

Effect of Non-Enzymatic Glycation on Cystatin: A Spectroscopic Study

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