Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidant activity

Jakuš, Vladimír; Hrnciarová, M; Čársky, J; Krahulec, B; Rietbrock, N.

doi:10.1016/s0024-3205(99)00462-2

Cited by 50 publications

(24 citation statements)

References 6 publications

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“…1 clearly reveals that captopril was capable of inhibiting AGEs formation when assessed by fluorometry. This finding is in harmony with previous report consuming HSA/glucose system [35] instead of BSA/G6Psystem used in this study. Moreover, this figure exhibits comparative sight of the inhibitory effect of captopril to the aminoguanidine, the distinguished AGEs inhibitor [27,35,36].…”

Section: Discussionsupporting

confidence: 94%

Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus

Mariee

Al‐Shabanah

2006

Journal of Pharmaceutical and Biomedical Analysis

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Section: Discussionsupporting

confidence: 94%

Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus

Mariee

Al‐Shabanah

2006

Journal of Pharmaceutical and Biomedical Analysis

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“…The inhibitory activities against AGE formation of various vitamin B1 and B6 derivatives such as pyridoxamine (Khalifah et al 1999;Metz et al 2003;Voziyan et al 2002) and thiamine pyrophosphate (Booth et al 1997) have mainly been attributed to their abilities to scavenge reactive carbonyl compounds (Ahmed et al 2005a;Voziyan et al 2002). In addition, penicillamine could reduce the level of AGEs through decreasing the formation of Amadori products (Jakus et al 1999;Keita et al 1992).…”

Section: Anti-age Therapiesmentioning

confidence: 99%

Advanced glycation End-products (AGEs): an emerging concern for processed food industries

et al. 2015

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The global food industry is expected to increase more than US $ 7 trillion by 2014. This rise in processed food sector shows that more and more people are diverging towards modern processed foods. As modern diets are largely heat processed, they are more prone to contain high levels of advanced glycation end products (AGEs). AGEs are a group of complex and heterogeneous compounds which are known as brown and fluorescent cross-linking substances such as pentosidine, non-fluorescent cross-linking products such as methylglyoxal-lysine dimers (MOLD), or non-fluorescent, non-cross linking adducts such as carboxymethyllysine (CML) and pyrraline (a pyrrole aldehyde). The chemistry of the AGEs formation, absorption and bioavailability and their patho-biochemistry particularly in relation to different complications like diabetes and ageing discussed. The concept of AGEs receptor -RAGE is mentioned. AGEs contribute to a variety of microvascular and macrovascular complications through the formation of cross-links between molecules in the basement membrane of the extracellular matrix and by engaging the receptor for advanced glycation end products (RAGE). Different methods of detection and quantification along with types of agents used for the treatment of AGEs are reviewed. Generally, ELISA or LC-MS methods are used for analysis of foods and body fluids, however lack of universally established method highlighted. The inhibitory effect of bioactive components on AGEs by trapping variety of chemical moieties discussed. The emerging evidence about the adverse effects of AGEs makes it necessary to investigate the different therapies to inhibit AGEs.

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“…Garcinol, a benzophenone derivative in fruit rind, and extracts from several other plant tissues show glycation-inhibitory properties in a bovine serum albumin/fructose model system (134,135). Penicillamine also inhibits the formation of Amadori adducts when human serum albumin is incubated in the presence of 20 mM glucose (136). The soy flavinoid genistein prevents LDL peroxidation mediated by glycated LDL, although it does not affect the formation of glycated LDL (137).…”

Section: Therapeutic Implicationsmentioning

confidence: 99%

Amadori-modified glycated serum proteins and accelerated atherosclerosis in diabetes: Pathogenic and therapeutic implications

Cohen

Ziyadeh

Chen

2006

Journal of Laboratory and Clinical Medicine

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Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidant activity

Cited by 50 publications

References 6 publications

Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus

Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus

Advanced glycation End-products (AGEs): an emerging concern for processed food industries

Amadori-modified glycated serum proteins and accelerated atherosclerosis in diabetes: Pathogenic and therapeutic implications

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