Zinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity

Tupe, Rashmi S.; Kulkarni, Amruta; Adeshara, Krishna; Sankhe, Neena M.; Shaikh, Shamim; Dalal, Sayli; Bhosale, S.H.; Gaikwad, Sushama M.

doi:10.1016/j.ijbiomac.2015.05.028

Cited by 18 publications

(11 citation statements)

References 44 publications

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“…Numerous investigations have indicated protective effects of zinc supplementation against AGEs generation, glycation and AGEs‐induced harmful agents. Tupe et al investigated the effects of zinc on in vitro non‐enzymatic glycation of albumin by diabetic levels of glucose. They reported that albumin incubated with glucose had significantly higher levels of glycation markers including AGEs.…”

Section: Effect Of Zinc Supplementation On Age Generation and Age‐indmentioning

confidence: 99%

“…It has been reported that zinc administration before glycation of proteins is accompanied by intense inhibition of AGEs formation compared with zinc added after glycation . Therefore, it appears that zinc inhibit AGE formation via inhibition of protein glycation.…”

Section: Possible Mechanistic Model Of Zinc In the Inhibition Of Agesmentioning

confidence: 99%

“…Multiple evidence has indicated the protective effects of zinc against several chronic diseases such as diabetes . Numerous in vitro and animal model studies have demonstrated the anti‐glycation impact of zinc …”

Section: Introductionmentioning

confidence: 99%

“…8,9 Numerous in vitro and animal model studies have demonstrated the anti-glycation impact of zinc. 10,11 Despite the large number of important researches, zinc has not been applied as a therapeutic intervention in humans in part due to the fact that information on its anti-glycation effects has not been yet summarized. Therefore, the present study was undertaken to organize the effects of zinc on the formation of AGEs.…”

Section: Introductionmentioning

confidence: 99%

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Zinc against advanced glycation end products

Kheirouri

Alizadeh

Maleki

2018

Clin Exp Pharma Physio

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Summary Advanced glycation end products (AGEs) are destructive compounds with pathogenic importance in age‐related chronic diseases. Zinc has antioxidant, anti‐inflammatory and anti‐apoptotic potential. This study aimed to summarize effects of zinc on AGE formation and AGE‐induced damaging agents. Pubmed, Google scholar, Web of Sciences, and Scopus databases were searched. There was no limitation for publication date. English language original articles (in vitro, experimental and human studies) which examined the effect of external zinc on AGE formation, AGE‐induced apoptosis, or oxidative stress in mammals were included. To review the effect of zinc on AGE generation, the search keywords were as follows: “zinc” in title and “AGEs” or “methylglyoxal” or “pentosidine” or “carboxymethyllysine” or “glucosylation” or “carbonyl stress” or “AGEs‐induced apoptosis or oxidative stress or inflammation” in title/abstract. In total, 90 titles and abstracts were identified. Fifty‐two studies were screened after duplicates were removed. Six articles were chosen for review following analysis of both titles and summaries. Finally, based on intensive critical appraisal, 5 articles were included in the study. The evidence presented indicates that zinc has anti‐glycation, anti‐oxidative and anti‐apoptotic effects. Zinc insufficiency may stimulate AGEs formation. Whereas, zinc supplementation could inhibit formation of AGEs, AGE‐induced cell apoptosis and oxidative stress status, and protein carbonyl formation possibly through various signalling pathways.

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Section: Effect Of Zinc Supplementation On Age Generation and Age‐indmentioning

confidence: 99%

Section: Possible Mechanistic Model Of Zinc In the Inhibition Of Agesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Zinc against advanced glycation end products

Kheirouri

Alizadeh

Maleki

2018

Clin Exp Pharma Physio

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“…Evidence that zinc sulfate exerts in vitro inhibitory effect on BSA glycation has been documented (Tupe et al, 2015), while its supplementation reduces protein glycation and protein carbonyl formation in diabetic (Sacan et al, 2016) and protein malnourished (Adebayo et al, 2014) rats, which suggest that ZnSO 4 may improve Data are presented as mean ± SD of triplicate values. Different letters "a", "b", "c" and "d" mean that the value of one treatment group is significantly (p < .05) different from the other at a given treatment concentration and/or when compared to the controls peripheral tissues by insulin contributes to glycemic control in both normal and diabetic conditions (Aronoff et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Zinc(II) mineral increased the in vitro, cellular and ex vivo antihyperglycemic and antioxidative pharmacological profile of p‐hydroxybenzoic acid upon complexation

et al. 2021

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In this study, zinc was complexed with p-hydroxybenzoic acid to synthesize a complex with improved pharmacological profile. Proton NMR and FTIR analysis were used to characterize the complex. Several in vitro, cellular and ex vivo antihyperglycemic and antioxidative assays were used to evaluate the potency of the complex, relative to its precursors, while molecular docking was used to investigate interactions with insulin signaling targets (GLUT-4 and PKB). Also, the cytotoxicity of the complex was evaluated in Chang liver cells and L-6 myotubes using MTT assay. Complexation was through a Zn(O 4) coordination. This afforded the complex two moieties of phydroxybenzoic acid, which influenced its activities. While the complex retained the α-glucosidase and α-amylase inhibitory activity of its phenolic acid precursor, compl

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Communal interaction of glycation and gut microbes in diabetes mellitus, Alzheimer's disease, and Parkinson's disease pathogenesis

Patil,

Tupe

2023

Medicinal Research Reviews

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Diabetes and its complications, Alzheimer's disease (AD), and Parkinson's disease (PD) are increasing gradually, reflecting a global threat vis‐à‐vis expressing the essentiality of a substantial paradigm shift in research and remedial actions. Protein glycation is influenced by several factors, like time, temperature, pH, metal ions, and the half‐life of the protein. Surprisingly, most proteins associated with metabolic and neurodegenerative disorders are generally long‐lived and hence susceptible to glycation. Remarkably, proteins linked with diabetes, AD, and PD share this characteristic. This modulates protein's structure, aggregation tendency, and toxicity, highlighting renovated attention. Gut microbes and microbial metabolites marked their importance in human health and diseases. Though many scientific shreds of evidence are proposed for possible change and dysbiosis in gut flora in these diseases, very little is known about the mechanisms. Screening and unfolding their functionality in metabolic and neurodegenerative disorders is essential in hunting the gut treasure. Therefore, it is imperative to evaluate the role of glycation as a common link in diabetes and neurodegenerative diseases, which helps to clarify if modulation of nonenzymatic glycation may act as a beneficial therapeutic strategy and gut microbes/metabolites may answer some of the crucial questions. This review briefly emphasizes the common functional attributes of glycation and gut microbes, the possible linkages, and discusses current treatment options and therapeutic challenges.

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Zinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity

Cited by 18 publications

References 44 publications

Zinc against advanced glycation end products

Zinc against advanced glycation end products

Zinc(II) mineral increased the in vitro, cellular and ex vivo antihyperglycemic and antioxidative pharmacological profile of p‐hydroxybenzoic acid upon complexation

Communal interaction of glycation and gut microbes in diabetes mellitus, Alzheimer's disease, and Parkinson's disease pathogenesis

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