Effect of Cu(<scp>ii</scp>) on in vitro glycation of human serum albumin by methylglyoxal: a LC-MS-based proteomic approach

Segovia, Alejandra Sarahi Ramirez; Wróbel, Katarzyna; Aguilar, Francisco Javier Acevedo; Escobosa, Alma Rosa Corrales

doi:10.1039/c6mt00235h

Cited by 11 publications

(2 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In in vitro, proteomics study, it was found that elevated protein glycation might be associated with Cu deficiency and with excessive Cu(II) concentrations [ 52 ]. The data from clinical studies on diabetic patients are contradictory.…”

Section: Discussionmentioning

confidence: 99%

The Relationship between Dietary, Serum and Hair Levels of Minerals (Fe, Zn, Cu) and Glucose Metabolism Indices in Obese Type 2 Diabetic Patients

Król

Bogdański

Suliburska

et al. 2018

Biol Trace Elem Res

View full text Add to dashboard Cite

The aim of this study was to assess the levels of Zn, Fe and Cu in the serum and hair, and dietary intake of type 2 diabetic patients and their association with glucose and lipid indices. The study was conducted on 62 people aged 40-78 years (31 diabetic patients and 31 healthy subjects, who were the control group). The content of trace elements in the hair and serum was analysed with the AAS method. The serum insulin, HbA1c, glucose, total cholesterol and triacylglycerol concentrations were measured by means of RIA, HPLC and colorimetric methods, respectively. The diabetic patients were found to have significantly higher dietary iron intake, higher hair Fe and lower serum Zn concentrations than the non-diabetic subjects, while the hair Zn and Cu contents were comparable in both groups. The serum Zn and Cu levels of the diabetic subjects were negatively correlated with the serum glucose, the serum Zn and Cu/Zn ratio was inversely correlated with the serum total cholesterol and the serum insulin level was positively associated with the hair Cu/Zn ratio. The results of this study indicate that the trace element status (Zn, Fe, Cu), as reflected in the blood serum and hair, may be disturbed due to metabolic derangement occurring in diabetes.

show abstract

Section: Discussionmentioning

confidence: 99%

The Relationship between Dietary, Serum and Hair Levels of Minerals (Fe, Zn, Cu) and Glucose Metabolism Indices in Obese Type 2 Diabetic Patients

Król

Bogdański

Suliburska

et al. 2018

Biol Trace Elem Res

View full text Add to dashboard Cite

show abstract

“…В организме концентрации изучаемых металлов вариабельны. Так, физиологические концентрации меди и цинка в сыворотке здоровых людей составляют ~1 мг/л (~15,7 мкМ и ~15,3 мкМ соответственно) [31,32]. В то же время сообщается о значительно более высокой концентрации меди в амилоидных бляшках при болезни Альцгеймера (~400 мкМ) [10,25].…”

Section: Introductionunclassified

Influence of Certain D-Metals on Formation of Advanced Glycation End Products, Aggregation and Amyloid Transformation of Albumin in Glycation Reaction

Litvinov

Гонтарева

Усмиянова

et al. 2021

Farm. farmakol. (Pâtigorsk)

View full text Add to dashboard Cite

The aim of the research is to investigate the influence of the factor of the glycation behavior of bovine serum albumin (BSA) by glucose, and the factor of d-metal cations (nickel (II), cobalt (II), iron (II), iron (III), copper (II) or zinc (II)) presence, on the process of aggregation and the amyloid transformation of BSA and, therefore, to establish the effect of these cations on the rate of the formation of advanced glycation end products (AGEs), and the intensity of fluorescence of the amino acids tyrosine and tryptophan.Materials and methods. Reagents in the glycation are: glucose (at the final concentration of 0.36 M), BSA (at the final concentration of 1 mg/ml), deionized water, one of the d-metal cations, i. e. nickel (II), cobalt (II), iron (II), iron (III), copper (II) or zinc (II) (in the form of chloride, sulfate or nitrate salts, at the final concentration of 40 μM). The conditions for the glycation reaction are the incubation for 24 hours at the temperature of 60°C. The influence of two factors (the factor of the glycation reaction and the factor of a d-metal ion presence in the reaction medium) on the concentration of glycation end products (AGEs) formed during the glycation reaction, on the fluorescence intensity of the amino acids tryptophan and tyrosine, on the aggregation of BSA, and on the ability of BSA to the amyloid transformation under the described conditions, have been studied.Results. It was found out that the studied factors have a statistically significant effect on the considered parameters. The highest activity was found for the copper ion (II), which intensifies the formation of the AGEs in the samples where glycation occurs, reduces the fluorescence intensity of the amino acids’ tryptophan and tyrosine (independently and increasing the effect against the background of glycation). Besides, it independently causes the aggregation of BSA hereby intensifying the effect against the background of glycation, it independently causes the amyloid transformation of BSA enhancing the effect against the background of glycation. The above-listed effects were the least pronounced in the reaction media with the addition of nickel (II) or cobalt (II). These cations reduce the rate of the AGEs formation, do not cause the formation of protein aggregates. In the presence of glucose, nickel (II) weakly suppresses the fluorescence intensity of tryptophan and tyrosine, and slightly enhances the amyloid transformation of BSA. Cobalt (II) slightly inhibits the amyloid transformation of BSA. In terms of the severity and nature of the effects, the iron (II), iron (III) and zinc (II) cations occupy an intermediate position between copper (II), on the one hand, and nickel (II) and cobalt (II), on the other hand, combining the influence on the AGEs formation, the intensity of fluorescence of tryptophan and tyrosine, the aggregation and amyloid transformation of BSA. In the absence of glucose, the ability of zinc (II) to induce the formation of protein aggregates turned out to be the highest, and its ability to stimulate the amyloid transformation of BSA corresponded to that of copper (II).Conclusion. The presence of d-metal cations affects the rate of the AGEs formation in the glycation reaction, affects the rate of the BSA amyloid transformation and the protein aggregates formation. Among such ions as nickel (II), cobalt (II), iron (II), iron (III), copper (II) and zinc (II), copper (II) ions turned out to be the most active in their ability to accelerate the AGEs formation, suppress the fluorescence of tryptophan and tyrosine, enhance the aggregation and amyloid transformation of BSA in the glycation reaction. The least manifestation of these properties is observed for nickel (II) and cobalt (II) ions.

show abstract

Interplay of Metal Ions and Posttranslational Modifications in Proteins

Peana,

Frączyk,

Zoroddu

2024

Eur J Inorg Chem

View full text Add to dashboard Cite

Posttranslational modifications (PTMs) and metal ions are integral players in the complex regulatory orchestra governing protein function. Several metal ions, including zinc, iron, copper, and others, intricately influence protein structure and activity as cofactors. Concurrently, PTMs, such as phosphorylation, acetylation, and ubiquitination, add an additional layer of complexity to the proteome, dynamically shaping cellular responses. Understanding this bidirectional relationship is crucial for unraveling the complex web of cellular regulation. This review explores the reciprocal impact of metal ions on PTMs and vice versa and provides examples and insights into how metal ions modulate PTMs and, conversely, how PTMs influence metal‐binding proteins, shedding light on the complex crosstalk between these two crucial facets of cellular biology. This interplay is not only central to cellular homeostasis but also holds implications for diseases associated with dysregulated metal‐ion and PTM processes.

show abstract

Effect of Cu(ii) on in vitro glycation of human serum albumin by methylglyoxal: a LC-MS-based proteomic approach

Cited by 11 publications

References 41 publications

The Relationship between Dietary, Serum and Hair Levels of Minerals (Fe, Zn, Cu) and Glucose Metabolism Indices in Obese Type 2 Diabetic Patients

The Relationship between Dietary, Serum and Hair Levels of Minerals (Fe, Zn, Cu) and Glucose Metabolism Indices in Obese Type 2 Diabetic Patients

Influence of Certain D-Metals on Formation of Advanced Glycation End Products, Aggregation and Amyloid Transformation of Albumin in Glycation Reaction

Interplay of Metal Ions and Posttranslational Modifications in Proteins

Contact Info

Product

Resources

About