Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal

Aćimović, Jelena M.; Stanimirovic, Bojana; Todorović, Nina; Jovanović, Vesna; Mandić, Ljuba M.

doi:10.1016/j.cbi.2010.07.013

Cited by 20 publications

(18 citation statements)

References 46 publications

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“…In contrary to glucose, after 30 min of incubation of HSA with MG guanidine, thiol and amino groups react in significant yield [30], and that opens possibilities for precise monitoring of the HSA molecule changes.…”

Section: Preparation Of Fas-free Hsa and Fas-bound Hsa Modified With Mgmentioning

confidence: 99%

“…MG has been suggested as a good marker for investigating the association between AGEs with adverse health outcomes [48]. During in vitro modification of HSA with MG the kinetics and levels of carbonylation of Lys amino, Arg guanidine and Cys34 thiol group were determined, and the crosslinking of protein molecules was detected [30]. The evidenced decrease of HSA-SH content in diabetes [14,49] could be the consequence of higher content of reactive oxygen species and a-oxoaldehydes and/or increasing reactivity/accessibility of the thiol group due to FAs binding.…”

Section: Influence Of Fas Bound To Hsa On Modification Of Hsa-sh Groumentioning

confidence: 99%

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Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal

Pavićević

Jovanović

Takić

et al. 2014

Chemico-Biological Interactions

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Section: Preparation Of Fas-free Hsa and Fas-bound Hsa Modified With Mgmentioning

confidence: 99%

Section: Influence Of Fas Bound To Hsa On Modification Of Hsa-sh Groumentioning

confidence: 99%

Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal

Pavićević

Jovanović

Takić

et al. 2014

Chemico-Biological Interactions

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“…31 The free sulydryl group content is a parameter of the redox state of the protein. 33 As a result the native functional properties of HSA may be changed due to the alteration in protein conformation. Average free sulydryl group content of three independent assay (mean AE SD).…”

Section: Thiol Group Estimationmentioning

confidence: 99%

Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

2015

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Early glycation involves attachment of glucose on 3-NH 2 of lysine residues. Human serum albumin (HSA), a lysine rich protein, is highly prone to non-enzymatic glycation. In this study, the effect of different concentrations of glucose on HSA through early glycation was assessed by various physicochemicaltechniques. An early glycation product Amadori HSA was estimated by colorimetric method, nitro blue tetrazolium (NBT) and thiobarbituric acid assay (TBA). The conformational changes were confirmed by UV-visible spectroscopy, tryptophan fluorescence quenching, circular dichroism (CD), and sodium dodecyl sulphate poly acrylamide gel electrophoresis (SDS-PAGE). Biochemical alterations in Amadori-HSA were analyzed by NaBH 4 reduction, increased carbonyl content and decrease in free lysine, arginine and sulfhydryl groups. Most studies have reported the structural changes in protein due to AGEs or Amadori protein at a particular glucose concentration; to the best of our knowledge, no reports have been published comparing the physicochemical changes in HSA due to early glycation within a range of glucose concentrations. In the present study, the investigations confirmed the structural and biochemical alterations in Amadori-HSA which is directly proportional to glucose concentration. This might interfere with the normal function of HSA and can contribute to the progression of diabetes and its associated complications. Amadori modified HSA might be used as a biomarker for early detection of diabetes and be beneficial in preventing the diabetic complications at early stages of diabetes. In this context, this study provides additional information about biochemical and biophysical changes occurring in Amadori-HSA within the glucose range upon early glycation.

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“…It was shown that the reactivity of the SH groups of the investigated thiols with MG decreased in the order cysteine>GSH>NAC [47]. Elsewhere, the scavenging activity of penicillamine toward the dicarbonyl phenylglyoxal was more efficacious than aminoguanidine under physiological conditions in vitro [32].…”

Section: Discussionmentioning

confidence: 96%

High throughput assay for evaluation of reactive carbonyl scavenging capacity

et al. 2014

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Many carbonyl species from either lipid peroxidation or glycoxidation are extremely reactive and can disrupt the function of proteins and enzymes. 4-hydroxynonenal and methylglyoxal are the most abundant and toxic lipid-derived reactive carbonyl species. The presence of these toxics leads to carbonyl stress and cause a significant amount of macromolecular damages in several diseases. Much evidence indicates trapping of reactive carbonyl intermediates may be a useful strategy for inhibiting or decreasing carbonyl stress-associated pathologies. There is no rapid and convenient analytical method available for the assessment of direct carbonyl scavenging capacity, and a very limited number of carbonyl scavengers have been identified to date, their therapeutic potential being highlighted only recently. In this context, we have developed a new and rapid sensitive fluorimetric method for the assessment of reactive carbonyl scavengers without involvement glycoxidation systems. Efficacy of various thiol- and non-thiol-carbonyl scavenger pharmacophores was tested both using this screening assay adapted to 96-well microplates and in cultured cells. The scavenging effects on the formation of Advanced Glycation End-product of Bovine Serum Albumin formed with methylglyoxal, 4-hydroxynonenal and glucose-glycated as molecular models were also examined. Low molecular mass thiols with an α-amino-β-mercaptoethane structure showed the highest degree of inhibitory activity toward both α,β-unsaturated aldehydes and dicarbonyls. Cysteine and cysteamine have the best scavenging ability toward methylglyoxal. WR-1065 which is currently approved for clinical use as a protective agent against radiation and renal toxicity was identified as the best inhibitor of 4-hydroxynonenal.

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Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal

Cited by 20 publications

References 46 publications

Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal

Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal

Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

High throughput assay for evaluation of reactive carbonyl scavenging capacity

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