Analysis of glycated protein by capillary electrophoresis

Hinton, D.J.S.; Ames, Jennifer M.

doi:10.1016/s0531-5131(02)00953-6

Cited by 9 publications

(6 citation statements)

References 3 publications

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“…One current clinical assay based on an enzymatic method utilizes an albumin-specific proteinase (i.e., ketoamine oxidase) to digest glycated HSA, followed by treatment with a fructosaminase to oxidize the glycated amino acids and produce hydrogen peroxide, which is then measured [59–61]. Raman spectroscopy [63], refractive index measurements [64], capillary electrophoresis [65] and other electrophoretic methods [66,67] have also been explored as alternative techniques for measuring glycated albumin.…”

Section: Measurement Of Glycated Albuminmentioning

confidence: 99%

Review: Glycation of human serum albumin

Anguizola

Matsuda

Barnaby

et al. 2013

Clinica Chimica Acta

327

300

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Glycation involves the non-enzymatic addition of reducing sugars and/or their reactive degradation products to amine groups on proteins. This process is promoted by the presence of elevated blood glucose concentrations in diabetes and occurs with various proteins that include human serum albumin (HSA). This review examines work that has been conducted in the study and analysis of glycated HSA. The general structure and properties of HSA are discussed, along with the reactions that can lead to modification of this protein during glycation. The use of glycated HSA as a short-to-intermediate term marker for glycemic control in diabetes is examined, and approaches that have been utilized for measuring glycated HSA are summarized. Structural studies of glycated HSA are reviewed, as acquired for both in vivo and in vitro glycated HSA, along with data that have been obtained on the rate and thermodynamics of HSA glycation. In addition, this review considers various studies that have investigated the effects of glycation on the binding of HSA with drugs, fatty acids and other solutes and the potential clinical significance of these effects.

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Section: Measurement Of Glycated Albuminmentioning

confidence: 99%

Review: Glycation of human serum albumin

Anguizola

Matsuda

Barnaby

et al. 2013

Clinica Chimica Acta

327

300

View full text Add to dashboard Cite

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“…In terms of the gel-based approach, protein mixtures can be separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS-PAGE) [ 87 , 167 , 168 ] or by two-dimensional gel electrophoresis (2D-GE) [ 169 , 170 , 171 , 172 , 173 ], with subsequent digestion of the proteins representing individual electrophoretic zones followed by MS or/and MS/MS analysis of resulted hydrolysates. In contrast, LC-based approach relies on limited enzymatic proteolysis of complex protein mixtures (such as cell lysates or tissue extracts) with subsequent separation of resulted hydrolytic peptides by RP-HPLC [ 52 , 174 , 175 ] or capillary electrophoresis (CE) [ 176 , 177 ] with on-line mass spectrometric detection [ 114 , 177 ].…”

Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

Maillard Proteomics: Opening New Pages

Soboleva

Schmidt

Vikhnina

et al. 2017

IJMS

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Protein glycation is a ubiquitous non-enzymatic post-translational modification, formed by reaction of protein amino and guanidino groups with carbonyl compounds, presumably reducing sugars and α-dicarbonyls. Resulting advanced glycation end products (AGEs) represent a highly heterogeneous group of compounds, deleterious in mammals due to their pro-inflammatory effect, and impact in pathogenesis of diabetes mellitus, Alzheimer’s disease and ageing. The body of information on the mechanisms and pathways of AGE formation, acquired during the last decades, clearly indicates a certain site-specificity of glycation. It makes characterization of individual glycation sites a critical pre-requisite for understanding in vivo mechanisms of AGE formation and developing adequate nutritional and therapeutic approaches to reduce it in humans. In this context, proteomics is the methodology of choice to address site-specific molecular changes related to protein glycation. Therefore, here we summarize the methods of Maillard proteomics, specifically focusing on the techniques providing comprehensive structural and quantitative characterization of glycated proteome. Further, we address the novel break-through areas, recently established in the field of Maillard research, i.e., in vitro models based on synthetic peptides, site-based diagnostics of metabolism-related diseases (e.g., diabetes mellitus), proteomics of anti-glycative defense, and dynamics of plant glycated proteome during ageing and response to environmental stress.

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“…The concentration of GA can be directly measured by several methods, including boronate affinity chromatography, ion exchange chromatography, high performance liquid chromatography and immunoassays (eg, enzyme-linked immunosorbent assays or radioimmunoassays). A number of alternative methods have been developed, including Raman spectroscopy, 17 refractive index measurements, 18 capillary electrophoresis, 19 and other electrophoretic techniques, 20 but their usefulness in clinical practice has been challenged by requirements for dedicated instrumentation and poor analytical performance. Recently, a user-friendly, highly accurate and automated enzymatic assay (Lucica GA-L kit, Asahi Kasei Pharma, Tokyo, Japan) has been developed.…”

Section: Biochemistry and Biology Of Fructosamine And Glycated Albuminmentioning

confidence: 99%

Advantages and Pitfalls of Fructosamine and Glycated Albumin in the Diagnosis and Treatment of Diabetes

Danese

Montagnana

Nouvenne

et al. 2015

J Diabetes Sci Technol

152

130

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Diabetes is one of the most severe and frequent human disorders. According to recent statistics, this condition afflicts as many as 382 million persons around the globe, with an estimated prevalence of approximately 8.3% in 2013. At variance with other frequent pathologies such as cardiovascular disease and bacterial infections, the trend toward an increased prevalence is not expected to soon reverse. Worldwide, as many as 592 million individuals may be affected by diabetes in 2035, a remarkable 55% increase in prevalence over the next 2 decades. 1 Due to its high global prevalence and severe, frequently life-threatening complications (eg, retinopathy, nephropathy, neuropathy, cardiovascular disease), diabetes must be regarded as a serious and increasing global health burden. The most recent Standards of Medical Care in Diabetes published by the American Diabetes Association (ADA) emphasize that early diagnosis and monitoring are critical for preventing or delaying the onset of acute complications and lowering the risk of long-term complications of diabetes. 2 The current diagnostic criteria for this condition are based on the presence of (1) glycated hemoglobin (HbA1c) value ≥6.5% (ie, ≥48 mmol/mol), (2) fasting plasma glucose (FPG) ≥126 mg/dL (ie, ≥7.0 mmol/L), (3) 2-hour plasma glucose ≥200 mg/dL (ie, ≥11.1 mmol/L) during an oral glucose tolerance test (OGTT) using a 75 g glucose load, or (4) random plasma glucose ≥200 mg/dL (ie, ≥11.1 mmol/L). An increased risk of diabetes (ie, prediabetes) is defined in the presence of (1) HbA1c value between 5.7-6.4% (ie, 39-46 mmol/mol), (2) FPG between 100-126 mg/dL (ie, 5.6-6.9 mmol/L), (3) 2-hour plasma glucose between 140-199 mg/ dL (ie, 7.8-11.0 mmol/L) during an OGTT. With regard to diabetes monitoring, the glycemic targets for nonpregnant adults with diabetes include HbA1c value <7.0% (ie, <53 mmol/mol), preprandial capillary plasma glucose between 567227D STXXX10.

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Analysis of glycated protein by capillary electrophoresis

Cited by 9 publications

References 3 publications

Review: Glycation of human serum albumin

Review: Glycation of human serum albumin

Maillard Proteomics: Opening New Pages

Advantages and Pitfalls of Fructosamine and Glycated Albumin in the Diagnosis and Treatment of Diabetes

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