Low Plasma Albumin Levels Are Associated with Increased Plasma Protein Glycation and HbA1c in Diabetes

Bhonsle, Hemangi S.; Korwar, Arvind M.; Kote, Sachin; Golegaonkar, Sandeep B.; Chougale, Ashok D.; Shaik, Mahemud L.; Dhande, Nitin L.; Giri, Ashok P.; Shelgikar, K.M.; Boppana, Ramanamurthy; Kulkarni, Mahesh J.

doi:10.1021/pr201030m

Cited by 69 publications

(59 citation statements)

References 23 publications

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“…In addition, as there was no change in plasma glucose concentrations from feeding a protein-free diet, the increase in the ratio of glycoalbumin to albumin might be due to both an increase in plasma glycoalbumin and a decrease in plasma albumin by feeding the CP 0% diet. A similar phenomenon was reported where low level of albumin was associated with an increase in plasma HbA1c (Bhonsle et al, 2012), which supports the results derived from the present study.…”

Section: Discussionsupporting

confidence: 93%

Influence of Varying Dietary Protein Levels on Glycation of Albumin, Tryptophan and Valine in the Plasma of Chickens

et al. 2017

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Glycation is a chemical reaction in which reducing sugars bind non-enzymatically to compounds containing amino groups. Avian species like chickens are hyperglycemic animals and have high body temperature compared to mammalian species, which enables avian species to accelerate the glycation of proteins and amino acids with glucose. Although varying dietary crude protein (CP) levels alter plasma concentrations of proteins and amino acids, the influence of varying CP levels on the glycation of plasma proteins and amino acids has not been studied so far. In the present study, therefore, glycation of albumin, tryptophan and valine in the plasma of chickens fed diets with varying CP levels (0, 10, 20, 40 and 60%) was examined. At the end of the experimental period, blood samples were collected and plasma concentrations of glycoalbumin, glycated tryptophan (tryptophan-Amadori product and (1R, 3S) -1 -(D -gluco -1, 2, 3, 4, 5 -pentahydroxypentyl) -1, 2, 3, 4 -tetrahydro -β -carboline -3 -carboxylic acid (PHP-THβC)), and valine-Amadori product were measured. Although plasma albumin concentration was reduced along with the decrease in dietary CP levels from 20% to 0%, glycoalbumin in the plasma was increased under such dietary conditions. Similar increase in the ratios of tryptophan-Amadori product to tryptophan and valine-Amadori product to valine in the plasma of chickens fed a protein-free diet was observed. These results suggest that dietary protein deficiency might enhance the non-enzymatic glycation of plasma proteins and amino acids in chickens.

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Section: Discussionsupporting

confidence: 93%

Influence of Varying Dietary Protein Levels on Glycation of Albumin, Tryptophan and Valine in the Plasma of Chickens

et al. 2017

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“…AGE-HSA reflects glycemic status over the preceding 3-4 weeks and has been recommended in gestational diabetes (12). In diabetes, the levels of AGE-HSA increase and were found to be positively correlated with hyperglycemia (13,14). In addition, several recent studies have suggested that the levels of AGE-HSA are associated with prediabetic condition (15) and microalbuminuria (16).…”

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confidence: 99%

Development of Diagnostic Fragment Ion Library for Glycated Peptides of Human Serum Albumin: Targeted Quantification in Prediabetic, Diabetic, and Microalbuminuria Plasma by Parallel Reaction Monitoring, SWATH, and MSE

Korwar

Vannuruswamy

Jagadeeshaprasad

et al. 2015

Molecular & Cellular Proteomics

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Human serum albumin is one of the most abundant plasma proteins that readily undergoes glycation, thus glycated albumin has been suggested as an additional marker for monitoring glycemic status. Hitherto, only Amadori-modified peptides of albumin were quantified. In this study, we report the construction of fragment ion library for Amadori-modified lysine (AML), N()-(carboxymethyl)lysine (CML)-, and N()-(carboxyethyl)lysine (CEL)-modified peptides of the corresponding synthetically modified albumin using high resolution accurate mass spectrometry (HR/AM). The glycated peptides were manually inspected and validated for their modification. Further, the fragment ion library was used for quantification of glycated peptides of albumin in the context of diabetes. Targeted Sequential Window Acquisition of all THeoretical Mass Spectra (SWATH) analysis in pooled plasma samples of control, prediabetes, diabetes, and microalbuminuria, has led to identification and quantification of 13 glycated peptides comprised of four AML, seven CML, and two CEL modifications, representing nine lysine sites of albumin. Five lysine sites namely K549, K438, K490, K88, and K375, were observed to be highly sensitive for glycation modification as their respective m/z showed maximum fold change and had both AML and CML modifications. Thus, peptides involving these lysine sites could be potential novel markers to assess the degree of glycation in diabetes. Molecular & Cellular Proteomics

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“…The substances did not cause any significant alteration in absorbance in a 100-ml solution taken in a cuvette in concentration 5 g/l for albumin and 5 mM reduced glutathione. The values covered expected range in a plasma sample [28][29][30] . Principle of the reaction is depicted as Figure 5.…”

Section: Resultsmentioning

confidence: 61%

Evaluation of 2,6-dichlorophenolindophenol acetate as a substrate for acetylcholinesterase activity assay

Pohanka

Holas

2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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Ellman's method is a standard protocol for the determination of cholinesterases activity. Though the method is ready for laboratory purposes, it has some drawbacks as well. In the current article, 2,6-dichloroindophenol acetate is performed as a chromogenic substrate suitable for acetylcholinesterase (AChE) activity examination. Michaelis constant and maximal velocity for 2,6-dichloroindophenol acetate were determined (38.0 mM and 244 pkat) and compared to the values for acetythiocholine (K m 0.18 mM; V max 5.1 nkat). Docking for 2,6-dichloroindophenol acetate and human AChE was done as well. In conclusion, 2,6-dichloroindophenol acetate seems to be suitable chromogenic substrate for AChE and spectrophotometry and based on this it can be easily performed whenever AChE activity should be tested.

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Low Plasma Albumin Levels Are Associated with Increased Plasma Protein Glycation and HbA1c in Diabetes

Cited by 69 publications

References 23 publications

Influence of Varying Dietary Protein Levels on Glycation of Albumin, Tryptophan and Valine in the Plasma of Chickens

Influence of Varying Dietary Protein Levels on Glycation of Albumin, Tryptophan and Valine in the Plasma of Chickens

Development of Diagnostic Fragment Ion Library for Glycated Peptides of Human Serum Albumin: Targeted Quantification in Prediabetic, Diabetic, and Microalbuminuria Plasma by Parallel Reaction Monitoring, SWATH, and MSE

Evaluation of 2,6-dichlorophenolindophenol acetate as a substrate for acetylcholinesterase activity assay

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