A study on human serum albumin influence on glycation of fibrinogen

Kielmas, Martyna; Szewczuk, Zbigniew; Stefanowicz, Piotr

doi:10.1016/j.bbrc.2013.08.025

Cited by 8 publications

(7 citation statements)

References 26 publications

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“…In this context, correct selection of proteolytic enzymes is critical for success of the whole BUP experiment. Accordingly, a wide range of proteases of various specificity were proposed during the last decade ( Table 1 ): trypsin [ 144 , 145 ], chymotrypsin [ 146 , 147 ], LysC [ 137 , 148 ], AspN [ 67 , 74 ], GluC [ 149 , 150 ], endopeptidase Arg C [ 137 ], pepsin [ 151 ], proteinase K [ 152 ], and papain [ 153 ]. Due to its moderately high specificity (C-terminally from K and R residues) and convenient size of resulting hydrolytic peptides (0.5–3.0 kDa) [ 154 ], trypsin remains the most widely used protease [ 155 ].…”

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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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

View full text Add to dashboard Cite

show abstract

“…[ 7 ] This study was corroborated in a recent finding where low albumin levels were associated with increased fibrinogen glycation. [ 8 ] It has also been suggested that low plasma albumin predicts the glycated hemoglobin (HbA1c) in type 2 diabetes,[ 9 ] thus, strongly implicating albumin in regulation of plasma protein glycation and HbA1c.…”

Section: Introductionmentioning

confidence: 99%

Association between serum albumin and glycated hemoglobin in Asian Indian subjects

Tiwari¹,

Bothale²,

Hasan³

et al. 2015

Indian J Endocr Metab

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Background:Protein glycation plays a significant role in diabetic complications. Glycated hemoglobin (HbA1c) is a known predictor of diabetes and its complications. Albumin, found to be profoundly glycated in diabetes, and its level could regulate plasma protein as well as hemoglobin glycation.Aim:We aimed to evaluate the association between variations in albumin level with HbA1c in the Asian Indian population.Materials and Methods:We screened data of 929 subjects who have had a simultaneous measurement of fasting plasma glucose (FPG), HbA1c and albumin levels via the same blood collection. Data were analyzed by SPSS for 610 subjects who met the study criteria.Results:There was a significant negative correlation between HbA1c and albumin concentration (r = −0.284; P < 0.001). Univariate analysis showed the statistically significant decrease of average HbA1c but not for fasting plasma glucose (FPG) across increasing tertiles of albumin. Stepwise multiple regression model showed a significant correlation between HbA1c and serum albumin (P < 0.05), FPG (P < 0.001), hemoglobin (Hb) (P < 0.001) and serum globulin (P < 0.05). FPG was the strongest predictor (63.4%) of variation of HbA1c. The albumin concentration (r = −0.114) accounted for 0.3% (P < 0.05) of the total variance in HbA1c independent of age, body mass index, FPG, Hb, creatinine, total protein and globulin. It was also observed that HbA1c decreases with increasing albumin concentration in those having FPG between 100 to <126 mg/dl.Conclusion:Serum albumin negatively correlates with HbA1c in Asian Indians independent of other variables. This study suggests that predicting diabetes and its complication based on the HbA1c needs to be further investigated in Indian subjects.

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“… 11 , 12 , 14 The plausible explanation that albumin could competitively protect hemoglobin glycation was derived from previous studies where low albumin levels were associated with increased glycation of plasma proteins including insulin, fibrinogen, etc. 13 − 15 In this study, we have unequivocally demonstrated in erythrocyte culture that albumin levels influence hemoglobin glycation, i.e., higher levels of albumin reduce hemoglobin glycation and vice versa. At lower albumin levels, increased albumin glycation was observed, which perhaps decreased its ability to reduce hemoglobin glycation.…”

Section: Discussionmentioning

confidence: 67%

Albumin Abundance and Its Glycation Status Determine Hemoglobin Glycation

et al. 2018

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Diabetes diagnosis and management majorly depend upon the measurement of glycated hemoglobin (HbA1c) levels. Various factors influence HbA1c levels such as the use of various analytical methods and the presence of various clinical conditions. Plasma albumin levels were known to be negatively associated with HbA1c. However, the precise mechanism by which they affect HbA1c is not well understood. Therefore, we have studied the influence of albumin levels and its glycation status on hemoglobin glycation using erythrocyte culture experiments. Erythrocytes maintained at low albumin concentration exhibited relatively increased albumin and hemoglobin glycation as compared to that in those maintained at higher albumin concentration. Increase in albumin glycation may decrease its ability to protect hemoglobin glycation. This was demonstrated by treatment of erythrocytes with N(ε)-(carboxymethyl)lysine-modified serum albumin (CMSA), which failed to protect hemoglobin glycation; instead, it increased hemoglobin glycation. The inability of CMSA to reduce hemoglobin glycation was due to the lack of free lysine residues of albumin, which was corroborated by using N(ε)-(acetyl)lysine serum albumin (AcSA) and clinical diabetic plasma. This is the first study which demonstrates that the modification of lysine residues of albumin impairs its ability to inhibit hemoglobin glycation. Furthermore, correlation studies between HbA1c and albumin levels or relative albumin fructosamine from clinical subjects supported our experimental finding that albumin abundance and its glycation status influence hemoglobin glycation. Therefore, we propose albumin level and its glycation status to be quantified in conjunction with HbA1c for better management of diabetes.

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A study on human serum albumin influence on glycation of fibrinogen

Cited by 8 publications

References 26 publications

Maillard Proteomics: Opening New Pages

Maillard Proteomics: Opening New Pages

Association between serum albumin and glycated hemoglobin in Asian Indian subjects

Albumin Abundance and Its Glycation Status Determine Hemoglobin Glycation

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