5-hydroxymethylfurfural has been researched along with Diabetes-Mellitus--Type-2* in 6 studies
1 trial(s) available for 5-hydroxymethylfurfural and Diabetes-Mellitus--Type-2
5 other study(ies) available for 5-hydroxymethylfurfural and Diabetes-Mellitus--Type-2
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Investigation into the mechanisms of quercetin-3-O-glucuronide inhibiting α-glucosidase activity and non-enzymatic glycation by spectroscopy and molecular docking.
The inhibition of α-glucosidase and glycation is closely related to the treatment of type 2 diabetes mellitus (DM) and its complications. In this study, quercetin-3-O-glucuronide (Q3GA) showed reversible and mixed-mode inhibition of α-glucosidase activity, with an IC Topics: alpha-Glucosidases; Diabetes Mellitus, Type 2; Furaldehyde; Glycation End Products, Advanced; Glycoside Hydrolase Inhibitors; Glycosylation; Humans; Kinetics; Molecular Docking Simulation; Quercetin | 2021 |
Detection of Circulating Auto-Antibodies Against Ribosylated-LDL in Diabetes Patients.
This study analyzes effect of glycation on ApoB-100 residues by D-ribose as D-ribosylated-glycated LDL might be responsible for the cause of diabetes mellitus because of its far higher antigenic ability. The binding characteristics of circulating auto-antibodies in type 1 and type 2 diabetes patients against native and modified LDL were assessed.. T1 Diabetes (n = 43), T2 diabetes patients (n = 100) were examined by direct binding ELISA as well as inhibition ELISA, were compared with healthy age-matched controls (n = 50).. High degree of specific binding was observed by 74.42% of T1 diabetes and 45.0% of T2 diabetes patient's sera toward glycated LDL, in comparison to its native analog. Competitive inhibition ELISA reiterates the direct binding results. Furthermore, ketoamine content, Hydroxymethylfurfural (HMF) content and carbonyl content were also estimated in patient's sera healthy subjects. The increase in total serum protein carbonyl levels in the diabetes patients was largely due to an increase in oxidative stress. The increase in ketoamine as well as HMF content inpatients sera than healthy subjects is an agreement of induced glycation reaction in patients than healthy subjects.. D-ribosylated-LDL has resulted in structural perturbation causing generation of neo-antigenic epitopes that are better antigens for antibodies in T1 and T2 diabetes patients. Topics: Adult; Aged; Apolipoprotein B-100; Autoantibodies; Diabetes Mellitus, Type 1; Diabetes Mellitus, Type 2; Enzyme-Linked Immunosorbent Assay; Epitopes; Female; Furaldehyde; Glycation End Products, Advanced; Glycosylation; Humans; Lipoproteins, LDL; Male; Middle Aged; Protein Binding; Ribose | 2017 |
Preferential recognition of Amadori-rich lysine residues by serum antibodies in diabetes mellitus: role of protein glycation in the disease process.
This study analyzes effect of glycation on proteins rich in lysine residues as hyperglycemia induced protein glycation has been mainly reported in diabetes mellitus at the intrachain lysine residues leading to the formation of Amadori modified proteins. We have studied the effect of glucose on poly-l-lysine (PLL), a homopolymer of lysine residues. Levels of Amadori products in the glycated PLL were evaluated by fructosamine assay and the presence of 5-hydroxymethylfurfural (HMF) in the glycated PLL was analyzed by thiobarbituric acid assay. Fluorescence and FT-IR spectroscopy were applied to characterize the modified PLL. Binding characteristics of experimentally induced antibodies against glycated PLL and the presence of antibodies against glycated PLL in the sera of diabetes patients was evaluated by solid phase enzyme immunoassays. The fructosamine assay showed significantly high yield of early glycation (Amadori) products in the glycated PLL, which was confirmed by increased yield of HMF from Amadori products of glycated PLL. Loss in fluorescence intensity and appearance of a new band corresponding to Amadori products were observed in FT-IR spectrum of the glycated PLL. Glycated PLL was found to be highly immunogenic in rabbits as compared to the native form. Serum antibodies from diabetes patients showed appreciably high recognition of the glycated PLL. The results conclusively show the glycation induced damage to the lysine molecules and specific recognition of Amadori-lysine residues by serum antibodies from diabetes patients. The glycated lysine residues may serve as a diagnostic biomarker for early glycation process in diabetes mellitus. Topics: Adult; Animals; Antibodies; Diabetes Mellitus, Type 1; Diabetes Mellitus, Type 2; Female; Fructosamine; Furaldehyde; Glycosylation; Humans; Lysine; Male; Middle Aged; Polylysine; Rabbits | 2009 |
Glycosylated serum proteins and glycosylated hemoglobin in the assessment of glycemic control in insulin-dependent and non-insulin-dependent diabetes mellitus.
To evaluate the relative value of glycosylated serum proteins (GSPs) versus glycosylated hemoglobin (HbA1c) in assessing glycemic control in diabetes mellitus, we performed regular monitoring of GSPs and HbA1c in 30 subjects with insulin-dependent diabetes mellitus (IDDM) or non-insulin-dependent diabetes mellitus (NIDDM) who performed frequent self-glucose monitoring. Analysis of the relationship between patterns of glycemic control and GSPs and HbA1c demonstrated that subjects with IDDM and NIDDM appeared similar when the more traditional indicators of glycemic control such as mean blood glucose level (166.9 +/- 20.9 v 177.4 +/- 39.6 mg/dL) or HbA1c (83.57 +/- 12.8 v 80.24 +/- 15.7 mmol hydroxymethyl furfuraldehyde [HMF]/mol hemoglobin [Hgb]) were used. However, when GSP levels or the standard deviation of mean glucose levels (SDMG) were used to assess glycemic control, higher levels were found in subjects with IDDM (52 +/- 10.3 mg/g protein and 28.59 +/- 7.60 mg/dL) versus NIDDM (44.6 +/- 15.2 mg/g protein and 21.6 +/- 15.9 mg/dL). Using multivariate analysis, GSPs were predictive of SDMG (P = .046), whereas HbA1c added no significant further information (P = .27). Our results suggest that GSPs may be more sensitive than HbA1c assay to the greater fluctuations in blood glucose levels generally associated with IDDM. Topics: Adult; Blood Glucose; Blood Glucose Self-Monitoring; Blood Proteins; Colorimetry; Diabetes Mellitus, Type 1; Diabetes Mellitus, Type 2; Furaldehyde; Glycated Hemoglobin; Glycated Serum Proteins; Glycoproteins; Humans; Middle Aged; Multivariate Analysis | 1993 |
[Measurement of glycosylated hair of diabetics and its clinical significance].
Topics: Aged; Diabetes Mellitus, Type 2; Female; Furaldehyde; Glycated Hemoglobin; Glycosylation; Hair; Humans; Male; Middle Aged | 1988 |