To Study the Relationship Between the Glycosylated Hair Protein and HBA1C for Assessment of Blood Glucose Level in Diabetes Mellitus Type II (original) (raw)
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Aims: To determine if glycated protein found in scalp hair can predict blood glucose control as characterised by HbA1c. Also, to investigate cosmetic hair treatments' effect and hair sample mass's effect on the assay. Materials and Methods: 192 participants were included in this study. Anthropometrics, medical history and about 50 strands of hair, 4 cm long, proximal to the scalp, were collected. The concentration of fructosamine in hair was determined using the Thiobarbituric Acid (TBA) method with a fructose calibration curve. The strength of the correlation between HbA1c and fructosamine for hair samples with and without hair treatments was assessed using Pearson's R. Results: For the samples with no reported hair treatments, there was a statistically positive association between HbA1c and fructosamine when the sample mass ranged between 40mg to 120 mg. A high positive association, r(28) = 0.647, p = <0.001 was observed when hair samples greater than 70mg were used...
Journal of Immunological Methods, 2007
We describe immunochemical assays of non-enzymatic glycation products in human head-hair protein extracts and hair cross sections using Western blots and a novel "dot-block" methodology. In the latter, groups of approximately 15 hair fibers, clipped at about 1 mm proximal to the scalp-skin were aligned, wound around, and attached to 3 mm diameter araldite screw rods. Up to 40 such rods were next embedded lengthwise in additional araldite polymer creating a solid block and the top surface of the block was sectioned off to the half-diameters of the screw rods thus exposing accurately transected hair cross sections at regular (∼ 0.5 cm) intervals. Early-and advanced-glycation products (EGAs and AGEs, respectively) were determined in the exposed cross sections in-situ using specific antibodies and ECL densitometry as in conventional Western blots. Both Western blots and this technique demonstrated 3.1 fold EGAs increases in the proximal 2 cm of hair of diabetics as compared to non-diabetics. Dot-blocks, in addition, were less variable and demonstrated exponential EGAs decreases along fibers distally, with calculated intercepts (at the hair roots) of 4.9 fold increases in diabetics as opposed to non-diabetics and half-lives of 6.0, 5.9 and 9.0 months in hair of nondiabetics, gestational diabetics and diabetic patients, respectively. Correlations in amounts of BG vs. HbA1 c , BG vs. EGAs, and HbA1 c vs. EGAs, using dot-block and clinical lab data were all significant (p b 0.05). Acute onset T1D patients, defined as previously unsuspected patients diagnosed upon hospitalization due to diabetic complications, exhibited nearly identical EGAs levels in their proximal 0-9 cm hair as did T1D patients with long-established diabetes, thus supporting the notion of long and insidious T1D etiology. Removal of 1-2 μm layers from dot-block surfaces enabled their re-use for multiple assays. Applied anti-AGEs antibodies demonstrated slight decreases or no significant changes in CML and MGI along hair shafts of normal and diabetic subjects. Fluctuations in EGAs and AGEs along hair shafts, indicating alterations in glycemic control were also observed. We conclude that the dot-block method has a potential for early diagnosis and monitoring of diabetes, and more generally, as a long term "biological record" of various chronic medical conditions.
A new effective method for the evaluation of glycated intact plasma proteins in diabetic subjects
Diabetologia, 1995
The molecular weights of plasma proteins from healthy subjects and from patients with well-or badly-controlled diabetes mellitus have been determined by use of a matrix-assisted laser desorption ionization method, representing a highly accurate technique for the determination of the molecular weight of large biomolecules. Using this approach, different molecular weights of human serum albumin have been found for healthy (66,572-66,694 dalton) and diabetic (66,785-68,959 dalton) subjects. Such differences can be rationalized as being due to the different number of glucose molecules condensed on the protein and/or their further oxidation products; in the case of our diabetic patients this number is in the range of 1.4-14.8. The data show the high validity and specificity of the technique, which allows us to evaluate, without any protein degradation procedure, the number of glucose molecules condensed on a specific protein and ascertain the relationship of this number to the physiopathogenetic conditions of the subjects studied. [Diabetologia (1995) 38: 1076-1081] Key words Protein glycation, human serum albumin, mass spectrometry, laser desorption ionization. Among the various theories concerning the aetiopathogenesis of chronic diabetic complications, the multifactorial theory is the most widely accepted; it suggests that the tissue damage following metabolic alteration (hyperglycaemia) is favoured by genetic (individual susceptibility) and environmental factors (obesity, hypertension, smoking) [1]. Several studies have shown that hyperglycaemia can cause damage by a series of mechanisms, the
Changes in the Molecular Structure of Hair in Insulin-Dependent Diabetes
Biochemical and Biophysical Research Communications, 1997
sults obtained from synchrotron X-ray diffraction Low-angle synchrotron X-ray diffraction has restudies and swelling experiments, Feughelman and vealed clear and consistent changes in the molecular James have developed a new model for a-keratin structure of a-keratin of hair in insulin-dependent diawhich satisfies all previously established results betes (IDDM) both for human IDDM subjects and for (5,6). This model shows that on the microscopic level, baboons with streptozocin induced diabetes. These the macrofibrils are composed of hexagonal arrays of changes in both meridional and equatorial intensity intermediate filaments (IFs), each of which is comdistributions are fully explained by a newly developed posed of 8 highly organised tetramers of low sulphur hexagonally packed model for keratin which locates content, embedded in a cystine rich matrix. Each tet-
A comparison of the Glycosylation Gap and Hemoglobin Glycation Index in patients with diabetes
Journal of Diabetes and its Complications, 2005
The Glycosylation Gap (GGAP) based on fructosamine (F) measurement and the Hemoglobin Glycation Index (HGI) based on mean blood glucose (MBG) are two indices of between-individual differences in glycated hemoglobin (HbA1c) adjusted for glycemia. We sought to simultaneously compare GGAP with HGI and other estimates of glycemia. HbA1c, F, and MBG level were obtained at a clinic visit from 62 patients with Type 1 diabetes. GGAP and HGI were calculated from the data as previously described. The variables were compared by correlation analysis. The concordance of patient classification by GGAP and HGI was compared by weighted kappa test. The mean HbA1c=11.1+/-2.7%, F=372.0+/-136.6 mol/l, MBG=186.5+/-58.4 mg/dl, HGI=0.0+/-2.0, and GGAP=0.0+/-1.9. MBG, HbA1c, and F were all highly correlated with each other. The HGI and GGAP were highly correlated (r=.73, P&amp;amp;amp;amp;amp;amp;amp;amp;amp;lt;.0001) and similar in both magnitude and direction. There was good agreement between HGI and GGAP classifications of patients into high, moderate, and low glycation groups (P&amp;amp;amp;amp;amp;amp;amp;amp;amp;lt;.0075). GGAP and MBG give similar information regarding between-patient differences in HbA1c among patients with diabetes. Thus, biological variation in HbA1c is not an artifact of variability in glucose measurements comprising the MBG. Individual patient factors influence the intracellular glycation of HbA1c in addition to the effect of extracellular glycemia, which is manifested as a between-individual biological variation in HbA1c.
Study of significance of glycosylated hemoglobin in diabetic patient
2016
Background: Investigation of the structure and biosynthesis of glycosylated Hemoglobin (HbA1c) in the past decade have provided a means to objectively access the average level of glycemia in diabetic patient. The use of Glycosylated hemoglobin level as integrated index of long term blood glucose level, represent a significant tool in our research and therapeutic armamentarium. In this study, we have estimated glycosylated Hemoglobin (HbA1c) in diabetic and non diabetic person and its relationship with fasting and post prandial blood sugar levels. Materials and methods: In present study, Glycosylated hemoglobin levels were estimated by using cation exchange resin method. The study was conducted from November 2012 to October 2014. Measurement of total HbA1c and blood sugar were carried out at Diabetic research laboratory, Tertiary care centre, Teaching Institute. 110 Non diabetic persons studied as a control, which were proved to be Non diabetic from history, FBS, PPBS, Urine sugar. P...
2019
The objective of the present study was to correlate estimated average glucose (eAG) values calculated from HbA1c values obtained from Tosoh TLC-723 G8 based on cation exchange based HPLC, TBA 12 FR enzymatic fructosyl peptide oxidase (FPOX) method and D10 HbA1c analyser Bio Rad Laboratories (USA) with fasting plasma glucose (FPG) levels by hexakinase method for diagnosis and prognosis of diabetes. A total of 300 randomly selected patient samples were analysed for FPG by hexakinase method and HbA1c values were estimated by using Tosoh TLC-723 G8 analyser based on cation exchange HPLC, enzymatic FPOX (Manufacture by Seikisui Medical Co. Ltd., Japan) programmed on TBA 12 FR biochemistry analyser and D10 HbA1c analyser Bio Rad Laboratories (USA). The eAG values were calculated using Nanthan’s regression equation for both HbA1c values. The correlation between FPG, HbA1c and eAG values has been done by Pearson correlation (r) and regression analysis was done by SPSS software. The correla...