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Query: UMLS:C0011849 (diabetes)
 277,896 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To evaluate changes in glycemic control during a 2-wk diabetes summer camp program, fasting plasma glucose (FPG), glycosylated hemoglobin (GHb), and glycosylated serum protein ( GSP ) levels were measured in a group of 36 children at the beginning and end of camp. Average FPG and GHb were unchanged during the 2-wk period, but the average decrease in GSP (7%) was significant (P less than 0.005). The results of this study indicate that a measurable improvement in diabetic control occurred in some children during the 2-wk summer camp program.
Diabetes Care
PMID:Changes in blood protein glycosylation during a diabetes summer camp. 673 84

Glycosylated serum protein (GSP) and glycosylated hemoglobin (GHb) were measured in 263 insulin-dependent and 41 non-insulin-dependent diabetic subjects. Both indices provided useful information in type II diabetes, but were extremely poor in judging control in type I diabetes. In both groups, there was poor correlation of the fasting serum glucose with either GSP or GHb. Only 4% of type I diabetic subjects had normal values for both GSP and GHb. Of subjects with elevated GSP, 98% had elevated GHb; 25% of subjects with elevated GHb values had normal values for GSP.
Diabetes Care
PMID:Comparison of two indices of glycemic control in diabetic subjects: glycosylated serum protein and hemoglobin. 683 20

We describe here some useful modifications of the thiobarbituric acid (TBA) assay for measurement of nonenzymatic glucosylation of serum protein. The modified assay minimizes interference by glucose without a lengthy dialysis step, and does not require an independent blank determination. These modifications should make the TBA assay more convenient for evaluating glycemic control in diabetes. Serum protein is first precipitated with cold ethanol to remove endogenous glucose. The protein is then hydrolyzed in an oxalic acid solution to release glucose as hydroxymethylfurfural (HMF). The HMF is reacted with TBA to form a chromophore which is extracted into isobutanol for spectrophotometric analysis (lambda max = 435 nm). The absorbance at 435 nm is corrected by subtracting a blank reading at 500 nm, and the nmol HMF released is determined using a standard curve prepared with pure HMF. Normal values of this assay for both adults and children are 0.38 +/- 0.10 nmol HMF/mg serum protein (means +/- 2 SD). When the assay was applied to serum samples from a group of 39 Type I diabetic children more than 90% of the children exceeded the normal range of the assay.
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PMID:Measurement of nonenzymatically glucosylated serum protein by an improved thiobarbituric acid assay. 687 56

A within-person trial in 35 diabetic subjects investigated the effect of six months' administration of 750 mg of calcium dobesilate daily on the erythrocyte sedimentation rate, erythrocyte and leucocyte counts, platelet aggregation, blood cholesterol and triglyceride concentrations, total serum protein concentration, electrophoretically determined serum proteins fractions, and the escape rate of intravenously injected 131-I-albumin. Significant increases in intravenous retention of 131-I-albumin, serum albumin and beta-globulin fractions, and total serum protein concentration resulted. No change in the remaining variables was detected. The results suggest that calcium dobesilate reduces pathologically increased transcapillary escape rate in diabetes mellitus.
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PMID:Effects of permeation of plasma proteins in diabetic patients. 694 49

The relationship between concentrations of blood glucose and nonenzymatically glucosylated serum proteins was studied in rats with alloxan-induced diabetes of varying severity. Fasting serum glucose correlated strongly with both glucosylated albumin (r = 0.91, P less than 0.001) and glucosylated serum protein (r = 0.93, P less than 0.001). The relative rates of response of serum protein and hemoglobin glycosylation to changes in blood glucose were also compared. Following withdrawal of insulin from diabetic rats, the half-times to reach new steady state levels of blood glucose, glucosylated serum proteins, and glycohemoglobins were about 2, 3, and 8 days, respectively. Similarly, on reinstitution of insulin therapy, the half-times for these same indices to return to baseline values were 2, 3.5, and 15 days, respectively. Changes in glucosylated albumin were more sensitive than glycohemoglobins to changes in serum glucose, consistent with the observation that albumin was glucosylated at about 10 times the rate for hemoglobin in incubations in vitro. These data indicate that glucosylated serum protein measurements can serve as a sensitive, short-term integrator of blood glucose homeostasis in diabetes.
Diabetes 1980 Jul
PMID:Nonenzymatic glucosylation of serum proteins and hemoglobin: response to changes in blood glucose levels in diabetic rats. 699 38

The 8% increase in serum viscosity in diabetes mellitus, more striking in diabetics with evidence of microangiopathy, has been further investigated. Methodology has been developed to eliminate the effect of fluctuating levels of glucose, lipids and protein. This was accomplished first by dialysis of fresh serum and later by ultracentrifugation to remove lipoprotein followed by dialysis. The distinction between diabetic and nondiabetic viscosity levels was improved by removing glucose and correcting for fluctuations in serum protein level, principally because variation between observations on the same subject was substantially reduced. Two methods were utilized to adjust for protein concentration differences. Ether technique increased the statistical significance of the viscosity increase in diabetes. Without lipoprotein removal the regression of specific fluidity (1-1/relative viscosity) with concentration differed between the sexes. When lipoprotein was removed the sex difference disappeared and the regression line passed through the origin. Removal of lipoprotein also further increased the discrimination between diabetic and normal serum. Even without lipoprotein removal elevated serum viscosity was readily detected in advanced glucose intolerance. In both studies, viscosity was higher in diabetics with microangiopathic sequelae, increasing progressively with more evidence of microangiopathy. No effect of severity of hyperglycemia or duration of diabetes could be demonstrated. Increased serum viscosity' association with microvascular sequelae and its presence early in the disorder suggest that the protein changes responsible for its elevation may play a role in the development of diabetic microangiopathy.
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PMID:Further observations on serum viscosity changes in diabetes mellitus. 707 13

The modification of haemoglobin A by glucose to haemoglobin A Ic is a classical example for a nonenzymatic glucosylation (n. e. glu.) reaction of a protein. It has been suggested, that various proteins are subjected to this process during hyperglycemia phases, if the protein meets certain steric, electrostatic and biochemical characteristics. In the present report n. e. glu. of haemoglobin, serum protein, collagen, basement membrane protein and alkaline phosphatase is discussed. It is suggested that n. e. glu. might influence protein function and forms thus the biochemical basis for specific complications of diabetes mellitus in an outside pregnancy.
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PMID:[Non-enzymatic glucosylation of proteins]. 709 97

With a view to studying the eventual alterations of protein metabolism, some serum protein fractions such as: immunoglobulins (IgG, IgA, IgM), transferrin and ceruloplasmin were determined in 100 diabetics (52 males, 48 females) in comparison with a control group of 26 healthy subjects. Significant differences were found between IgA and transferrin values both in diabetics and in controls. IgA tended to increase with the length of disease, whereas IgG, IgM and transferrin showed a contrary trend. IgA and transferrin values were higher in the patients with juvenile and young adult diabetes, as compared to maturity onset and senile diabetes. Other immunoglobulin and transferrin changes were related to sex, age, type of treatment, degree of stability, presence of chronic complications. No significant anomalies were found for ceruloplasmin. The results confirm the presence of serum protein alterations in diabetes mellitus, whose significance may be correlated with the clinical particularities of the disease.
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PMID:Study of some serum protein fractions in various clinical forms of diabetes mellitus. 723 48

This study shows that the thiobarbituric acid (TBA) reaction as applied to the measurement of non-enzymatically glycosylated serum proteins(s) [1], yields erroneous results unless strictly standardized conditions are followed. Critical points are in particular (a) the concentrations of NaBH4 required for the preparation of the blanks by reduction of the ketoamine linkages; (b) the amounts of protein which should be identical in all serum samples to be compared; (c) dialysis for removal of glucose and NaBH4 prior to hydrolysis; (d) increase in the yield of 5-hydroxymethylfurfural (HMF) by appropriate conditions of hydrolysis. From our data obtained with an improved TBA-assay it appears that about 90% of total glycosylated serum protein is accounted for by glycosylated albumin. Thus changes in the latter used for diagnostic purposes in diabetes, may well be reflected by total serum glycosylprotein measurement.
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PMID:Improvement of the thiobarbituric acid assay for serum glycosylprotein determination. 723 26

We measured non-enzymatically-glycosylated serum protein by a colorimetric assay in 107 diabetic and 82 control subjects. The mean level in diabetics was more than twice that in controls. Cross sectional and longitudinal studies in diabetic patients showed that glycosylated serum protein levels correlated with both fasting serum glucose and glycosylated haemoglobin levels. The correlation between glycosylated serum protein and fasting serum glucose was closer in Type 2 than in Type 1 diabetes. Treatment aimed at improving control in eight poorly controlled diabetic patients resulted in a 37% mean fall in glycosylated serum protein within one week, whereas glycosylated haemoglobin decreased only 8%. These studies confirm that non-enzymatic glycosylation of serum proteins is enhanced in diabetes. Measurement of glycosylated serum protein appears to provide an index of glycaemia over the preceding several days. It has the advantage of detecting improvements in glycaemic control much sooner than does glycosylated haemoglobin measurement.
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PMID:Non-enzymatically glycosylated serum protein in diabetes mellitus: an index of short-term glycaemia. 726 78


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