Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011849 (diabetes)
 277,896 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To determine whether the carbohydrate content of serum proteins is related to overall glycemic control, we studied serum protein-bound hexose and glycosylated hemoglobin [HbA1(a+b+c)] in 37 ambulant diabetic patients and 32 nondiabetic controls. Protein-bound hexose was correlated with HbA1(a+b+c) in the diabetic patients (r = 0.36, P less than 0.025). The mean protein-bound hexose level of the diabetic patients was greater than that of the controls (190.8 versus 174.7 mg/dl, P less than 0.01), but diabetic patients with HbA1(a+b+c) less than 12% had a mean protein-bound hexose similar to the controls. In nine of the diabetic patients, mean protein-bound hexose and HbA1(a+b+c) were significantly reduced during a period of intensive outpatient care, while two major serum glycoproteins, haptoglobins and alpha-1-antitrypsin, were unchanged. Our findings support the hypothesis that increased glycosylation of serum proteins may occur in diabetes mellitus; this abnormality in serum protein-bound hexose may be corrected by close attention to overall glycemic control.
Diabetes 1979 Nov
PMID:Serum protein-bound hexose in diabetes: the effect of glycemic control. 48 38

The extent of nonenzymatic glucosylation of serum protein in control and diabetic subjects was measured by a chemical procedure using thiobarbituric acid. A mean value of 0.81 (+/- 0.21 SD) nmol glucose per milligram serum protein was observed in the control group. Diabetics displayed elevated levels of glucosylated serum proteins, up to 4 nmol glucose per milligram protein. Glucosylation of serum protein correlated strongly with fasting blood sugar (r = 0.71), percent hemoglobin A1 (r = 0.79), and percent glucosylated albumin (r = 0.99). There was no overlap between control and diabetic groups, i.e., within 3 SD of the mean of controls. These studies indicate that the assay for glucosylated serum protein appears to be an especially sensitive indicator of the degree of hyperglycemia in diabetes.
Diabetes 1979 Nov
PMID:Nonenzymatic glucosylation of serum proteins in diabetes mellitus. 48 39

This study was designed to focus on the genetic control of tolbutamide dispositon in humans and to provide insight into the potential for high accrued blood levels in individuals receiving fixed dosage regimens. Tolbutamide was administered intravenously to 42 nondiabetic subjects, eight of their relatives, and to five sets of twins. A ninefold variation in the rate of tolbutamide disappearance from plasms (Kd) was found. This variation was characterized by a trimodal frequency distribution, suggestive of monogenic inheritance and consistent with pedigree analysis, indicating autosomal transmission of rapid and slow inactivation of tolbutamide. A heritability value of 0.995 for Kd indicated little influence of environmental factors on variation of this rate. Interindividual differences in the binding of 35S-tolbutamide to serum proteins were also assessed. No correlation was found between tolbutamide serum protein binding affinity and Kd. Analysis of the metabolites of tolbutamide in urine samples provided evidence for the microsomal oxidation of the drug to hydroxytolbutamide as the primary site of genetic control. In conclusion, this study provides evidence for monogenic control of tolbutamide metabolism in man. The results suggest that fixed dosage regimens of this drug, as were prescribed in the controversial University Group Diabetes Program study, might lead to higher accrued blood levels in slow inactivators.
Diabetes 1979 Jan
PMID:Pharmacogenetics of tolbutamide metabolism in humans. 56 11

The effects of alloxan-induced diabetes on liver regeneration were investigated. Normal and diabetic rats were sacrificed at eight time periods between 16 hours and 4 weeks following two-thirds partial hepatectomy or sham operation. The results indicate that alloxan-induced diabetes delays but does not prevent liver regeneration following partial hepatectomy. This delay is indicated by a depressed synthesis of RNA, DNA and protein during the first post-operative day and a lack of mitotic figures in the 24-hour sample. In addition, the synthesis of these three cellular constituents did not return to control levels as rapidly in the diabetics. Compared with the sham operated animals, the concentrations of total serum protein remained depressed longer in the diabetic hepatectomized animals. The data indicate that the metabolic alterations associated with alloxan diabetes delay the onset of the regenerative process and prolong the recovery period.
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PMID:Liver regeneration in normal and alloxan-induced diabetic rats. 88 99

A comparison of serum protein fractions (electrophoretic separation) between control and mild alloxan-diabetic rats examined 10 days after alloxan indicates a decrease in total protein, a decrease in percentage albumin accompanied by a decrease in A/G ratio. In severe diabetic rats examined 48 hours after the administration of alloxan, there were no changes in total protein or in serum-protein fractions. The changes in the serum protein and serum albumin in mild diabetic cases are not the result of the degree of diabetes only. But they are rather explained by the longer time interval of the uncontrolled diabetic state. ATP administered to mild diabetic rats producing the following changes: two injections of 5 mg per rat exhibit a lowering effect on the blood glucose, with a decrease in liver fat. ATP resulted also in a significant increase in serum albumin and a decrease in beta-globulin with a consequent increase in the A/G ratio. Comparison of the different protein fractions of male and female control rats did not show any significant difference. ATP administered to control animals did not alter the normal electrophoretic pattern.
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PMID:Effect of repeated doses of ATP on serum protein pattern and fat content of the liver in experimental diabetes. 89 65

Free and protein-bound serum sugars and serum lipids were analyzed in 65 adult diabetic patients, 10 age-matched controls, and 24 male medical students for correlation of carbohydrate changes with the extent of retinal, renal, and cardiovascular disease. In diabetic sera, both protein-bound sugars and free mannose, fucose, and hexosamine were significantly elevated; free galactose and inositol were elevated in some diabetic patients, and essentially undetectable in sera from controls. Serum triglycerides and pre-beta-lipoproteins were also elevated in diabetics, but alpha-lipoproteins decreased. Although no specific relationships were observed with the extent of retinal and renal disease, bivariate analyses by Pearson coefficients of correlation showed correlations between levels of serum-free mannose and systolic blood pressure, free hexosamine and duration of diabetes, and serum protein-bound fucose and age. Serum triglycerides and pre-beta-lipoprotein levels correlated with insulin therapy. These are preliminary leads of laboratory studies related to carbohydrate macromolecular changes which might aid in a better understanding of the cardiovascular complications associated with diabetes.
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PMID:Serum-free and protein-bound sugars and cardiovascular complications in diabetes mellitus. 124 17

Fructosamine, a glycated serum protein, was evaluated as an index of glycemic control in normal and diabetic cats. Fructosamine was determined manually by use of a modification of an automated method. The within-run precision was 2.4 to 3.2%, and the day-to-day precision was 2.7 to 3.1%. Fructosamine was found to be stable in serum samples stored for 1 week at 4 C and for 2 weeks at -20 C. The reference range for serum fructosamine concentration in 31 clinically normal colony cats was 2.19 to 3.47 mmol/L (mean, 2.83 +/- 0.32 mmol/L). In 27 samples from 16 cats with poorly controlled diabetes mellitus, the range for fructosamine concentration was 3.04 to 8.83 mmol/L (mean, 5.93 +/- 1.35 mmol/L). Fructosamine concentration was directly and highly correlated to blood glucose concentration. Fructosamine concentration also remained high in consort with increased blood glucose concentration in cats with poorly controlled diabetes mellitus over extended periods. It is concluded that measurement of serum fructosamine concentration can be a valuable adjunct to blood glucose monitoring to evaluate glycemic control in diabetic cats. The question of whether fructosamine can replace glucose for monitoring control of diabetes mellitus requires further study.
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PMID:Evaluation of serum fructosamine concentration as an index of blood glucose control in cats with diabetes mellitus. 145 23

In an investigation into the effect of prostaglandin E1 on proteinuria in nephrotic diabetic nephropathy, five patients were treated with 40 micrograms prostaglandin E1 administered intravenously over 2 h twice daily for 4 weeks. The following parameters were compared before and after treatment: protein excretion in urine; total serum protein concentration; serum albumin concentration; creatinine clearance; blood urea nitrogen; and serum creatinine content. A further five patients with nephropathy resulting from non-insulin-dependent diabetes mellitus were selected as controls. Analysis of the results using Student's t-test showed no significant change in any of the parameters before and after treatment.
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PMID:Influence of prostaglandin E1 on slight proteinuria in non-azotaemic diabetics. 156 24

Serum albumin, transferrin, transthyretin (prealbumin), and retinol binding protein concentrations were determined in 74 children with insulin-dependent diabetes mellitus before and after a 10-day camp session during which blood glucose concentrations were controlled. Initial concentrations of albumin and transferrin in the subjects were not different from those in 21 children and adults without diabetes, and did not change during the study period. Transthyretin and retinol binding protein concentrations were lower in subjects with diabetes than in the control population, and increased from 182 +/- 49 mg/l and 42.5 +/- 13.4 mg/l to 232 +/- 71 mg/l and 47.2 +/- 13.5 mg/l, respectively. We observed correlations between the changes in transferrin, transthyretin, and retinol binding protein. Although reductions in glycated albumin and transferrin indicated improvement in blood glucose control, there was no correlation between changes in the glycated markers and the concentrations of serum transport proteins. Thus, serum protein concentrations were influenced by the metabolic control of diabetes, but did not directly reflect blood glucose.
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PMID:Effect of metabolic control on serum protein concentrations in diabetes. 175

An analytical method of fructosamine (glycated serum protein) determination in hemolytic samples from cadavers was investigated for the postmortem diagnosis of diabetes mellitus. Fructosamine level is usually measured by the reduction of nitroblue tetrazolium (NBT) using a spectrophotometer. This assay was significantly disturbed by more than 1 g/l hemoglobin, which strongly reduced NBT by the catalytic action of the sulfhydryl and glycated groups. Glycated and total hemoglobin levels were then determined simultaneously to exclude the interferences. Total protein concentration was analyzed to eliminate dilutional effects by hemolysis. With these modifications, corrected fructosamine levels in samples containing not more than 10 g/l hemoglobin could be estimated. The assay of such hemolytic samples from 32 cadavers indicated higher fructosamine values in diabetic group than in non-diabetic subjects and the postmortem degradation of the levels as previously reported.
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PMID:Colorimetric determination of fructosamine in hemolytic samples for the postmortem diagnosis of diabetes mellitus. 181 Nov 1


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