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

The fractions of lipoproteids, lactate dehydrogenase (LDH), malate dehydrogenase (MDH) and their isoenzymes as well as the fructoso-1-phosphate aldolase (F-1-PhA) and cholinesterase (ChE) activity were studied in 220 patients with diabetes mellitus, of which 156 had diabetes mellitus combined with ischemic heart disease (IHD). It was shown that the level of atherogenic lipoproteids is augmented in all the forms of diabetes mellitus and its latent stage, their highest content being seen in the disease, aggravated by IHD. An elevated level of pre-beta-lipoproteid atherogenic fraction was more common in diabetics with IHD. An increased F-1PhA and LDH5 activity was observed in all the patients examined, whereas in severe diabetes mellitus a decrease in the ChE activity was seen. The composed table of changes in the enzyme activity and atherogenic lipoproteid levels in diabetes mellitus combined with IHD, significantly differing from those of the diabetics without IHD, can be used for early IHD diagnosing in diabetes mellitus patients.
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PMID:[Diagnostic coefficients of ischemic heart disease in diabetes mellitus]. 688 7

Tissue samples were taken from the gastrocnemius muscle of 26 randomly selected, glucose-tolerant, 48-yr-old men. Hexokinase, phosphorylase, lactate dehydrogenase (LDH), succinate dehydrogenase, and lipoprotein lipase activity (LPLA), as well as the area per fiber type and capillary density, were determined. Mean fiber area correlated positively with relative body weight (r equals 0.53, P less than 0.01), but capillary density did not. The result is that, in cases of high body weight, each capillary supplies a larger muscle fiber area. Serum insulin concentration in the fasting state correlated positively with body weight (r equals 0.77, P less than 0.001) and with mean fiber area per capillary (r equals 0.87; P less than 0.001). Only during the latter part of an oral glucose tolerance test (OGTT) did blood glucose concentrations correlate with relative body weight and mean fiber area per capillary (r equals 0.42, r equals 0.51, P less than 0.05). A stepwise multiple regression analysis showed that the different muscle morphology measurements could account for 3/4 of the variation in the fasting serum insulin concentration, the fasting insulin/glucose ratio, and the blood glucose concentration at 120 min in the OGTT. Of the intracellular enzymes, only LDH (r equals -0.71, P less than 0.001) correlated with the mean fiber area per capillary. LPLA correlated with capillary density (r equals 0.66, P less than 0.001), and, long with the muscle morphology measurements, could account for 3/4 of the variation in serum triglyceride concentrations. The results show that a large mean muscle fiber area/capillary ratio indicates a morphologic imbalance, which is related to both glucose tolerance and various degrees of insulin sensitivity.
Diabetes 1981 Jan
PMID:Body weight, skeletal muscle morphology, and enzyme activities in relation to fasting serum insulin concentration and glucose tolerance in 48-year-old men. 701 1

Arylsulfonylamino acids, displaying a wide range of inhibitory activities versus rat lens aldose reductase (RLAR), were analyzed for enzyme selectivity in several test systems. These RLAR inhibitors were found not to produce significant inhibition of genetically-linked reductases (aldehyde reductase, ALR), catalytically similar reductases (Pachysolen tannophilus xylose reductase, PTXR), functionally distinct oxidoreductases (glutathione reductase, GR, lactate dehydrogenase, LDH, and gamma-transaminase, GABA-T), and thymidylate synthase (TS). These data suggest that aldose reductase differs significantly from other oxidoreductases in its inhibitor binding domain(s). Furthermore, the aldose reductase selectivity demonstrated by the arylsulfonylamino acids suggests that these compounds may not inhibit other key metabolic transformations in various cell types and that they may function as selective probes for studies of the relationship between aldose reductase mediated biochemical changes and the pathologies of chronic diabetes.
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PMID:Enzyme selectivity analyses of arylsulfonylamino acid aldose reductase inhibitors. 750 72

Glucagonoma Syndrome is a rare syndrome comprising hyperglucagonemia, diabetes mellitus, necrolytic migratory erythema and hypoaminoacidemia in the setting of a glucagon producing, alpha cell tumour of the pancreas. We report a case of Glucagonoma Syndrome palliatively treated successfully with octreotide. In addition to classical clinical and biochemical findings, this patient also had a Glomus Jugulare tumour, and Empty Sella Syndrome and demonstrated an unusual pattern of plasma lactate dehydrogenase isoenzymes, features not previously reported in this syndrome.
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PMID:Glucagonoma syndrome with increased lactate dehydrogenase isoenzymes: octreotide treatment. 752 1

CBL/57 strain db/db mice exhibit type II (noninsulin-dependent) diabetes. The affected mice are markedly hyperinsulinemic, hyperglycemic, and hypercholesterolemic, and their serum K+ levels are decreased. The brains of the diabetic mice are significantly smaller than those of their lean, control littermates, but the protein concentration is normal. The low brain weight is accompanied by a loss of major fatty acid components within the whole brain, nerve endings, and mitochondrial membranes. Cholesterol levels are low in whole brain but are not significantly different from normal in the synaptosomal membranes. The phospholipid concentration is significantly decreased in whole brain homogenates, crude synaptosomal membranes, and crude mitochondrial membranes of the diabetic mice. In addition, the specific activities of membrane-bound synaptosomal acetylcholinesterase, Na+,K(+)-ATPase, and Mg(2+)-ATPase are decreased in crude synaptosomal membranes of the diabetic mice. The specific activities of carnitine palmitoyltransferase I and carnitine acetyltransferase are significantly increased in the crude mitochondrial fraction isolated from the brains of the type II diabetic mice, whereas the specific activity of pyruvate dehydrogenase complex is decreased. The specific activities of two other mitochondrial enzymes--monoamine oxidase B and citrate synthase--and a cytosolic enzyme--lactate dehydrogenase--are unaltered. The ability to synthesize cyclic AMP is markedly decreased in the brains of the diabetic mice. The concentrations of carnitine and of the amino acids, glutamate, aspartate, glutamine, and serine are unaltered, whereas glycine levels are significantly elevated in the brains of the db/db mice. The data suggest that in vivo the brains of the diabetic mice exhibit a decreased capacity for glucose oxidation and increased capacity for fatty acid oxidation. This hypothesis is supported by the finding that cerebral mitochondria isolated from the db/db mice oxidize [1-14C]palmitate to 14CO2 at a rate almost twice that of control mitochondria. The present findings emphasize the potentially serious alteration of brain metabolism in uncontrolled type II diabetes.
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PMID:Lipid metabolism and membrane composition are altered in the brains of type II diabetic mice. 772 1

The aim of the present study is to compare normal and tumoral pancreatic islet cells in terms of both the activity of selected cytosolic and mitochondrial enzymes participating to nutrient catabolism and the intrinsic properties of FAD-glycerophosphate dehydrogenase. The activity of the glycolytic enzymes hexokinase and lactate dehydrogenase was higher in tumoral (RINm5F) than normal islet cells. The opposite was seen for glutamate decarboxylase, glutamate-oxaloacetate transaminase, glutamate-pyruvate transaminase, glutamate dehydrogenase, 2-ketoglutarate dehydrogenase and FAD-glycerophosphate dehydrogenase (m-GDH). These findings are consistent with the high rates of glycolysis and protein synthesis seen in tumoral islet cells compared with normal islet cells, which favour mitochondrial oxidative events associated with the catabolism of D-glucose and amino acids. The intrinsic catalytic properties of m-GDH were comparable, albeit not identical, in normal and tumoral islet cells. Since a deficiency of m-GDH in pancreatic islets may represent a contributing factor in the pathogenesis of non-insulin-dependent diabetes, it is proposed that RINm5F cells may readily yield sufficient islet m-GDH for purification and further gene cloning.
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PMID:Activity of cytosolic and mitochondrial enzymes participating in nutrient catabolism of normal and tumoral islet cells. 776 86

Serial changes in myocardial parameters related to non-insulin-dependent diabetes mellitus were investigated in DDY mice (control), untreated KK mice, and KK mice treated with diltiazem (150 micrograms/kg body weight, KKd1: or 300 micrograms/kg body weight diltiazem, KKd2). The isozyme ratio of lactate dehydrogenase (LDH) [(LDH1+LDH2)/(LDH4+LDH5)] was used as an index of aerobic metabolism of myocardial tissue. Mean blood sugar levels did not vary between 5 weeks and 30 weeks of age, ranging from 108 (range 60-198) mg/dl in DDY mice to 170 (range 110-282) mg/dl in KK mice. The ratio of heart weight to body weight was larger in KK mice than in DDY mice at 20 weeks of age, but was unaffected by diltiazem treatment. The LDH isozyme ratio showed that DDY mice were in an aerobic state at 15 and 20 weeks of age, while KK mice were in an anaerobic state at 10 and 15 weeks of age. The KKd1 and KKd2 groups exhibited the same LDH isozyme ratios as untreated KK mice; diltiazem had no effect on the LDH isozyme ratio at 20 and 30 weeks of age. The mean diameter of myocytes was increased in KK mice but diltiazem had no effect on this parameter. Interstitial fibrotic changes appeared at 15 weeks in untreated KK mice and progressed with age. These changes were completely suppressed in KK mice treated with diltiazem. These results suggest that hyperglycemia induces an anaerobic state in heart muscle, leading to muscle hypertrophy, degeneration, and fibrosis and that calcium antagonists may suppress these pathological changes.
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PMID:Correlation between metabolic and histopathological changes in the myocardium of the KK mouse. Effect of diltiazem on the diabetic heart. 830 47

An electrophoretic variant of the lactate dehydrogenase (LDH)-B(H) subunit was discovered in a patient with diabetes mellitus. His LDH activity in serum was slightly lower than normal and the LDH isozyme pattern showed an abnormal migration indicating an LDH-B subunit variant of the fast type. The LDH containing the variant subunit revealed a decreased heat stability. DNA analysis of the variant allele detected a base substitution, an A to G transition, at codon 6 (AAA-->GAA). The mutation resulted in the replacement of a lysine by a glutamic acid (K6E). The change may cause the heat instability and affect the net charge of the variant subunit, resulting in an electrophoretic LDH-B subunit variant of the fast type.
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PMID:Analysis of a genetic mutation in an electrophoretic variant of the human lactate dehydrogenase-B(H) subunit. 831 53

Although inflammatory or degenerative changes in salivary glands have been demonstrated in genetic animal models of diabetes mellitus and in experimental diabetes, no information is available in diabetics on the possible leakage in saliva of cytosolic enzymes as markers of salivary cell injury. Aspartate (GOT) and alanine (GPT) aminotransferases and lactate dehydrogenase (LDH) were determined in saliva samples collected by the Salivette method from well-controlled insulin-dependent (IDDM n = 11) and non-insulin-dependent (NIDDM n = 18) diabetic patients and from age-cross-matched healthy subjects (n = 33). In IDDM salivary concentrations of GOT (112.55 +/- 23.94 UI/L) and LDH (1120.27 +/- 168.31 UI/L) were similar to those found in the NIDDM (90.94 +/- 19.64, and 1255.43 +/- 221.40 UI/L respectively), but higher (p < 0.05) than those observed in normal subjects (33.09 +/- 3.71, and 423.58 +/- 39.94, UI/L respectively). GPT was higher in NIDDM than IDDM, which in turn was higher than in normal subjects (42.78 +/- 14.72, 16.45 +/- 3.74 and 6.85 +/- 1.52 UI/L respectively). Salivary and serum values of GOT, GPT and LDH were not correlated. Determination of cytosolic enzymes in saliva may be useful for monitoring the diabetic involvement of salivary glands.
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PMID:Aminotransferases and lactate dehydrogenase in saliva of diabetic patients. 844 46

Force generation and tissue glucose metabolism were measured in the urinary bladder smooth muscle from rats with streptozotocin-induced diabetes (7-8 wk duration). Bladder wet wt was almost 4-fold higher in the diabetic animals compared with the untreated controls. Morphological analysis showed that the growth was associated with hypertrophy of the smooth muscle component in the bladder wall. Force generation of isolated bladder strip preparations was measured in vitro at different ambient oxygen tensions. Activation of intramural nerves, with electrical field stimulation, induced contractions that were unaffected by reduction of oxygen tension down to PO2 100 mmHg for both control and diabetic muscle strips. At zero PO2 force was reduced by approximately 10-20%, in both groups. High-K+ solution induced 'tonic' contractions that were slightly more inhibited by lowering PO2. At intermediate PO2 (between 100 and 20 mmHg) the diabetic muscle gave slightly higher force. At zero PO2 no significant difference could be detected between strips from control and diabetic animals. Oxygen consumption and lactate production in the preparations were determined at a PO2 of 290 mmHg and related to the volume of smooth muscle. At zero PO2, lactate formation increased 3- to 4-fold. The metabolic tension cost was lower at zero PO2. No differences in basal and contraction related metabolic rates could be detected between the two groups under normoxic and anoxic conditions. The maximal activity of lactate dehydrogenase (LDH) determined in tissue samples was about 2-fold higher in the diabetic bladder muscle.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Energy turnover and lactate dehydrogenase activity in detrusor smooth muscle from rats with streptozotocin-induced diabetes. 849 74


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