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)

1. Six weeks after the injection of streptozotocin at 125 mg/kg i.p. in the AV line nondiabetic Chinese hamsters, the animals showed hyperglycemia, increased kidney, pancreas and stomach weights and stomach glucagon contents and depletion of insulin and glucagon in the pancreas. 2. Plasma beta-D-galactosidase and N-acetyl-beta-D-glucosaminidase were elevated; whereas alpha-D-glucosidase was decreased and alpha-D-galactosidase remained unchanged in the plasma. 3. In the kidney, streptozotocin-diabetes led to depression of alpha-D-mannosidase, beta-D-fucosidase and N-acetyl-beta-D-glucosaminidase activities in both 12,000 g supernatant and precipitate fractions, decreases in alpha-D-glucosidase in the supernatant only and no change in alpha-L-fucosidase, alpha-D-galactosidase, beta-D-galactosidase and beta-D-glucuronidase. 4. In the liver, significant increases in N-acetyl-beta-D-glucosaminidase, alpha-D-galactosidase, beta-D-galactosidase, beta-D-fucosidase, beta-D-glucosidase and alpha-D-mannosidase were found in either the supernatant or the precipitate fraction of the diabetic animals. The data indicate diabetes-dependent tissue-specific changes in glycohydrolases in the Chinese hamster.
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PMID:Alterations in glycohydrolase activities in streptozotocin-diabetic Chinese hamsters (Cricetulus griseus). 31 16

Lysosomal enzymes degrade membrane glycoconjugates, and increased circulating enzyme activity may be an important mechanism in the pathogenesis of diabetic microangiopathy. We have assayed a profile of seven lysosomal enzyme activities (nmol.h-1.ml-1) in platelet-free plasma from 54 Type 1 (insulin-dependent) diabetic subjects (median age 31 years) and 42 matched normal control subjects. A significant increase in median (interquartile range) enzyme activity was measured in diabetic compared to control subjects for beta-D-glucuronidase, 121 (97.7-171) vs 88.8 (62.8-113), p less than 0.001; beta-D-Nacetylglucosaminidase, 693 (568-799) vs 568 (462-686), p less than 0.001; alpha-D-mannosidase, 23.8 (16.7-28.9) vs 14.5 (10.1-20.0), p less than 0.001; and beta-D-galactosidase, 6.94 (6.11-9.99) vs 6.66 (4.78-8.33), p less than 0.04. In contrast, alpha-L-fucosidase, alpha-D-galactosidase and beta-D-mannosidase activities were similar in diabetic and control subjects. None of the enzyme activities differed significantly (p less than 0.05) between 24 diabetic patients with clinical complications and 30 complication-free diabetic patients with similar glycaemic control which does not support the hypothesis that enzyme increases in diabetes arise simply by leakage from damaged tissues. In the diabetic subjects HbA1, median (interquartile range) 9.10 (7.40-10.60), was significantly related to beta-D-glucuronidase (rs = 0.56, p less than 0.001) and beta-D-Nacetylglucosaminidase (rs = 0.55, p less than 0.001). We have therefore demonstrated in diabetic subjects an increase in certain lysosomal glycosidases, that correlates with glycaemic control.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Increases in plasma lysosomal enzymes in type 1 (insulin-dependent) diabetes mellitus: relationship to diabetic complications and glycaemic control. 145 59

The plasma levels of three lysosomal enzymes, beta-D-N-acetylglucosaminidase, beta-D-glucuronidase, and alpha-L-fucosidase, were fluorimetrically determined in seven insulin-dependent diabetic patients one day before, one day after, and during a two-day treatment with the artificial pancreas, at 4 to 5 h intervals. A statistically significant decrease of the plasma level of each enzyme was observed during artificial pancreas treatment. The extent of decrease was 30 to 35% for beta-N-acetylglucosaminidase, 35 to 40% for beta-D-glucuronidase, and 20 to 25% for alpha-L-fucosidase. The decrease occurred earlier (at the first day of treatment) for beta-D-N-acetylglucosaminidase, and later (at the second day of treatment, and lasting to the first day after treatment) for the other two enzymes. These results suggest a direct connection between the lysosomal apparatus and insulin-controlled metabolic pathways, and a potential role for lysosomal enzymes as indicators of the metabolic compensation in diabetes.
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PMID:Behaviour of some lysosomal enzymes in the plasma of insulin dependent diabetic patients during artificial pancreas treatment. 343 39

A study of four lysosomal glycosidases' activities was carried out on sera from 64 diabetic patients, which revealed important variations in comparison with the activities observed in sera of control subjects. Depending on the type of diabetes mellitus (I, insulin-dependent, or II, non-insulin-dependent), three activities were more or less increased: alpha-L-fucosidase, alpha-D-mannosidase, and N-acetyl-beta-D-glucosaminidase, in agreement with previously published results. Against that, the beta-D-mannosidase activity shows a highly significant decrease in sera from either diabetic type. Up to now, no suitable explanation has been found for these variations occurring in an unusual direction.
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PMID:Decreased serum beta-D-mannosidase activity in diabetic patients, in comparison with other glycosidases. 405 98

The activities of several glycosidases (alpha-L-fucosidase, alpha-D-mannosidase, alpha-D-galactosidase, beta-D-galactosidase, beta-N-acetylglucosaminidase and beta-D-glucuronidase) were determined in human sera from 10 normal subjects and in three groups each of 10 patients with diabetes mellitus, hepatic cirrhosis and gastric carcinoma. The results show significantly higher activities in the patients for alpha-L-fucosidase (p less than 0.001) and for beta-N-acetylglucosaminidase (p less than 0.1, p less than 0.001 and p less than 0.05, respectively), and smaller or not significantly greater values for the other glycosidases.
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PMID:Increased serum alpha-L-fucosidase and beta-N-acetylglucosaminidase activities in diabetic, cirrhotic and gastric cancer patients. 624 16

N-Acetyl beta-D-glucosaminidase and alpha-L-fucosidase were determined in human sera from 25 control subjects, in 23 diabetic patients without retinopathy and in 22 diabetic patients with retinopathy. The results show significantly higher N-acetyl beta-D-glucosaminidase activity in diabetic patients independently of the development of retinopathy and also independently of the length of diabetes. No correlation was found between either serum enzymes and serum glucose concentration and glycosylated hemoglobin (HbA1).
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PMID:N-acetyl beta-D-glucosaminidase and alpha-L-fucosidase activities in relation to glycosylated hemoglobin levels and to retinopathy in diabetes. 710 1

L-Fucose is a monosaccharide that is present at low concentrations in serum and is a normal constituent of glycoproteins. In some pathological conditions, such as cancer, rheumatoid arthritis, and diabetes, there is an abnormal fucosylation of acute phase serum proteins. Because most serum proteins are produced in the liver, we have examined L-fucose accumulation, metabolism, and secretion of L-fucose-containing proteins in human Hep G2 liver cells. Accumulation of L-fucose by Hep G2 cells approached 3.5 nmol/mg protein after a 48 h incubation. This accumulation appears similar to accumulation in other cells, which we have shown occurs via a specific transport protein. Exogenous L-fucose was incorporated into protein in both O- and N-linked glycosidic linkages. After a 48 h incubation, 61% of the accumulated L-fucose was incorporated into protein and secreted into the medium, whereas 39% of the L-fucose remaining in the cells was incorporated into integral membrane proteins. Utilizing reverse-phase high-performance liquid chromatographic separation of L-[5,6-(3)H]fucose-containing proteins and detection by scintillation counting, we determined that two major fucoproteins and numerous minor fucoproteins were produced and secreted by normal Hep G2 cells. This elution profile was unchanged when glucose-conditioned cells were examined. By size-separating secreted proteins by nondenaturing HPLC we determined that the size of the two major fucoproteins were approximately 60 and approximately 100 kDa. In these studies we also examined the effect of diabetes on hepatic fucosyltransferase and serum alpha-L-fucosidase activity and found that the activity of these enzymes is increased by 40 and 100%, respectively in diabetic rats.
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PMID:Effect of L-fucose and D-glucose concentration on L-fucoprotein metabolism in human Hep G2 cells and changes in fucosyltransferase and alpha-L-fucosidase activity in liver of diabetic rats. 913 43

The erythrocyte membrane in 71 patients with type 2 diabetes mellitus was assessed for glycohydrolase activity: N-acetyl-beta-D-glucosaminidase, beta-D-glucuronidase, alpha- and beta-D-galactosidase, alpha- and beta-D-glucosidase, alpha-D-mannosidase, and alpha-L-fucosidase. Only beta-D-glucuronidase, alpha-D-glucosidase, and beta-D-glucosidase showed markedly elevated levels with respect to the controls regardless of the presence of complications. Among the examined patients, those with good metabolic control (not yet submitted to any therapy) showed the same enzyme levels as the reference subjects, while the levels in patients with unsatisfactory metabolic control (treated with oral hypoglycemic and/or insulin) significantly differed from the control levels. For alpha-D-glucosidase and beta-glucosidase, a correlation with glycemia and the parameters of metabolic control was also evidenced. Alterations of beta-D-glucuronidase, alpha-D-glucosidase, and beta-D-glucosidase were also ascertained in the plasma of the same diabetic patients according to the literature; each enzyme correlated with the other, either in plasma or in the erythrocyte membrane. This study shows a correlation between plasma and erythrocyte membrane levels for these three enzymes. The strict parallelism of the glycohydrolases in the two different compartments provides a profile of these enzymes in the pathology of diabetes.
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PMID:Alterations in the activity of several glycohydrolases in red blood cell membrane from type 2 diabetes mellitus patients. 1042 Dec 18

Chromatographic separation of the pod extract of Angylocalyx pynaertii resulted in the isolation of 13 sugar-mimic alkaloids (1-13). The structures of the new alkaloids were elucidated by spectroscopic methods as the 6-O-beta-D-glucoside (10) and N-hydroxyethyl derivative (11) of 1,4-dideoxy-1,4-imino-D-arabinitol (DAB) (1), 1,6-dideoxynojirimycin (12), and 1,3,4-trideoxynojirimycin (13). 2,5-Imino-1,2,5-trideoxy-L-glucitol (7), 2,5-dideoxy-2,5-imino-D-fucitol (8), and beta-homofuconojirimycin (9), isolated from the pods as well as the bark, were very specific inhibitors of alpha-L-fucosidase with no significant inhibitory activity toward other glycosidases. In this work, 1,4-dideoxy-1,4-imino-D-ribitol (6) was found to be a better inhibitor of lysosomal beta-mannosidase than 2,5-imino-1,2,5-trideoxy-D-mannitol (2). N-Hydroxyethyl-1-deoxynojirimycin (miglitol), which is commercially available for the treatment of diabetes, retained its inhibitory potential toward rat intestinal maltase and sucrase, whereas 11 and the synthetic N-hydroxyethyl derivative of 2,5-dideoxy-2,5-imino-D-mannitol markedly lowered or abolished their inhibition toward all enzymes tested.
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PMID:New sugar-mimic alkaloids from the pods of Angylocalyx pynaertii. 1185 56

Disturbed metabolism of glycosaminoglycans (GAGs) has been proposed to play an important role in the pathogenesis of late diabetic complications. The effect of diabetic complications and metabolic control on both total serum GAGs content and the serum activity of lysosomal glycosidases (N-acetyl-beta-D-glucosaminidase, alpha-L-fucosidase, beta-D-galactosidase, and alpha-D-mannosidase) contributing to GAGs degradation, was investigated in 48 patients with type 2 diabetes mellitus. The activity of beta-D-glucosidase and acid phosphatase, the lysosomal enzymes unrelated to GAGs metabolism, was determined for comparison. The elevated serum total GAG concentration in diabetic patients was strongly and positively influenced by poor metabolic compensation of diabetes and the presence of vascular complications. A similar tendency has been shown in regard to the activity of enzymes involved in GAG degradation, especially N-acetyl-beta-D-glucosaminidase, alpha-L-fucosidase and beta-D-galactosidase. Furthermore, the total serum GAG concentrations, as well as the activity of lysosomal enzymes involved in the extracellular matrix degradation, closely followed metabolic compensation, regardless of diabetic vascular complications. Thus, we suggest that increased values of the investigated parameters may indicate the degree of endothelial cell dysfunction and may be useful to predict the development of diabetic vascular pathology.
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PMID:Alterations of glycosaminoglycan metabolism in the development of diabetic complications in relation to metabolic control. 1617 71


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