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

Levels of fasting blood glucose, serum beta-glucuronidase and beta-N-acetylglucosaminidase in 47 Libyan diabetic patients were determined. The respective mean values were 254.5 +/- 11 mg/dl, 74 +/- 5.7 Sigma units/ml and 171.8 +/- 25.5 microM PNP/dl. The mean body mass index and duration of diabetes of the patients were 30.5 +/- 0.91 kg/m2 and 7.5 +/- 1.16 years, respectively. Statistically significant correlations were found between fasting blood glucose and serum beta-glucuronidase levels (r = 0.65; p less than 0.001) and also between fasting blood glucose and beta-N-acetylglucosaminidase levels (r = 0.58; p less than 0.001). The activities of these two enzymes increase in serum with increasing fasting blood glucose levels. Patients with positive family history of diabetes have higher activities of these two enzymes than those without positive history of diabetes in the family. Patients with secondary complications have both enzymes elevated as compared with patients without secondary complications. Female patients have higher beta-N-acetylglucosaminidase activity and lower beta-glucuronidase activity than males. Age and duration of diabetes do not appear to have any effect on the activities of these enzymes.
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PMID:Serum beta-glycosidases in diabetes mellitus. 280 66

Alterations in the cardiac tissue and serum acid hydrolase activities were studied in chronic streptozotocin-induced diabetes in rats. No changes were observed in total cardiac tissue homogenate lysosomal enzyme activities at 4 weeks of diabetes but there were significant alterations in the distribution of selected enzymes. Significant decreases in nonsedimentable beta-N-acetylglucosaminidase (NAG) and beta-galactosidase (Gal) activities were observed at 4 weeks of diabetes. At 8 weeks of the disease, decreased activities of NAG and Gal were observed in heart homogenates but no changes were apparent in alpha-mannosidase (Man) or acid phosphatase activities. Nonsedimentable activities of NAG and both sedimentable and nonsedimentable activities of Gal were decreased at 8 weeks. At 16 weeks of the diabetic condition, increased activities of NAG, Gal and acid phosphatase were observed. This increase at 16 weeks of the disease was due to an increase in sedimentable enzyme activity. At all times of diabetes, serum enzyme activities were significantly increased. Insulin treatment reversed all of the observed changes in tissue homogenates, but serum levels were not completely reversed. These results suggest that cardiac lysosomal hydrolases are probably only involved in the later stages of the diabetic cardiomyopathy when extensive ultrastructural derangements are evident. The present evidence also suggests that the heart may be a source of serum hydrolase activities.
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PMID:Alterations in heart and serum lysosomal activities in streptozotocin-induced diabetes. 295 2

The effects of glucose and insulin in culture medium on the release and cellular content of beta-hexosaminidase were studied in fibroblast cultures obtained from patients with type II diabetes and from control subjects. The release of beta-hexosaminidase was (positively) correlated to extracellular glucose concentration. The cellular activity was not influenced by glucose. Insulin had no effect on the cellular activity or the release of beta-hexosaminidase. The results were similar for both cell types. It is proposed that increased plasma levels of lysosomal hydrolases (e.g. beta-hexosaminidase) from human diabetics might be due to increased release from cells exposed to elevated glucose concentrations.
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PMID:The effects of glucose and insulin on beta-hexosaminidase in cultured fibroblasts from diabetic and non-diabetic subjects. 315 29

The pattern of islet lysosomal enzyme activities, islet insulin concentration and the plasma levels of insulin and glucose were studied in freely fed mice after the in vivo administration of diazoxide in doses known to induce crinophagy in islet beta-cells. After diazoxide treatment at time 0 and at 18 hr, the plasma glucose levels at 20 hr were markedly enhanced from 6.6 +/- 0.2 mmol/l (controls) to 27.2 +/- 2.7 mmol/l (diazoxide). Inhibition of insulin secretion by diazoxide was reflected in the insulinogenic index, which was reduced by approximately 40% (p less than 0.01) in the diazoxide-treated animals, who also displayed an increased concentration of islet insulin (+50%; p less than 0.01). Moreover, we found that the activities of certain lysosomal enzymes in islet tissue were markedly increased following diazoxide treatment. Thus the activities of the acid phosphatase, (+57%; p less than 0.02) the hexosaminidase N-acetyl-beta-D-glucosaminidase, (+52%; p less than 0.001), and the carboxyl proteinase cathepsin D (+41%; p less than 0.001), were all enhanced after diazoxide, whereas the activity of another lysosomal enzyme, the glycogen hydrolysing acid amyloglucosidase, was not altered by diazoxide treatment. The present data thus indicate that the morphological observation of diazoxide-induced crinophagy in pancreatic beta-cells has a biochemical correlate in enhanced levels of certain islet lysosomal enzyme activities known to participate in degradative processes. The results also suggest that islet lysosomal enzyme activities and/or lysosome populations can be modulated by a relative independence from each other.
Diabetes Res 1987 Oct
PMID:Biochemical determination of islet lysosomal enzyme activities following crinophagy-stimulating treatment with diazoxide in mice. 332 35

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

We report on a 26-yr-old patient with an 11-yr history of insulin-dependent diabetes mellitus who exhibited insulin resistance with a requirement of up to 15,000 U of intravenous (i.v.) insulin/day. Attempts to diminish her insulin requirement by administration of sulfated insulin or Trasylol were unsuccessful, with the patient remaining resistant to subcutaneous (s.c.) and i.v. administration of pure pork insulin. Chloroquine phosphate therapy (500 mg twice a day) resulted in a decreased requirement for i.v. insulin (700 U/day as compared with the pretreatment requirement of 8400 U/day). Accelerated insulin degradation in s.c. fat tissue of the patient before treatment with chloroquine was demonstrated. This activity was decreased by 64% during chloroquine therapy. Inhibition of insulin degrading activity (IDA) during chloroquine therapy was associated with reductions in the leukocyte lysosomal enzymes alpha-galactosidase and hexosaminidase-A but not hexosaminidase-B and beta-glucuronidase. This study constitutes the first reported use of chloroquine for treatment of insulin resistance as a result of accelerated insulin degradation, and it provides evidence of the effectiveness of this agent in this rare condition.
Diabetes 1984 Dec
PMID:In vivo chloroquine-induced inhibition of insulin degradation in a diabetic patient with severe insulin resistance. 609 90

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

Plasma beta-N-acetylglucosaminidase (NAG) activity was measured in streptozotocin diabetic rats, in non-diabetic rats during starvation and refeeding, and in diabetic patients and normal subjects. The enzyme activity increased significantly in the diabetic rats and in the starved non-diabetic rats. The activity decreased markedly after insulin injection in diabetic rats and after refeeding in non-diabetic rats. The plasma NAG activity (532 +/- 24 nmole/hr/ml, M +/- SE) in 21 diabetics with FBS value less than 100 mg/dl was higher than the enzyme activity (455 +/- 15) in 42 normal subjects (p < 0.01), supporting the idea that a more intensive treatment is necessary to normalize the metabolic derangement of diabetes. There was no significant difference between diabetics with and without microangiopathy. While the influence of age and abnormal liver function was noted, there was no correlation between the NAG activity and the platelet adhesiveness or between the NAG activity and the plasma triglyceride. The results suggest that the plasma NAG activity increases in diabetes mellitus, either with microangiopathy or not. The reason for the failure to demonstrate a significant correlation between the total plasma NAG activity and microangiopathy is discussed. The analysis of the subfractionation of the plasma NAG may be necessary to disclose a significant correlation with microangiopathy.
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PMID:Studies of plasma beta-N-acetylglucosaminidase activity in experimental and clinical diabetes mellitus. 645 Jun 78

In order to elucidate the factors influencing the development of diabetic vascular complications, a retrospective clinical study was carried out in 255 patients, who had been treated in our diabetes clinic for more than 10 years. The patients were divided into three groups according to their retinal lesions: group A, 89, had no retinal lesions; group B, 118, Scott I and II; and group C, 48, Scott III or more advanced lesions. Although there were no significant differences in body weight or age at onset of diabetes between the three groups, the severity of the disease at the first visit and the method of treatment were regarded as important factors in the development of vascular complications. Hypertension, albuminuria and hypercholesterolemia were observed more often in group C than groups A and B, while there was no difference in EKG abnormalities between the three groups. No significant difference was demonstrated concerning control of blood glucose, incidence of hypoglycemia, urinary glucose and ketone bodies, serum triglyceride, hemoglobin A1c, beta-N-acetylglucosaminidase or serum lipoperoxide. These results suggest that the complicated mechanism involved in the development of vascular complications should be investigated and a long-term dynamic observation should be carried out.
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PMID:Factors influencing the development of diabetic vascular complications. 668 May 32

Rates of proteolysis by hearts obtained from alloxan diabetic rats and perfused as working preparations with buffer simulating control sera were accelerated 30% above identically perfused control hearts. The total homogenate activities of cathepsin D and beta-N-acetylglucosaminidase, assayed in the presence of Triton X-100, decreased 15-35% in diabetic heart, but the activities of these lysosomal enzymes assayable in the absence of detergent were unchanged in the diabetic tissue. The effects of diabetes were examined further by centrifugation of particulate fractions from subtilisin-treated hearts of control and diabetic rats on polyvinylpyrrolidone-coated colloidal silica (Percoll) gradients. Two species of lysosomes were resolved on the basis of their densities. Both dense and buoyant lysosomes accumulated radioactivity when hearts were exposed to [14C]phenylalanine methyl ester. Dense lysosomes (1.06-1.09 g/ml) sedimented with mitochondria while buoyant lysosomes banded with Golgi and sarcolemmal particles (1.02-1.03 g/ml). When particulate fractions of hearts from diabetic animals were layered on the Percoll gradients, total activities of beta-N-acetylglucosaminidase and cathepsin D were decreased from control in buoyant lysosomes, but unchanged in dense lysosomes. These results demonstrated that the increase in proteolysis in the diabetic heart was associated with decreased total activity and latency of cathepsin D and beta-N-acetylglucosaminidase and an increased proportion of dense lysosomes in the particulate fraction.
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PMID:Effects of diabetes on cardiac lysosomes and protein degradation. 686 24


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