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

Measurements have been made of the total hexokinase activity and of the relative amounts of types I and II hexokinase in rat mammary gland and at different stages of the lactation cycle. The total hexokinase activity increased during lactation, that of type II increasing to a greater extent than that of type I; the type II/type I activity ratio rose from a pregnancy value of about 1 to a mid-lactation value of 3, returning to 1 on involution. The changes in type II hexokinase activity during the lactation cycle parallel the changes in the insulin sensitivity of mammary-gland tissue. A study of the effect of alloxan-diabetes on mammary-gland hexokinase during the mid-lactation period revealed that, although the total glucose-phosphorylating capacity of the mammary gland was almost unchanged, the relative contributions of type I and type II hexokinases altered, decreasing the type II/type I activity ratio to about 1.
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PMID:Multiple forms of glucose-adenosine triphosphate phosphotransferase in rat mammary gland. 604 24

The activity of hepatic fructokinase increased about 2-fold in desert-derived spiny mice (Acomys cahirinus) and laboratory bred albino mice and rats, maintained on a 50% sucrose diet for 3 months. The role of fructose as the specific inducer was apparent, as 25% fructose diet produced activity increases similar to those of sucrose in contrast to 25% glucose diet. The activity of hexokinase was not affected by the sucrose diet, that of glucokinase rose marginally but those of pyruvate kinase and NADP-malate dehydrogenase rose pronouncedly, especially in the spiny mice. Fructokinase activity increased significantly only after 2 weeks on the diet and continued to rise gradually. The activities of other gycolytic enzymes rose markedly already after 3 days and peaked at about 14 days. Fasting for 48 hr did not influence fructokinase activity while markedly reducing that of glucokinase, pyruvate kinase and NADP-malate dehydrogenase. Streptozotocin diabetes in rats resulted in a 40% reduction in fructokinase activity after 14 days which was restored after 6 days of insulin treatment. The activity increases of other glycolytic enzymes were more marked. However, the fructokinase induction on the sucrose diet was evident also in diabetic rats, suggesting that the insulin and substrate effects are independent. The preference of fructose over glucose phosphorylation capacity was clearly demonstrable in the non-diabetic and diabetic rats and became enhanced on sucrose feeding. The activity of triokinase also increased on the sucrose diet in the 3 rodent species, suggesting a coordinative substrate effect on the induction of these two rate-limiting fructolysis enzymes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Response of hepatic fructokinase to long-term sucrose diets and diabetes in spiny mice, albino mice and rats. 608 70

The effects of diabetes on hepatic carbohydrate metabolism were investigated in spontaneously diabetic Bio-Breeding Worcester (BB/W) rats. The juvenile-onset-type syndrome displayed by these animals is characterized by beta-cell destruction with subsequent ketosis-prone insulinopenia. Livers from diabetic animals demonstrated increased adenosine 3',5'-cyclic monophosphate levels but subnormal total protein and glycogen content. Isolated perfused livers of diabetic BB/W rats demonstrated an increased rate of glucose production from [14C]lactate and an impaired rate of glycogen synthesis. These data were consonant with hepatic enzyme studies demonstrating markedly increased activities of component gluconeogenic (glucose-6-phosphatase, fructose-1,6-diphosphatase, phosphoenolpyruvate carboxykinase) and glycogenolytic (glycogen phosphorylase) enzymes with decreased activities of glycolytic (hexokinase, pyruvate kinase) and glycogenic (glycogen synthase) enzymes. These findings agree with previous studies using alloxan- and streptozotocin-induced diabetic animals and suggest that accelerated hepatic gluconeogenesis and impaired glucose utilization are pathognomonic of all insulin-deficient diabetic syndromes.
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PMID:Hepatic carbohydrate metabolism in the spontaneously diabetic Bio-Breeding Worcester rat. 625 45

The activities of hexokinase, glucose-6-phosphate dehydrogenase, hydroxyacyl-CoA-dehydrogenase, adenylate kinase and glutathione reductase were determined in the aorta of rats made diabetics with streptozotocin for over two weeks and in noninjected controls. Adenosinetriphosphate (ATP) and total adenine nucleotide content were also measured. Glutathione reductase activity was not significantly changed in the diabetic aorta whereas the activities of glucose-6-phosphate dehydrogenase, hydroxyacyl-CoA-dehydrogenase and adenylate kinase were all increased. Hexokinase activity was significantly decreased in diabetic rat aorta. When measured after incubation in vitro for 2 h with 5.6 mmol/l glucose, the ATP-concentration was reduced in the diabetic aorta while the total concentration of adenine nucleotides was unchanged. Insulin treatment started three days after induction of diabetes with streptozotocin and continued for twelve days restored the growth rate of the rats but their glucose metabolism was not completely normalized. After insulin treatment no significant differences between diabetic and normal rats were found in the aortic activities of glucose-6-phosphate dehydrogenase, hydroxyacyl-CoA-dehydrogenase, adenylate kinase or in the ATP content.
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PMID:Influence of diabetes on enzyme activities in rat aorta. 626 26

We evaluated the possible role of islet glucokinase in controlling the rate of islet glucose metabolism, and thereby the rate of glucose-induced insulin release. The activities of glucokinase, hexokinase, P-fructokinase, and glyceraldehyde-P dehydrogenase were quantitated in sonicated or isotonically homogenized islet preparations using pyridine nucleotide-dependent fluorometric assays. In sonicates, about 1/4 of the islet glucose phosphorylating activity was due to an enzyme with kinetic properties similar to glucokinase; 3/4 of the activity was due to hexokinase. The procedure for determining islet glucokinase activity was improved by centrifuging isotonic islet homogenates at 12,000 x g. The supernatant fraction was enriched for glucokinase. About 1/2 of the glucose phosphorylating activity in this fraction was due to glucokinase and 1/2 was due to hexokinase. The glucokinase activity in islet homogenates was !23 of the activity of hexokinase, 1/40 of the activity of P-fructokinase, and 1/400 of the activity of glyceraldehyde-P dehydrogenase. Detailed concentration dependency curves of glucose and mannose utilization were also obtained with intact isolated pancreatic rat islets. Glucose and mannose usage in islets was governed by two superimposed hyperbolic systems differing in Km and Vmax. A high Km system (Km for glucose 11 mM and for mannose 21 mM) predominated. A low Km system (Km for glucose 215 and for mannose 530 microM) contributed about 15% to the total activity. The available data with intact islets could be rationalized by the existence of two distinct hexose phosphorylating enzymes with differing capacities and kinetic properties. These enzymes, tentatively identified as glucokinase and hexokinase, could coexist in the same cell or could be distributed among different cell types. The possible physiologic significance of these results is discussed, emphasizing the idea of dual control of glycolysis and insulin release by glucokinase and hexokinase. An earlier proposal that glucokinase serves as glucoreceptor of beta-cells [J. Biol. Chem. 243:2730 (1968)] is greatly strengthened by the present studies.
Diabetes 1981 Nov
PMID:Regulation of glucose metabolism in pancreatic islets. 627 17

Streptozotocin-induced maternal diabetes has been shown to alter developmental patterns of carbohydrate-metabolizing enzyme activities, glycogen deposition and surfactant levels in late fetal rat lung in a tissue-specific manner, as follows: (a) marked reduction in glycogen synthase a activity, due to aberrant interconversion between active and inactive forms of the enzyme; less glycogen was thus accumulated; (b) lowered activities of hexokinase, phosphofructokinase and pyruvate kinase at term; (c) reduced disaturated phosphatidylcholine (surfactant) concentrations. The diminished synthesis and accumulation of glycogen and glycolytic capacity in the lungs of fetuses of diabetic mothers has been related to reduction in surfactant level, which underlies respiratory distress syndrome frequently encountered in neonates of diabetic pregnancies.
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PMID:Effects of maternal diabetes on the development of carbohydrate-metabolizing enzymes, glycogen deposition and surface active phospholipid levels in fetal rat lung. 630 58

It was shown previously in experiments on white rats with alloxan diabetes that trihydroxyoctadecadiene acids from Bryonia alba L. have a hypoglycemic action. The present paper is concerned with the effects of the above-indicated compounds on the activity of glycogen phosphorylase (a- and b-forms), phosphoprotein phosphatase and hexokinase in liver and muscle tissues of white rats with alloxan diabetes. One of the possible mechanisms of the hypoglycemic action of trihydroxyoctadecadiene acids is discussed.
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PMID:[Effect of trihydroxyoctadecadiene acids from Bryonia alba L. on the activity of glycogen metabolism enzymes in alloxan diabetes]. 632 80

Three reflectance meters available in Canada for glucose self monitoring were assessed for accuracy and reliability in determining capillary blood glucose compared with venous serum glucose assayed by the laboratory hexokinase method and to capillary whole blood glucose determined by the glucose-oxidase method on a YSI (Yellow Springs Instrument, Yellow Springs, Ohio). The readings with all three meters correlated with serum glucose rather than with whole blood glucose. The Ames Glucometer (Ames Division, Miles Laboratories, Rexdale, Ontario, Canada) was found to have the best predictive value over the full range of serum glucoses from 30 to 399 mg/dl. The Lifescan Glucoscan (Lifescan Inc., Mountainview, California), although reading satisfactorily in the range 30-180 mg/dl, significantly underestimated the capillary glucose at values greater than 180 mg/dl. The Hypoguard Hypocount B (Hypoguard Ltd., Suffolk, England) on the other hand read consistently high in the range 30-99 mg/dl but read satisfactorily over the range 100-399 mg/dl. All three methods, however, had inherent limitations that must be taken into account in their clinical application.
Diabetes Care
PMID:Self glucose monitoring: a comparison of the Glucometer, Glucoscan, and Hypocount B. 634 79

The flux of glucose through the pentose phosphate pathway, important in relation to the provision of ribose 5-phosphate for nucleotide and RNA synthesis, was decreased by 70% in the diabetic rat heart in parallel with a similar decreased flux through the glycolytic route. A common factor linking the decreased flux through these alternative routes is the known fall in cardiac hexokinase; in these experiments there is a 50% decrease in Type II hexokinase (EC 2.7.1.1.) in both soluble and particulate fractions. The level of fructose 2,6-bisphosphate, a regulator of phosphofructokinase activity, is decreased by 20% in the alloxan diabetic rat heart, this may be a significant additional factor in the marked decrease in the flux of glucose through the glycolytic route in the myocardium in diabetes.
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PMID:Regulation of alternative pathways of glucose metabolism in rat heart in alloxan diabetes: changes in the pentose phosphate pathway. 636 95

Glycosylated hemoglobin and blood sugar levels in the fasting state and two hours after oral 100 g glucose load were measured in 180 patients. Glycosylated hemoglobin was measured by cation exchange column chromatography, and blood sugar was measured by hexokinase reaction. Patients with an elevated postprandial and/or fasting blood sugar level (positive screen) subsequently underwent three-hour glucose tolerance test. The mean value of glycosylated hemoglobin in patients with a negative screen and normal hemoglobin was 6.17 +/- 0.61%; and the value for glycosylated hemoglobin in patients with class A diabetes and normal hemoglobin electrophoresis was 6.85 +/- 0.73% (P less than .001). A glycosylated hemoglobin value greater than 6.78 (mean + 1 SD) was considered elevated. Glycosylated hemoglobin values were elevated in 21 of 33 patients with gestational diabetes and in 27 of 147 patients with normal blood sugar levels. The sensitivity and specificity of glycosylated hemoglobin for the diagnosis of gestational diabetes were 63.6 and 81.6%, respectively. Fifty percent of patients with an initially elevated glycosylated hemoglobin value delivered macrosomic infants, whereas no patient with a normal glycosylated hemoglobin value had a macrosomic infant. An elevated glycosylated hemoglobin value may alert the obstetrician of a potentially elevated mean blood sugar level and may warrant aggressive management of gestational diabetes.
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PMID:Use of glycosylated hemoglobin as a screen for macrosomia in gestational diabetes. 646 65


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