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)

Plasma potassium lowering effect of a selective beta-2 adrenergic stimulant, terbutaline sulfate (TRB) was investigated in fourteen patients with chronic renal failure (CRF) receiving maintenance hemodialysis. Fourteen CRF patients with chronic glomerulonephritis (CGN) (5 male, 2 female) and diabetes mellitus (DM) (3 male, 4 female) were infused with 0.4 mg TRB dissolved in 100 ml of 10% maltose solution. Serum potassium level in the CGN group significantly (p less than 0.01) decreased after 20 minutes infusion and maximum lowering effect (1.1 mEq/l) was obtained 40 minutes after the start. On the other hand, the maximum lowering effect of serum potassium level in the DM group (0.77 mEq/l) was obtained 60 minutes after the start. No serious metabolic and hemodynamic side effect was observed except only slight transient tachycardia in 2 CGN patients and 3 DM patients. Thus, a beta-2 selective adrenergic stimulant, terbutaline sulfate may be useful for acute treatment of hyperkalemia in CRF patients by way of the stimulation of potassium uptake in the cells.
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PMID:[A new treatment of hyperkalemia in renal failure with selective beta 2-adrenergic stimulant, terbutaline sulfate]. 274 8

With isoelectric focusing, we examined heterogeneity of autoantibodies to insulin receptors in serums of two patients with insulin-resistant diabetes and one patient with hypoglycemia. Immunoglobulins were prepared by ammonium sulfate precipitation and ion-exchange chromatography with DEAE-Sepharose and subjected to isoelectric focusing for separation into 30 fractions. The fractions were tested for their ability to inhibit 125I-labeled insulin binding to human placental membranes, immunoprecipitate solubilized insulin receptor cross-linked with 125I-insulin, and mimic or inhibit the action of insulin in rat adipocytes. The results varied among the three patients. In the first patient, inhibition of 125I-insulin-binding activity (IBA) and insulin-receptor-precipitating activity (IPA) were distributed almost identically, but the distribution of insulinlike bioactivity (ILBA) was somewhat different. In the second patient, some fractions exhibited potent IBA without IPA, and these fractions inhibited the action of insulin in rat adipocytes. In the third patient, all of the isoelectric fractions showed IBA without IPA and were insulin antagonists. These observations indicate that some patients have antibodies with pure insulin-antagonist properties and provide further evidence that autoantibodies to insulin receptors are polyclonal and recognize different antigenic sites on insulin-receptor molecules. The findings also suggest that the ability of antibodies to elicit ILBA is linked to the ability to immunoprecipitate 125I-insulin-cross-linked and solubilized receptors, whereas antibodies that only inhibit insulin binding behave as insulin antagonists.
Diabetes 1989 Sep
PMID:Demonstration of heterogeneity of autoantibodies to insulin receptors in type B insulin resistance by isoelectric focusing. 276 37

Administration of protamine sulfate into circulation was shown to increase the diabetogenic effect of alloxan. Protamine sulfate bound endogenous heparin, as a result of which the diabetogenic factor caused more severe forms of experimental diabetes. At the same time, the diabetogenic factor exhibited distinctly higher activity during the heparin deficiency developed.
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PMID:[Intensification of the diabetogenic effect of alloxan by protamine sulfate]. 281 70

To study the effects of chronic diabetes on heart rate and adrenergic responsiveness we compared unanesthetized diabetic rabbits, 10-13 mo after alloxan monohydrate injection, to age-matched controls. There were no significant differences found between groups for body or heart weight. Both resting and intrinsic heart rate (the latter obtained after atropine sulfate and propranolol HCl) were similar. In addition, serum and left ventricular epinephrine and norepinephrine concentrations as well as left ventricular beta-receptor density and affinity were unchanged in diabetic animals. Heart rate responses to isoproterenol were blunted in diabetics at the three highest doses. Base-line mean blood pressure was modestly lower in diabetic rabbits, and parallel declines in pressure for both groups were observed in response to isoproterenol. The diminished heart rate response to isoproterenol in diabetic rabbits may be due to diminished myocardial sensitivity to catecholamines, possibly combined with altered baroreceptor reflexes. These experiments may provide an explanation for the blunted heart rate response to exercise described in human diabetics.
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PMID:Heart rate control in diabetic rabbits: blunted response to isoproterenol. 284 38

The effect of moderate insulin deficiency of 2 weeks in duration on hypothalamic catecholamine metabolism in food-deprived and meal-fed rats was evaluated. Hypothalamic tyrosine content in food-deprived (from 0700 to 1600 h), diabetic rats was normal. Also normal were the rates of 3,4-dihydroxyphenylalanine accumulation following aromatic amino acid decarboxylase inhibition, norepinephrine and 3,4-dihydroxyphenylethylamine (dopamine) clearance after tyrosine hydroxylase inhibition, and intraneuronal amine accumulation following monoamine oxidase inhibition. Differences in hypothalamic amine metabolism were apparent, however, when diabetic and normal rats were fed 2-g meals. The 3-methoxy-4-hydroxyphenylethyleneglycol sulfate accumulation rate was depressed in diabetic rats by the carbohydrate meal but was stimulated by the tyrosine-supplemented protein meal. In contrast, the tyrosine-supplemented diet had no effect on 3,4-dihydroxyphenylacetic acid accumulation in diabetic animals, whereas the production rate in normal rats was increased. We conclude that normal responses occurring in hypothalamic catecholamine metabolism after the consumption of a meal are modified by the presence of diabetes.
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PMID:Hypothalamic catecholamine metabolism in diabetic rats: the effect of insulin deficiency and meal ingestion. 286 2

The metabolism of glomerular proteoglycans was studied in an effort to understand the mechanisms leading to reduction of glomerular basement membrane (GBM) heparan sulfate (heparan-SO4) proteoglycan in diabetes. Glomeruli were isolated from control and streptozocin-induced diabetic rats after exposure to [35S]sulfate. A pool of rapidly metabolized 35S-glycosaminoglycans (GAG), predominantly heparan-35SO4, was present in GBMs from controls but not diabetics, whereas intact isolated glomeruli from the two groups contained similar quantities of 35S-macromolecules after 4 and 16 h in vitro. Glomeruli from diabetics contained less 35S-proteoglycan than controls after 16 h in vivo. A more rapid disappearance of [35S]sulfate from serum and an increased inorganic sulfate concentration in diabetes may account for this difference. Glomeruli from diabetics contained more heparan-35SO4 and less dermatan-35SO4 proteoglycan than control glomeruli in vitro. Diabetic glomerular heparan-35SO4 proteoglycan and its GAG chains had hydrodynamic sizes similar to controls (Mr, 13 and 1.25 X 10(4), respectively). A heparin-releasable heparan-35SO4 proteoglycan detected in isolated control glomeruli by gel electrophoresis was present in chase medium of glomeruli from diabetics in the absence of heparin. Two dermatan-35SO4 proteoglycans were synthesized in vitro. One had size and charge properties similar to glomerular heparan-35SO4 proteoglycan. A second, larger dermatan-35SO4 proteoglycan accumulated in tissue over 16 h. It was partially excluded from Sepharose CL-6B columns and eluted from Sepharose CL-4B columns at Kav = 0.32. The hydrodynamic sizes of both tissue forms of dermatan-35SO4 proteoglycans were similar in diabetics and controls. Differences in the biochemical characteristics of the major de novo synthesized glomerular proteoglycan pools could not be invoked to explain altered metabolism of GBM heparan sulfate in diabetic animals. These changes may result from diminished affinity of heparan sulfate proteoglycan for extracellular matrix or cell surfaces and may account for altered glomerular ultrafiltration properties in diabetes mellitus.
Diabetes 1986 Oct
PMID:Glomerular proteoglycans in diabetes. Partial structural characterization and metabolism of de novo synthesized heparan-35SO4 and dermatan-35SO4 proteoglycans in streptozocin-induced diabetic rats. 294 82

Treatment of human glomerular basement membrane (GBM) with 4 M guanidine HCl resulted in a preferential extraction of noncollagenous components including laminin, fibronectin, entactin, and heparan sulfate proteoglycan, whereas effective solubilization of type IV collagen required exposure to denaturing solvents in the presence of reducing agents. The guanidine HCl-solubilized constituents were identified by immunochemical procedures after resolution by polyacrylamide gel electrophoresis, CL-6B filtration, and DEAE-cellulose chromatography. Two immunologically related heparan sulfate proteoglycans (Mr approximately 350,000 and 210,000) were observed by electrophoresis, with the higher-molecular-weight form being predominant. An examination of the two proteoglycans after heparitinase digestion or chemical deglycosylation indicated that heparan sulfate chains and other carbohydrate units are attached to core proteins with Mr approximately 140,000 and 110,000, respectively. Radioimmunoassays indicated that human diabetic GBM contained significantly lower (P less than .005) amounts of heparan sulfate proteoglycan and laminin with average values that were 30 and 60%, respectively, of nondiabetic controls; the fibronectin content of the diabetic GBM, however, was not significantly different from the normal. These findings, together with previous studies showing increases in GBM collagen, indicate that an alteration in the macromolecular architecture of this basement membrane occurs in diabetes that may be responsible for the filtration defect and the ultimate glomerular occlusion.
Diabetes 1987 Mar
PMID:Studies on macromolecular components of human glomerular basement membrane and alterations in diabetes. Decreased levels of heparan sulfate proteoglycan and laminin. 294 55

A heat- and acid-stable protein fraction that inhibited peptide chain initiation in rabbit reticulocyte lysates was extracted from frozen, powdered rat skeletal muscles by stepwise trichloroacetic acid precipitation. Streptozotocin-induced diabetes increased the inhibitory activity; this was prevented by insulin therapy. Size-exclusion high-performance liquid chromatography resolved four inhibitory fractions; only one was consistently increased (approximately 2-fold) in muscle extracts from diabetic rats. Polysome profiles of lysates incubated with this fraction indicated peptide chain initiation inhibition. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis the purified inhibitory fraction migrated with apparent Mr 30 and 32 kDa, which on Western blot immunostained with antisera against histone H1/H1(0). Perchloric acid extraction of muscle homogenates yielded approximately twofold more H1 from diabetic than from control rats; yield from diabetics decreased to control values 5 h after subcutaneous insulin injection. Inclusion of detergent during homogenization increased H1 yield more from muscles of control than from diabetic rats and abolished the difference between them. Because H1 affects several biochemical reactions, its facilitated extraction from insulin-deprived tissues can bias interpretation of studies of insulin action.
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PMID:A translational inhibitor from muscles of diabetic rats: identification as histone H1. 295 2

Adrenalectomy in young obese (ob/ob) and the diabetic (db/db) mouse slowed body weight gain. Treatment of adrenalectomized ob/ob mice with cortisone or deoxycorticosterone acetate (DOCA) significantly increased weight gain in a dose-related manner. Cortisone had no effect on weight gain on lean mice and treatment with dehydroepiandrosterone sulfate was without effect on either ob/ob or lean mice. The increment in body weight of adrenalectomized ob/ob mice treated with corticosterone and DOCA was associated with an increase in body weight and an increase in food intake. When adrenalectomy was performed at twenty-three days of age (five days before weaning), animals carrying the (db/db) genotype remained lighter than their normal littermates. These data document the importance of the adrenal gland and its steroids for the development and maintenance of many features of the obese or diabetes mouse.
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PMID:Adrenalectomy and steroid treatment in obese (ob/ob) and diabetic (db/db) mice. 295 97

The ATPase activity of myofibrils and myosin from hindlimb muscle was investigated in animals 4 wk after the induction of diabetes by an intravenous injection of streptozotocin (65 mg/kg). Ca2+-stimulated ATPase in myofibrils was increased in diabetic muscle at various times of incubation (1-7 min) as well as at different concentrations of free Ca2+ (10(-7)-10(-5) M Ca2+). Such an increase in Ca2+-stimulated ATPase was evident as early as 1 wk after streptozotocin injection, but Mg2+-ATPase activity remained unaltered. Treatment of diabetic animals with insulin Ca2+-ATPase and actin-activated ATPase activities of pure myosin were similarly increased in diabetic muscle. Myosin ATPase was also activated by K+- or NH4+-EDTA; these responses were more in diabetic muscle. However, sodium dodecyl sulfate gel electrophoresis failed to reveal differences in the patterns of contractile proteins, and pyrophosphate gels did not show significant changes in myosin isozyme patterns between diabetics and controls. The results of this study demonstrate an activation of contractile protein ATPase of skeletal muscle in diabetes and seem to indicate that such an alteration may be responsible for enhanced contractile function of skeletal muscle in this disease.
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PMID:Altered contractile proteins in skeletal muscle of diabetic rats. 295 57


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