HYPOGLYCEMIC DRUGS AND THE DEXTRAN 'ANAPHYLACTOID' INFLAMMATION

1960 ◽  
Vol 38 (8) ◽  
pp. 823-827 ◽  
Author(s):  
V. W. Adamkiewicz ◽  
R. J. Fitko ◽  
A. A. Fortier
Keyword(s):  
Alloxan Diabetes ◽  
Diabetic Rat ◽  
Normal Rat ◽  
Hypoglycemic Drug

Tolbutamide (Orinase) (260 mg/kg s.c), a hypoglycemic drug of the sulphonylurea class, sensitizes the normal rat (135–185 g) towards the 'anaphylactoid' inflammation induced by the administration of dextran (1 ml 6% w/v solution in saline s.c. per rat). However, the drug does not sensitize the alloxan diabetic rat towards this inflammation, nor does it alleviate the classical signs of alloxan diabetes. It is suggested that the sensitization of normal rats towards dextran by tolbutamide is mediated through insulin.

HYPOGLYCEMIC DRUGS AND THE DEXTRAN 'ANAPHYLACTOID' INFLAMMATION

1960 ◽  
Vol 38 (1) ◽  
pp. 823-827 ◽  
Author(s):  
V. W. Adamkiewicz ◽  
R. J. Fitko ◽  
A. A. Fortier
Keyword(s):  
Alloxan Diabetes ◽  
Diabetic Rat ◽  
Normal Rat ◽  
Hypoglycemic Drug

Tolbutamide (Orinase) (260 mg/kg s.c), a hypoglycemic drug of the sulphonylurea class, sensitizes the normal rat (135–185 g) towards the 'anaphylactoid' inflammation induced by the administration of dextran (1 ml 6% w/v solution in saline s.c. per rat). However, the drug does not sensitize the alloxan diabetic rat towards this inflammation, nor does it alleviate the classical signs of alloxan diabetes. It is suggested that the sensitization of normal rats towards dextran by tolbutamide is mediated through insulin.

scholarly journals 3-oxo acid coenzyme A-transferase in normal and diabetic rat muscle

1976 ◽  
Vol 158 (2) ◽  
pp. 509-512 ◽  
Author(s):  
A Fenselau ◽  
K Wallis
Keyword(s):  
Skeletal Muscle ◽  
Coenzyme A ◽  
Substrate Inhibition ◽  
Diabetic Rats ◽  
Diabetic Rat ◽  
Functional Parameters ◽  
Rat Muscle ◽  
Coa Transferase ◽  
Normal Rat ◽  
Streptozotocin Diabetic Rats

The amounts of succinyl-CoA--3-oxo acid CoA-transferase (EC 2.8.3.5) decrease progressively in skeletal muscle in streptozotocin-diabetic rats, reaching after 10 days about 50% of the value in normal rat muscle. Electrofocusing studies indicate the occurrence of partial proteolysis of the enzyme in diabetic muscle. However, several functional parameters relating to acetoacetate utilization, including substrate inhibition, are quite similar for muscle transferase preparations from normal and diseased rats. The development of pathological ketoacidosis is discussed in the light of these observations.

Bioassay of endothelium-derived relaxing factor in diabetic rat aorta

1992 ◽  
Vol 263 (3) ◽  
pp. H676-H680 ◽  
Author(s):  
G. M. Pieper ◽  
D. A. Mei ◽  
P. Langenstroer ◽  
S. T. O'Rourke
Keyword(s):  
Rat Aorta ◽  
Diabetic Rat ◽  
Arginine Infusion ◽  
Relaxing Factor ◽  
Oxygen Derived Free Radicals ◽  
Donor Segment ◽  
Normal Rat ◽  
Bioassay Technique ◽  
Endothelium Derived Relaxing Factor ◽  
A Site

The bioassay technique was utilized to quantitate endothelium-derived relaxing factor (EDRF) released from perfused donor segments of control and diabetic rat aorta. In the presence of indomethacin, perfusates of donor segments with endothelium were allowed to superfuse recipient detector rings of normal rat aorta without endothelium. Under basal conditions, relaxations of the bioassay rings to perfusates of control and diabetic donor segments were similar. Perfusion of donor segments with acetylcholine produced relaxation of bioassay rings, which was decreased from endothelial perfusion of diabetic donor segments. These relaxations were inhibited by addition of methylene blue to the detector ring or by perfusion of donor segments with nitro-L-arginine. Infusion of superoxide dismutase (SOD) at a site proximal to the donor segment normalized relaxations induced by acetylcholine addition to diabetic donors. In contrast, infusion of SOD distal to the donor had no effect on acetylcholine-stimulated relaxations of detector rings from control donors while attenuating, paradoxically, the relaxations of detector rings from diabetic donors. These results suggest that diabetic rat aortas release similar levels of EDRF in response to acetylcholine, but the action of EDRF arising from diabetic donors is attenuated by enhanced release of oxygen-derived free radicals, which limits EDRF-mediated relaxation of vascular smooth muscle.

Insulin, glucagon, and somatostatin secretion from isolated perfused rat and chicken pancreas-duodenum

1980 ◽  
Vol 238 (2) ◽  
pp. E150-E156 ◽  
Author(s):  
R. N. Honey ◽  
J. A. Schwarz ◽  
C. J. Mathe ◽  
G. C. Weir
Keyword(s):  
Insulin Secretion ◽  
Diabetic Rats ◽  
Diabetic Rat ◽  
Glucagon Release ◽  
Cell Regulation ◽  
Rat Pancreas ◽  
Somatostatin Secretion ◽  
Normal Rat ◽  
D Cell ◽  
Chicken Pancreas

Insulin, glucagon, and somatostatin secretion were evaluated in the following isolated perfused models: rat pancreas-duodenum (both normal and streptozotocin-diabetic animals) and the chicken pancreas with and without duodenum. Insulin secretion in response to glucose or arginine was greater from the normal rat than either the diabetic rat or the chicken. Glucagon release from both species was suppressed by glucose and stimulated by arginine except that poor inhibition by glucose was found in the diabetic rat. Somatostatin could be measured in the effluent from both normal and diabetic rats, but the responses to glucose and arginine were variable and modest. Clear increases of secretion in the rat were only observed in response to a combination of glucose, arginine, theophylline, and isoproterenol. In contrast, the chicken somatostatin secretion was markedly stimulated by glucose and by arginine. In conclusion, the perfused chicken pancreas-duodenum has been shown to secrete large amounts of somatostatin in comparison to the rat and should prove to be a useful system for the study of D-cell regulation.

Manganese action on pancreatic protein synthesis in normal and diabetic rats

1983 ◽  
Vol 245 (5) ◽  
pp. G628-G634 ◽  
Author(s):  
M. Korc
Keyword(s):  
Acinar Cells ◽  
Diabetic Rats ◽  
Pancreatic Acinar Cells ◽  
Diabetic Rat ◽  
Pancreatic Acini ◽  
Significant Stimulation ◽  
Biphasic Effect ◽  
Normal Rat ◽  
Streptozotocin Induced Diabetes

The effects of manganese on [3H]phenylalanine incorporation into protein were studied in pancreatic acini prepared from normal and streptozotocin-induced diabetic rats. In the absence of added Ca2+ manganese exerted a biphasic effect on [3H]phenylalanine incorporation in both groups of acini. Significant stimulation occurred at 3 X 10(-5) M manganese. At higher concentrations manganese inhibited incorporation. The magnitude of stimulation was similar in all acini, whereas the magnitude of inhibition was greater in acini from normal rats. Addition of Ca2+ to incubation media abolished the stimulatory effect of manganese in normal rat acini and greatly enhanced it in diabetic rat acini, significant stimulation now occurring at 10(-5) M manganese. The magnitude of inhibition was again greater in acini from normal rats. Insulin in vivo partially reversed the diabetes-induced alterations in acinar cell responsiveness to manganese. The present findings suggest that streptozotocin-induced diabetes is associated with postreceptor alterations in the pancreatic acinar cells.

Proteome map of normal rat retina and comparison with the proteome of diabetic rat retina: New insight in the pathogenesis of diabetic retinopathy

PROTEOMICS ◽  
2007 ◽  
Vol 7 (15) ◽  
pp. 2636-2650 ◽  
Author(s):  
Godfrey (Goff) J. Quin ◽  
Alice C. L. Len ◽  
Frank A. Billson ◽  
Mark C. Gillies
Keyword(s):  
Diabetic Retinopathy ◽  
Diabetic Rat ◽  
Rat Retina ◽  
Normal Rat

Glucose inhibits phenobarbital-induced δ-aminolevulinate synthase expression in normal but not in diabetic rat hepatocytes

1996 ◽  
Vol 74 (2) ◽  
pp. 271-281 ◽  
Author(s):  
Cecilia L. Varone ◽  
Eduardo T. Cánepa ◽  
Elena B. C. Llambías ◽  
Moisés Grinstein
Keyword(s):  
Phosphodiesterase Inhibitor ◽  
Rat Hepatocytes ◽  
Inhibitory Effect ◽  
Diabetic Rat ◽  
Glucose Effect ◽  
Camp Content ◽  
Aminolevulinate Synthase ◽  
Abnormal Metabolism ◽  
Normal Rat ◽  
Mrna Half Life

In the present work, we demonstrate the presence of a glucose inhibitory effect on the phenobarbital-mediated induction of the δ-aminolevulinate synthase mRNA in normal rat hepatocytes, consistent with the results obtained with the δ-aminolevulinate synthase activity previously reported. This "glucose effect" can be prevented by adding cAMP, adenylate cyclase activators, or a phosphodiesterase inhibitor. δ-Aminolevulinate synthase mRNA half-life is not modified in the presence of phenobarbital or glucose. When the same experiments are performed using diabetic cells, no glucose effect is observed, even when the endogenous cAMP content is lowered to normal levels. The results obtained in this study suggest that glucose decreases δ-aminolevulinate synthase biosynthesis by acting at a pretranslational step. Assuming that the glucose effect operates by a repression mechanism exerted by metabolites derived from or related to glucose, the present results may reflect a derangement in the formation of these metabolites as a result of the abnormal metabolism operating in the diabetic state.Key words: glucose, δ-aminolevulinate synthase expression, diabetic rat hepatocytes, phenobarbital, cAMP.

Regulation of phenobarbital-induced ferrochelatase mRNA activity by dibutyryl cAMP and glucose in normal and diabetic rat hepatocytes

1992 ◽  
Vol 70 (1) ◽  
pp. 26-33 ◽  
Author(s):  
Eduardo T. Cánepa ◽  
Marcelo Páez Pereda ◽  
Elena B. C. Llambías ◽  
Moïses Grinstein
Keyword(s):  
Experimental Evidence ◽  
Rat Hepatocytes ◽  
Diabetic Rat ◽  
Dibutyryl Camp ◽  
Glucose Effect ◽  
Normal Cells ◽  
Camp Content ◽  
Normal Rat ◽  
Increased Activity

The induction of ferrochelatase activity by phenobarbital and its potentiation by dibutyryl cAMP assayed in normal rat hepatocytes are associated with increased activity of ferrochelatase mRNA. Glucose inhibits this stimulatory effect. This inhibition can be reversed with increasing concentrations of dibutyryl cAMP. The inducing effect exerted by phenobarbital on the activity of ferrochelatase mRNA in diabetic hepatocytes is greater than that observed in normal cells. This enhanced response in diabetic rat hepatocytes is neither potentiated by adding dibutyryl cAMP nor repressed by glucose. The absence of a glucose effect persists even when the endogenous cAMP content is lowered to normal levels. The results obtained in this study are consistent with those reported in other published studies of ferrochelatase activity. This adds more experimental evidence to support the concept that ferrochelatase is inducible. The results obtained suggest that ferrochelatase is more susceptible to induction with phenobarbital in diabetic rat hepatocytes than in normal rat hepatocytes.Key words: ferrochelatase mRNA activity, phenobarbital, cAMP, glucose, diabetic rat hepatocytes.

Cellular mechanisms of glucose-induced myo-inositol transport upregulation in rat mesangial cells

1994 ◽  
Vol 267 (3) ◽  
pp. F459-F466 ◽  
Author(s):  
A. A. Chatzilias ◽  
C. I. Whiteside
Keyword(s):  
High Glucose ◽  
Mesangial Cells ◽  
Maximum Velocity ◽  
Diabetic Rat ◽  
Protein Synthesis Inhibitors ◽  
Cellular Mechanisms ◽  
Phosphoinositide Signaling ◽  
Normal Glucose ◽  
Normal Rat ◽  
And Function

Uptake of myo-inositol (MI) is necessary to maintain normal cellular phosphoinositide signaling and function. MI transport is up-regulated in the cells of diabetic rat glomeruli compared with normal rat glomeruli [C. I. Whiteside, J. C. Thompson, and J. Ohayon. Am. J. Physiol. 260 (Renal Fluid Electrolyte Physiol. 29): F138-F144, 1991]. To identify mechanisms associated with upregulation of MI transport, rat mesangial cells were cultured in high (25.6 mM) vs. normal (5.6 mM) glucose. Specific Na(+)-dependent [3H]MI uptake (> 97%), using L-[14C]glucose as the nonspecific marker, was linear for 120 min in high and normal glucose. In high glucose, compared with normal glucose, there was no change in Michaelis-Menten constant values [29.1 +/- 0.6 vs. 30.3 +/- 0.7 microM (SE)], whereas maximum velocity (Vmax) was increased (2.024 +/- 52 vs. 1.132 +/- 115 fmol.mg protein-1.min-1, P < 0.001). Mannitol (20.0 mM), used as an osmotic control, had no effect on the upregulation of MI transport. Maximum upregulation of MI transport measured by Vmax (control taken as 100%) was observed after 8 h of exposure to high glucose (222 +/- 6% above control, P < 0.0001) or galactose (20.0 mM) (194 +/- 6%, P < 0.0001) and was sustained for up to 48 h. The protein synthesis inhibitors cycloheximide (20 micrograms/ml) or actinomycin D (5 micrograms/ml), the F-actin depolymerizing agent cytochalasin D (2 micrograms/ml), and the aldose reductase inhibitor Tolrestat (0.3 mM) independently prevented glucose- or galactose-induced upregulation of MI transport.(ABSTRACT TRUNCATED AT 250 WORDS)

Troglitazone prevents falty changes of the liver in obese diabetic rat

2001 ◽  
Vol 120 (5) ◽  
pp. A207-A208
Author(s):  
D JIA ◽  
T AKIYAMA ◽  
K FUKUMITSU ◽  
M YAMAMOTO ◽  
S ABE ◽  
...  
Keyword(s):  
Diabetic Rat
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