Increase in Long Fatty Acyl-CoA Hydrolase Activity in the Liver and Kidney of Alloxan Diabetic Rat

1971 ◽  
Vol 69 (1) ◽  
pp. 247-249 ◽  
Author(s):  
Shigeru KUROOKA ◽  
Kanoo HOSOKI ◽  
Yoshio YOSHIMURA
Keyword(s):  
Fatty Acyl ◽  
Hydrolase Activity ◽  
Diabetic Rat ◽  
Liver And Kidney ◽  
Coa Hydrolase

Influence of dietary status and diabetes on aortic acyl-CoA hydrolase activity

1977 ◽  
Vol 26 (3) ◽  
pp. 289-296 ◽  
Author(s):  
Sam Hashimoto ◽  
Seymour Dayton
Keyword(s):  
Hydrolase Activity ◽  
Coa Hydrolase

Distribution of 125I-labelled insulin-binding sites in peripheral tissues of the normal and diabetic rat: an autoradiographic study

1991 ◽  
Vol 128 (1) ◽  
pp. 85-NP ◽  
Author(s):  
C. S. Thompson ◽  
R. M. Sykes ◽  
J. Muddle ◽  
M. R. Dashwood
Keyword(s):  
Binding Sites ◽  
Regional Distribution ◽  
Insulin Receptors ◽  
Insulin Binding ◽  
Autoradiographic Study ◽  
Diabetic Rat ◽  
Peripheral Tissues ◽  
Liver And Kidney ◽  
Impaired Insulin Action

ABSTRACT In-vitro autoradiography was used to demonstrate the regional distribution of 125I-labelled insulin-binding sites in the liver, kidney and heart of normal rats and rats made diabetic with streptozotocin. The distribution of insulin-binding sites in the liver of control rats was uniformly high, while in the kidney of control rats there was weak 125I-labelled insulin binding in the medulla and dense binding in the cortex. In the hearts of control rats a high density of 125I-labelled insulin-binding sites was evident both in the atrial and ventricular muscle. Non-ketotic diabetes mellitus caused a marked increase in 125I-labelled insulin-binding sites in both the liver and kidney with the former tissue exhibiting a time-dependent (7 to 62 days) increase. There was no apparent effect of diabetes on insulin-binding sites in the heart. Since experimental diabetes causes (1) a decrease in circulating insulin concentration and (2) impaired insulin action at many target tissues, the increase in 125I-labelled insulin-binding sites observed in the present study may represent a compensatory 'up regulation' of insulin receptors. Journal of Endocrinology (1991) 128, 85–89

scholarly journals Effects of ethanol and protein dilution on microsomal palmitoyl-CoA hydrolase activity assayed by different methods

FEBS Letters ◽  
1980 ◽  
Vol 110 (2) ◽  
pp. 205-208 ◽  
Author(s):  
Leif E. Hagen ◽  
Rolf R. Berge ◽  
Anne Bakken ◽  
Mikael Farstad
Keyword(s):  
Hydrolase Activity ◽  
Coa Hydrolase

Induction of cytosolic clofibroyl-CoA hydrolase activity in liver of rats treated with clofibrate

1987 ◽  
Vol 918 (1) ◽  
pp. 60-66 ◽  
Author(s):  
Rolf K. Berge ◽  
Erik Stensland ◽  
Asle Aarsland ◽  
Ghezai Tsegai ◽  
Harald Osmundsen ◽  
...  
Keyword(s):  
Hydrolase Activity ◽  
Coa Hydrolase

scholarly journals The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat

1976 ◽  
Vol 160 (2) ◽  
pp. 247-251 ◽  
Author(s):  
P J Brophy ◽  
D E Vance
Keyword(s):  
Fatty Acid ◽  
Microsomal Fraction ◽  
Specific Activity ◽  
Arachidic Acid ◽  
Fatty Acyl ◽  
Chain Elongation ◽  
Fatty Acid Chain ◽  
Specific Activities ◽  
Coa Hydrolase ◽  
Long Chain

1. The specific activities of long-chain fatty acid-CoA ligase (EC6.2.1.3) and of long-chain fatty acyl-CoA hydrolase (EC3.1.2.2) were measured in soluble and microsomal fractions from rat brain. 2. In the presence of either palmitic acid or stearic acid, the specific activity of the ligase increased during development; the specific activity of this enzyme with arachidic acid or behenic acid was considerably lower. 3. The specific activities of palmitoyl-CoA hydrolase and of stearoyl-CoA hydrolase in the microsomal fraction decreased markedly (75%) between 6 and 20 days after birth; by contrast, the corresponding specific activities in the soluble fraction showed no decline. 4. Stearoyl-CoA hydrolase in the microsomal fraction is inhibited (99%) by bovine serum albumin; this is in contrast with the microsomal fatty acid-chain-elongation system, which is stimulated 3.9-fold by albumin. Inhibition of stearoyl-CoA hydrolase does not stimulate stearoyl-CoA chain elongation. Therefore it does not appear likely that the decline in the specific activity of hydrolase during myelogenesis is responsible for the increased rate of fatty acid chain elongation. 5. It is suggested that the decline in specific activity of the microsomal hydrolase and to a lesser extent the increase in the specific activity of the ligase is directly related to the increased demand for long-chain acyl-CoA esters during myelogenesis as substrates in the biosynthesis of myelin lipids.

scholarly journals The presence of acyl-CoA hydrolase in rat brown-adipose-tissue peroxisomes

1989 ◽  
Vol 262 (1) ◽  
pp. 41-46 ◽  
Author(s):  
S E Alexson ◽  
H Osmundsen ◽  
R K Berge
Keyword(s):  
Adipose Tissue ◽  
Substrate Specificity ◽  
Brown Adipose Tissue ◽  
Cytochrome Oxidase ◽  
Gradient Centrifugation ◽  
Hydrolase Activity ◽  
Short Chain ◽  
Marker Enzyme ◽  
Brown Adipose ◽  
Coa Hydrolase

The subcellular distribution of acyl-CoA hydrolase was studied in rat brown adipose tissue, with special emphasis on possible peroxisomal localization. Subcellular fractionation by sucrose-density-gradient centrifugation, followed by measurement of short-chain (propionyl-CoA) acyl-CoA hydrolase in the presence of NADH, resulted in two peaks of activity in the gradient: one peak corresponded to the distribution of cytochrome oxidase (mitochondrial marker enzyme), and another peak of activity coincided with the peroxisomal marker enzyme catalase. The distribution of the NADH-inhibited short-chain hydrolase activity fully resembled that of cytochrome oxidase. The substrate-specificity curve of the peroxisomal acyl-CoA hydrolase activity indicated the presence of a single enzyme exhibiting a broad substrate specificity, with maximal activity towards fatty acids with chain lengths of 3-12 carbon atoms. The mitochondrial acyl-CoA hydrolase substrate specificity, in contrast, indicated the presence of at least two acyl-CoA hydrolases (of short- and medium-chain-length specificity). The peroxisomal acyl-CoA hydrolase activity was inhibited by CoA at low (microM) concentrations and by ATP at high concentrations (greater than 0.8 mM). In contrast with the mitochondrial short-chain hydrolase, the peroxisomal acyl-CoA hydrolase activity was not inhibited by NADH.

scholarly journals Mechanism of the beneficial and protective effects of exenatide in diabetic rats

2013 ◽  
Vol 220 (3) ◽  
pp. 291-304 ◽  
Author(s):  
Mohamed Lotfy ◽  
Jaipaul Singh ◽  
Hameed Rashed ◽  
Saeed Tariq ◽  
Erika Zilahi ◽  
...  
Keyword(s):  
Serum Insulin ◽  
Insulin Level ◽  
Pancreatic Tissue ◽  
Diabetic Rats ◽  
Diabetic Rat ◽  
Protective Effects ◽  
Expression Of Genes ◽  
Liver And Kidney ◽  
Glucagon Like Peptide 1 ◽  
Biochemical Analyses

Glucagon-like peptide 1 (GLP1) agonists are promising therapeutic agents in the treatment of diabetes mellitus. This study examines the mechanism of the protective effects of exenatide in experimental diabetes, employing four groups of ten rats each, in which two groups were streptozotocin-induced diabetic and two were control groups. One control and one diabetic group were treated with exenatide (1 μg/kg body weight (BW)) for 10 weeks. Blood plasma was taken for biochemical analyses while pancreatic tissue was taken for immunofluorescence and immunoelectron microscopy studies and real-time PCR to examine the expression of genes. The results show that exenatide improved BW gain and reduced blood glucose in diabetic rats compared with controls. Similarly, exenatide enhanced insulin release from the pancreatic fragments and improved liver and kidney functions and lipid profile in diabetic rats compared with controls. Exenatide not only induced significant increases in serum insulin level but also elevated the number of insulin-, GLP1- and exenatide-positive cells compared with untreated controls. Exenatide also elevated the number of catalase- and glutathione reductase-positive cells in diabetic rat pancreas compared with controls. Exenatide caused significant elevation in the expressions of pancreatic duodenal homeobox-1, heat shock protein-70, glutathione peroxidase, insulin receptor and GLP1 receptor genes in the pancreas of both control and diabetic rats compared with untreated animals. The results have demonstrated that exenatide can exert its beneficial and protective effects by elevating the levels of endogenous antioxidants and genes responsible for the survival, regeneration and proliferation of pancreatic β-cell.

scholarly journals Anti-diabetic, Antioxidants, Anti-hepatorenaltoxicity Activities of Cyperus rotundus Rhizome Extract in Alloxan-induced Diabetic Rats

2021 ◽  
Author(s):  
Mohammed Al-Awar ◽  
Turki Alqabbani
Keyword(s):  
Elevated Serum ◽  
Density Lipoprotein ◽  
Diabetic Rats ◽  
Cyperus Rotundus ◽  
Lipoprotein Cholesterol ◽  
Male Rats ◽  
Diabetic Rat ◽  
Histological Structure ◽  
Amylase Level ◽  
Liver And Kidney

Objective: The hypoglycemic, hepatorenalprotective, and antioxidant Activities of Cyperus rotundus rhizomes extract in an alloxan-induced diabetic rat model were investigated in this work.Methods: 25 Male rats were divided into 5 groups: normal control, diabetic control, diabetic of C. rotundus (200 mg/kg b.w), diabetic of C. rotundus (400 mg/kg b.w), diabetic of glibenclamide (0.6mg/kg).Treatments were administered orally for 6 weeks.Results: A single injection of alloxan to rats (150mg/kg b.w) caused pathological alterations in all studied parameters and histological structure of the pancreas. On the other hand, results showed that oral administration of C. rotundus rhizomes extract in dose of 200 and 400 mg/kg caused significant reduction in glucose, HbA1C%, α-amylase level and plasma lactate together with significant elevation in serum insulin, serum pyruvate with an improvement in insulin resistance. In line with amelioration of the diabetic state, C. rotundus rhizomes extract improved of the liver and kidney functions, and oxidative marker levels. Moreover, the extract succeeded to reduce the elevated serum total cholesterol, triglyceride (TG) and low-density lipoprotein- cholesterol (LDL-C) levels and to elevate the reduced high-density lipoprotein- cholesterol (HDL-C) level of diabetic rats.Conclusion: The investigation data concluded that C. rotundus rhizomes extract could be used as alternative treatments as antidiabetic, antioxidant and antihyperlipidemic, and agent as well as in liver and kidney protective in alloxan induced-diabetic rats. This may be related to the presence of saponin glycosides, polyphenols, flavonoids, and terpenoids in the ethanolic extract of C. rotundus rhizomes, which was discovered by phytochemical screening in this study to be present in the plant.

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