Rutin potentiates insulin receptor kinase to enhance insulin-dependent glucose transporter 4 translocation

2014 ◽  
Vol 58 (6) ◽  
pp. 1168-1176 ◽  
Author(s):  
Chia-Yu Hsu ◽  
Hung-Yuan Shih ◽  
Yi-Chen Chia ◽  
Chia-Hung Lee ◽  
Hitoshi Ashida ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Glucose Transporter ◽  
Receptor Kinase ◽  
Glucose Transporter 4 ◽  
Insulin Dependent ◽  
Insulin Receptor Kinase

Impaired insulin action but normal insulin receptor activity in diabetic rat liver: effect of vanadate

1990 ◽  
Vol 258 (3) ◽  
pp. E459-E467 ◽  
Author(s):  
O. Blondel ◽  
J. Simon ◽  
B. Chevalier ◽  
B. Portha
Keyword(s):  
Insulin Receptor ◽  
Insulin Action ◽  
Diabetic Rats ◽  
Receptor Kinase ◽  
Peripheral Tissues ◽  
Impaired Insulin ◽  
Insulin Dependent ◽  
Insulin Receptor Kinase ◽  
Impaired Insulin Action

In vivo insulin resistance is a characteristic of the liver and peripheral tissues in 10-wk-old female rats with non-insulin-dependent diabetes induced by streptozotocin given on day 5 after birth. Oral administration of vanadate (0.2 mg/ml) for 20 days in the diabetic rats lowered their plasma glucose levels to normal values without affecting their basal plasma insulin levels. In the basal state as well as after submaximal or maximal hyperinsulinemia (euglycemic clamp studies), peripheral glucose utilization and hepatic glucose production in vivo were normalized in the diabetic rats after the vanadate treatment. In wheat germ agglutinin purified receptors, 125I-labeled porcine insulin binding, basal and insulin-stimulated insulin receptor kinase activities for both the autophosphorylation of the beta-subunit and the phosphorylation of the artificial substrate poly (Glu-Tyr) 4:1, were found identical in diabetic and control rats, treated or not with vanadate. Liver phosphoenolpyruvate carboxykinase activity was significantly enhanced in untreated diabetic rats (P less than 0.01) as compared with control rats and returned to normal values after the 20-day vanadate treatment. Thus, in that model of non-insulin-dependent diabetes, 1) oral vanadate exerts a corrective insulin-like effect on impaired insulin action both at the level of liver and peripheral tissues, 2) impaired insulin action with no alteration of the insulin receptor tyrosine kinase is observed in the liver of untreated rats, and 3) corrective effect of vanadate on liver glucose metabolism is probably distal to the insulin receptor kinase activity.

Effects of a high-fat diet on insulin receptor kinase and the glucose transporter in rats

1992 ◽  
Vol 3 (5) ◽  
pp. 241-250 ◽  
Author(s):  
Mikiko Okamoto ◽  
Motozumi Okamoto ◽  
Shigeo Kono ◽  
Gen Inoue ◽  
Tatsuya Hayashi ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
High Fat Diet ◽  
Glucose Transporter ◽  
Receptor Kinase ◽  
High Fat ◽  
Insulin Receptor Kinase

scholarly journals Interaction between cAMP-dependent and insulin-dependent signal pathways in tyrosine phosphorylation in primary cultures of rat hepatocytes

1997 ◽  
Vol 324 (2) ◽  
pp. 379-388 ◽  
Author(s):  
Yoshiaki ITO ◽  
Yasunobu UCHIJIMA ◽  
Miyako ARIGA ◽  
Taiichiro SEKI ◽  
Asako TAKENAKA ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Insulin Receptor ◽  
Tyrosine Phosphorylation ◽  
Primary Cultures ◽  
Rat Hepatocytes ◽  
Β Subunit ◽  
Receptor Kinase ◽  
Dibutyryl Camp ◽  
Insulin Dependent ◽  
Insulin Receptor Kinase

The present studies were undertaken to determine whether the interaction between cAMP-dependent and insulin-dependent pathways in primary cultures of rat hepatocytes affects biological functions and tyrosine phosphorylation. Quiescent hepatocytes were pretreated with dibutyryl cAMP or cAMP-generating agents such as glucagon, and then treated or not with insulin. Preincubation for 6 h with dibutyryl cAMP or glucagon enhanced the effect of insulin on DNA synthesis, but not the effect of insulin on amino acid transport or glycogen and protein synthesis. Tyrosine phosphorylation of intracellular proteins was determined by immunoblot analysis using an anti-phosphotyrosine antibody. Maximum tyrosine phosphorylation of a 195 kDa protein, which may be a substrate of insulin receptor kinase, of 175–180 kDa proteins, including insulin receptor substrate (IRS)-1, and of 90–95 kDa proteins, including the insulin receptor β-subunit, was reached within 30 s of incubation with insulin. Pretreatment for about 3 h with dibutyryl cAMP or cAMP-generating agents clearly increased insulin-dependent tyrosine phosphorylation of the 195 kDa protein, but not IRS-1, IRS-2 or the insulin receptor β-subunit. Because dibutyryl cAMP and cAMP-generating agents did not increase insulin receptor number or its kinase activity, the effect of cAMP on this potentiation of tyrosine phosphorylation is assumed to be exerted at a step distal to insulin receptor kinase activation. The potentiation by cAMP pretreatment of insulin-stimulated tyrosine phosphorylation may in part be secondary to inhibition of phosphotyrosine phosphatase activity, because cAMP pretreatment blunted the effect of Na3VO4 on the net tyrosine phosphorylation of the 195 kDa protein as compared with cells pretreated with no additive. In summary, the interactions between cAMP-dependent and insulin-dependent pathways that lead to augmentation of DNA synthesis appear to parallel the changes in tyrosine phosphorylation. Further studies will be required to determine whether there is a causal relationship between these phenomena.

scholarly journals Insulin activation of insulin receptor kinase in erythrocytes is not altered in non-insulin-dependent diabetes and not influenced by hyperglycemia

2000 ◽  
Vol 166 (2) ◽  
pp. 275-281 ◽  
Author(s):  
HH Klein ◽  
R Muller ◽  
M Drenckhan ◽  
M Schutt ◽  
B Batge ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Insulin Receptors ◽  
Insulin Binding ◽  
Diabetic Control ◽  
Insulin Dependent Diabetes ◽  
Receptor Kinase ◽  
Kinase Activation ◽  
Insulin Dependent ◽  
Insulin Receptor Kinase

Recent studies suggest that high glucose concentrations impair insulin receptor phosphorylation and kinase activation in certain cell models. To examine whether such an effect of glucose can also be demonstrated in vivo, insulin receptor kinase activation was studied in erythrocytes from 11 patients with non-insulin-dependent diabetes (NIDDM), before and after reduction of hyperglycemia (from 14.6+/-1.6 to 6.6+/-0.5 mmol/l fasting plasma glucose within 8.6+/-0.6 days). For the measurement of receptor kinase activation, cells were incubated with insulin (0-400 nmol/l), solubilized and insulin receptors immobilized to microwells coated with anti-insulin receptor antibody. Kinase activity towards insulin receptor substrate-1 and insulin binding were then measured in these wells. Kinase activities (expressed as amol phosphate transferred per min and per fmol insulin binding activity) were similar before (2.4+/-0.4 and 32.2+/-2.0 amol/min per fmol with 0 and 400 nmol/l insulin, respectively) and after improvement of metabolic control (2.4+/-0.5 and 32.0+/-2.3 amol/min per fmol with 0 and 400 nmol/l insulin, respectively). Moreover, activities were also similar in 22 hyperglycemic patients with NIDDM (2.1+/-0.3 and 35.1+/-1.4 amol/min per fmol with 0 and 400 nmol/l insulin, respectively) compared with those in 21 non-diabetic control individuals (2.1+/-0.3 and 34.2+/-1.2 amol/min per fmol with 0 and 400 nmol/l insulin, respectively). We conclude that insulin activation of erythrocyte insulin receptor kinase is not impaired in NIDDM and is not influenced by hyperglycemia.

Insulin-receptor kinase activity of adipose tissue from morbidly obese humans with and without NIDDM

Diabetes ◽  
1987 ◽  
Vol 36 (5) ◽  
pp. 620-625 ◽  
Author(s):  
M. K. Sinha ◽  
W. J. Pories ◽  
E. G. Flickinger ◽  
D. Meelheim ◽  
J. F. Caro
Keyword(s):  
Adipose Tissue ◽  
Insulin Receptor ◽  
Kinase Activity ◽  
Morbidly Obese ◽  
Receptor Kinase ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity
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