Diethelm M. Kirsch

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Catecholamine treatment of isolated rat adipocytes decreases insulin binding and inhibits insulin stimulation of the glucose-transport system. There is increasing evidence that the insulin signal is transmitted after insulin is bound to the receptor via a tyrosine kinase, which is an intrinsic part of the receptor. To find whether the receptor kinase is(More)
Phorbol ester treatment of isolated rat adipocytes inhibits insulin stimulation of the glucose transport system. We studied whether this effect is related to a modification of the insulin receptor kinase. Insulin receptor of tetradecanoyl-beta-phorbol acetate (TPA)-treated adipocytes was solubilized and partially purified, and its kinase activity was(More)
The insulin receptor contains in its beta-subunit a tyrosine (-) specific protein kinase. It is believed that transmission of an insulin signal across the plasma membrane of target cells of insulin action occurs through activation of this kinase, autophosphorylation of the insulin receptor beta-subunit and subsequent phosphorylation of other cellular(More)
Postganglionic compound action potential (AP) and intracellular NAD(P)H-fluorescence were recorded simultaneously in the perifused superior cervical ganglion of the rat (SCG) to study the effects of the bispyridinium oximes HGG12, HGG42 and obidoxime. HGG12 and HGG42 inhibit the compound action potential (AP) (ID50: 70 μM) and the reductive part of NAD(P)H(More)
The C-kinase activating phorbolester TPA (12-O-Tetradecanoyl-beta-phorbol-13-acetate) and PdBu (4-beta-Phorbol-12,13,dibutyrate) stimulated D-glucose transport twofold in isolated rat adipocytes but inhibited high affinity insulin binding and the responsiveness of D-glucose transport to insulin stimulation by about 30%. Phorbolesters have therefore(More)
Ciglitazone (cig), a thiazolidine-dione, lowers glucose and insulin levels in animal models of diabetes type II but not in controls. Since catecholamines given to rat adipocytes in vitro induce insulin resistance similar to that seen in type II diabetes in vivo, we measured the effect of cig on mono-A14-[125I]insulin binding and 3-O-methyl-D-glucose(More)
Receptor-associated protein kinase activity has been shown in all primary target tissues of insulin action in the rat and a function of insulin receptor phosphorylation in signal transmission was proposed. Insulin receptor phosphorylation so far has not been demonstrated in human target tissues of insulin. We describe here insulin receptor kinase activity(More)
The effects of pre-incubation with isoprenaline and noradrenaline on insulin binding and insulin stimulation of D-glucose transport in isolated rat adipocytes are reported. (1) Pre-incubation of the cells with isoprenaline (0.1-10 microM) in Krebs-Ringer-Hepes [4-(2-hydroxyethyl)-1-piperazine-ethanesulphonic acid] buffer (30 min, 37 degrees C) at D-glucose(More)
The effect of cAMP on insulin binding and insulin stimulation of glucose transport was investigated in isolated rat adipocytes. Preincubation for 30 min in medium containing 16 mmol/l glucose and either db-cAMP or bromo-cAMP in concentrations of 10(-4)-10(-3) M inhibited high affinity binding of insulin by 15 to 30% and glucose transport by 30 to 50%.(More)
The insulin receptor is associated with a protein kinase activity. This has been shown for the receptor of liver, fat, and some other tissues which are not primary targets of insulin action. Here kinase activity is demonstrated for the insulin receptor of rat skeletal and cardiac muscle with similar characteristics. Insulin (10(-7) mol/l) stimulates(More)
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