Energy-dependent and protein synthesis-independent recycling of the insulin-sensitive glucose transport mechanism in fat cells.

Kôno, Tetsuro; Suzuki, Kazuo; Dansey, L E; Robinson, F W; Blevins, Teresa

doi:10.1016/s0021-9258(19)69179-9

Cited by 206 publications

(12 citation statements)

References 38 publications

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“…Sugar transport in skeletal muscle is stimulated by insulin, metabolic depletion, and contractile activity [see ]. Insulin appears to stimulate transport via a recruitment mechanism similar to that found in adipose (Wardzala & Jeanrenaud, 1983;Cushman & Wardzala, 1980;Suzuki & Kono, 1980;Kono et al, 1981). In adipose tissue, insulin-stimulated carrier recruitment is an energy-dependent phenomenon (Kono et al, 1981).…”

Section: Discussionmentioning

confidence: 77%

Anomalous asymmetric kinetics of human red cell hexose transfer: the role of cytosolic adenosine 5'-triphosphate

Carruthers¹

1986

Biochemistry

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Cytosolic adenosine 5'-triphosphate (ATP) modifies the properties of human red cell sugar transport. This interaction has been examined by analysis of substrate-induced sugar transporter intrinsic fluorescence quenching and by determination of Michaelis and velocity constants for D-glucose transport in red cell ghosts and inside-out vesicles lacking and containing ATP. When excited at 295 nm, human erythrocyte ghosts stripped of peripheral proteins display an emission spectrum characterized by a scattering peak and a single emission peak centered at about 333 nm. Addition of sugar transport substrate or cytochalasin B and phloretin (sugar transport inhibitors) reduces emission peak height by 10% and 5%, respectively. Cytochalasin B induced quenching is a simple saturable phenomenon with an apparent Kd (app Kd) of 60 nM and a capacity of 1.4 nmol of sites/mg of membrane protein. Quenching by D-glucose (and other transported sugars) is characterized by at least two (high and low) app Kd parameters. Inhibitor studies indicate that these sites correspond to sugar efflux and influx sites, respectively, and that both sites can exist simultaneously. ATP induces quenching of stripped ghost fluorescence with half-maximal effects at 20-30 microM ATP. ATP reduces the low app Kd and increases the high app Kd for sugar-induced fluorescence quenching. D-Glucose transport in intact red cells is asymmetric (Km and Vmax for influx less than Km and Vmax for efflux). In addition, two operational Km parameters for efflux are detected in zero- and infinite-trans efflux conditions. Protein-mediated sugar transport in ghosts and inside-out vesicles (IOVs) is symmetric with respect to Km and Vmax for entry and exit, and only one Km for exit is detected. Addition of millimolar levels of ATP to the interior of ghosts or to the exterior of IOVs restores both transport asymmetry and two operational Km parameters for native efflux. A model for red cell hexose transport is proposed in which ATP modifies the catalytic properties of the transport system. This model mimics the behavior of the sugar transport systems of intact cells, ghosts, and inside-out vesicles.

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Section: Discussionmentioning

confidence: 77%

Anomalous asymmetric kinetics of human red cell hexose transfer: the role of cytosolic adenosine 5'-triphosphate

Carruthers¹

1986

Biochemistry

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“…It is not possible to definitively distinguish between these two models unless additional assumptions are made. By analogy with exocytosis, it is probable that vesicle translocation is a temperature-and energy-dependent process, as has been noted by Kono et al (1981) and . If one assumes that the signal which triggers this event is rapidly generated, then a mechanism analogous to model II could be invoked to explain the timeand temperature-dependent stimulation of the Na+ pump.4 The lag time observed with H202 is also consistent with the translocation mechanism of model II, if it is assumed that peroxide mimics the action of the signal "X".…”

Section: Time(min)mentioning

confidence: 75%

Insulin activation of (sodium, potassium)-adenosine triphosphatase exhibits a temperature-dependent lag time. Comparison to activation of the glucose transporter

Resh¹

1983

Biochemistry

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The time course of insulin activation of sodium and potassium ion activated adenosinetriphosphatase [(Na+,K+)ATPase] was studied in the rat adipocyte and was compared to activation of the glucose transporter. Under conditions in which the binding of insulin to its cell surface receptor was not rate limiting, a distinct time lag was apparent between insulin addition and stimulation of transport activity. At 37 degrees C, 40-50 s elapsed before an increase in Rb+ uptake [a measure of (Na+,K+)ATPase transport activity] or 2-deoxyglucose uptake could be observed. This lag time increased in an identical manner for both transport processes as the temperature was lowered to 23 degrees C. Addition of the insulinomimetic agent hydrogen peroxide also produced a lag time similar to that for insulin before activation of Rb+ and 2-deoxyglucose uptakes was detected. These data provide the first evidence of a discrete time lag involved during stimulation of the adipocyte (Na+,K+)ATPase. A model for the molecular mechanism of insulin activation of (Na+,K+)ATPase is presented that incorporates these results into the hypothesis of insulin mediated "translocation" of glucose transporters to the plasma membrane.

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“…A classic cell model which was widely used to study the signal flow from the receptor to the glucose transport system is the isolated adipocyte where activation and deactivation of the glucose transport system can be easily studied [136,137]. Almost 10 years ago it was shown in this cell model by Cushman et al [138] and Kono et al [139] that insulin induces a translocation of glucose carriers from intracellular membranes to the plasma membrane. In the meantime data from many different groups, including our own, have suggested that a purely translocation model is not sufficient to explain the insulin effect [99,116,[140][141][142][143][144].…”

Section: Signal Transduction To the Glucose Transport System: The Fat Cell Modelmentioning

confidence: 99%

The insulin receptor: signalling mechanism and contribution to the pathogenesis of insulin resistance

Häring

1991

Diabetologia

131

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The insulin receptor is a heterotetrameric structure consisting of two alpha-subunits of Mr 135 kilodalton on the outside of the plasma membrane connected by disulphide bonds to beta-subunits of Mr 95 kilodalton which are transmembrane proteins. Insulin binding to the alpha-subunit induces conformational changes which are transduced to the beta-subunit. This leads to the activation of a tyrosine kinase activity which is intrinsic to the cytoplasmatic domains of the beta-subunit. Activation of the tyrosine kinase activity of the insulin receptor represents an essential step in the transduction of an insulin signal across the plasma membrane of target cells. Signal transduction on the post-kinase level is not yet understood in detail, possible mechanisms involve phosphorylation of substrate proteins at tyrosine residues, activation of serine kinases, the interaction with G-proteins, phospholipases and phosphatidylinositol kinases. Studies in multiple insulin-resistant cell models have demonstrated that an impaired response of the tyrosine kinase to insulin stimulation is one potential mechanism causing insulin resistance. An impairment of the insulin effect on tyrosine kinase activation in all major target tissues of insulin, in particular the skeletal muscle was demonstrated in Type 2 (non-insulin-dependent) diabetic patients. There is no evidence that the impaired tyrosine kinase response in the skeletal muscle is a primary defect, however, it is likely that this abnormality of insulin signal transduction contributes significantly to the pathogenesis of the insulin-resistant state in Type 2 diabetes.

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Energy-dependent and protein synthesis-independent recycling of the insulin-sensitive glucose transport mechanism in fat cells.

Cited by 206 publications

References 38 publications

Anomalous asymmetric kinetics of human red cell hexose transfer: the role of cytosolic adenosine 5'-triphosphate

Anomalous asymmetric kinetics of human red cell hexose transfer: the role of cytosolic adenosine 5'-triphosphate

Insulin activation of (sodium, potassium)-adenosine triphosphatase exhibits a temperature-dependent lag time. Comparison to activation of the glucose transporter

The insulin receptor: signalling mechanism and contribution to the pathogenesis of insulin resistance

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