Cyclic AMP acutely stimulates translocation of the major insulin-regulatable glucose transporter GLUT4.

Kelada, A. S. M.; Macaulay, S. Lance; Proietto, Joseph

doi:10.1016/s0021-9258(19)50530-0

Cited by 43 publications

(2 citation statements)

References 28 publications

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“…More recently, the isoprenaline-induced phosphorylation of the transporter GLUT4 was proposed to be responsible for the decrease in its intrinsic activity (Lawrence et al, 1990). In a similar manner, cAMP analogues induced a translocation of GLUT4 to the plasma membrane which was of lower magnitude than that promoted by insulin, but which was not linked to a net increase in transport activity, suggesting that cAMP was involved in phosphorylation of and decrease in intrinsic activity of GLUT4 (Kelada et al, 1992). Even though it has been shown that GLUTI is, but to a lesser extent than GLUT4 (Zorzano et al, 1989), also subjected to translocation processes, little information is available on the regulation of this protein by isoprenaline.…”

Section: Introductionmentioning

confidence: 84%

β 3-adrenergic receptors are responsible for the adrenergic inhibition of insulin-stimulated glucose transport in rat adipocytes

Carpéné

Chalaux

Lizarbe

et al. 1993

Biochemical Journal

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The inhibition of insulin-stimulated glucose transport by isoprenaline, a mixed beta-adrenergic-receptor (AR) agonist, is well documented in rat adipocytes. Since it has been described that rat adipocytes possess not only beta 1- and beta 2- but also beta 3-ARs, the influence of various subtype-selective beta-AR agonists and antagonists on 2-deoxyglucose (2-DG) transport was assessed in order to characterize the beta-AR subtype involved in the adrenergic counter-regulation of the insulin effect. The stimulation of 2-DG transport by insulin was counteracted, in a dose-dependent manner, by all the beta-AR agonists tested, and the magnitude of the inhibition followed the rank order: BRL 37344 > isoprenaline = noradrenaline >> dobutamine = procaterol. The same rank order of potency was obtained for lipolysis activation. This is not in accordance with the pharmacological definition of a beta 1- or a beta 2-adrenergic effect, but agrees with the pharmacological pattern of a beta 3-adrenergic effect. The inhibitory effect of the beta 3-agonist BRL 37344 on insulin-stimulated 2-DG transport was not reversed by either the selective beta 1-antagonist ICI 89406 or the beta 2-antagonist ICI 118551. In addition, neither of these beta-antagonists was able to block the isoprenaline and noradrenaline effects, supporting major beta 3-adrenoceptor-subtype involvement in the adrenergic inhibition of insulin-stimulated 2-DG transport. Like isoprenaline, BRL 37344 inhibited (60% inhibition) insulin-stimulated glucose transport only when adenosine deaminase was present in the assay. Furthermore, the maximal inhibitory effects of isoprenaline and BRL 37344 were not additive, and were both dependent on albumin concentration in the incubation medium: they increased when the albumin concentration decreased in the medium from 3.5 to 1%. To conclude, the similarities between isoprenaline and BRL 37344 action on insulin-stimulated 2-DG transport, the poor efficacy of the beta 1-/beta 2-agonists and the lack of effect of selective beta 1- and beta 2-antagonists are compelling arguments to support the important role of beta 3-adrenoceptors in the adrenergic inhibition of glucose transport in rat adipocytes.

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Section: Introductionmentioning

confidence: 84%

β 3-adrenergic receptors are responsible for the adrenergic inhibition of insulin-stimulated glucose transport in rat adipocytes

Carpéné

Chalaux

Lizarbe

et al. 1993

Biochemical Journal

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“…Involvement of cAMP-mediated mechanisms was investigated to explain the mechanism of action. Treatment of isolated fat cells with isoproterenol or incubating microsomal membranes with cAMP-dependent protein kinase increased phosphorylation of GLUT4 which occurs on a serine residue (S 488 ) of the intracellular COOH terminus of the glucose transporter protein (James et al, 1989;Lawrence et al, 1990;Kelada et al, 1992). Under such conditions glucose transport activity was significantly altered; its inhibition occurred without decreasing the transporter number.…”

Section: Glucose Transport In Fat Cellsmentioning

confidence: 99%

Adrenergic regulation of adipocyte metabolism

et al. 1997

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Five adrenoceptor (AR) subtypes (beta 1, beta 2, beta 3, alpha 2 and alpha 1), are involved in the control of white and brown fat cell function. A number of metabolic events are controlled by the adrenergic system in fat cells. The stimulatory effect of catecholamines on lipolysis and metabolism is mainly connected to increments in cAMP levels, cAMP protein kinase activation and phosphorylation of various target proteins. Norepinephrine and epinephrine operate through differential recruitment of alpha 2- and beta-AR subtypes on the basis of their relative affinity for the different subtypes (the relative order of affinity is alpha 2 > beta 1 > or = beta 2 > beta 3 for norepinephrine). Antagonistic actions at the level of cAMP production exist between alpha 2- and beta 1-, beta 2- and beta 3-AR-mediated lipolytic effects in human white fat cells. The role of fat cell alpha 2-ARs, which largely outnumber beta-ARs in fat cells of certain fat deposits, in human and primate has never been clearly understood. The other AR type which is not linked to lipolysis regulation, the alpha 1-AR, is involved in the control of glycogenolysis and lactate production. Pharmacological approaches using in-situ microdialysis and selective alpha 2- and beta-AR agonists and antagonists have revealed sex- and tissue-specific differences in the adrenergic control of fat cell function and nutritive blood flow in the tissue surrounding the microdialysis probe.

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Acute and chronic regulation of Na+/K+-ATPase transport activity in the RN22 Schwann cell line in response to stimulation of cyclic AMP production

Stewart

Pekala

Lieberman

1998

Glia

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Na+/K+‐ATPase‐dependent Rb+ uptake of RN22 Schwann cells was stimulated by cholera toxin (0.25 μg/ml), forskolin (2 mM), or 8‐bromo cAMP (1 mM). At 2 h Rb+ uptake was increased by 162 ± 6% (cholera toxin), 151 ± 14% (forskolin), and 207 ± 15% (8‐bromo cAMP). Cholera toxin or 8‐bromo cAMP treatment for 12–24 h resulted in a second peak of Na+/K+‐ATPase‐dependent Rb+ transport activity of 186 ± 12 and 265 ± 9% of control, respectively. Cholera toxin also transiently stimulated the activity of the Na+, K+, 2Cl−‐cotransporter with a peak at 2 h (179 ± 9%), returning to basal levels by 24 h. Inhibition of the Na+,K+,2Cl−‐cotransporter by bumetanide (0.1 mM) or by reduction of the Na+ gradient (10 mM veratridine treatment) prevented the early peak in ATPase activity but not the second peak. These results indicated that the early transient stimulation of Na+/K+ ATPase activity by cholera toxin was due to an increase in cellular Na+, secondary to stimulation of Na+,K+,2Cl−‐cotransport activity. Western blot analysis of cellular homogenates and purified membrane fractions showed that the second peak of Rb+ uptake activity was a result of translocation of transport protein from an intracellular microsomal pool to the plasma membrane. Rb+ uptake by dominant negative protein kinase A mutants of the RN22 cell was not stimulated by cholera toxin treatment (acute or chronic) confirming the cAMP/protein kinase A dependency of both acute and long‐term regulation of transport activity. In the absence of a change in Michaelis constants or of an increase in total transport protein of cellular homogenates, neither a change in enzyme kinetics nor an increase in de novo synthesis of transport protein could account for the increase in transport activity. GLIA 23:349–360, 1998. © 1998 Wiley‐Liss, Inc.

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Cyclic AMP acutely stimulates translocation of the major insulin-regulatable glucose transporter GLUT4.

Cited by 43 publications

References 28 publications

β 3-adrenergic receptors are responsible for the adrenergic inhibition of insulin-stimulated glucose transport in rat adipocytes

β 3-adrenergic receptors are responsible for the adrenergic inhibition of insulin-stimulated glucose transport in rat adipocytes

Adrenergic regulation of adipocyte metabolism

Acute and chronic regulation of Na+/K+-ATPase transport activity in the RN22 Schwann cell line in response to stimulation of cyclic AMP production

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