Regulation of glucose carrier activity by AlCl3 and phospholipase C in fat-cells

Obermaier-Kusser, B.; Mühlbacher, C; Mushack, Joanne; Rattenhuber, E.; Fehlmann, Max; Häring, Hans Ulrich

doi:10.1042/bj2560515

Cited by 33 publications

(34 citation statements)

References 29 publications

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“…PAF-stimulated GLUT4 Translocation-GTP␥S or NaF plus AlCl 3 treatments triggered the GLUT4myc translocation in both 3T3-L1-GLUT4myc adipocytes and CHO-GLUT4myc cells, as did the endogenous GLUT4 translocation in 3T3-L1-adipocytes (6,13,14,23).…”

Section: Resultsmentioning

confidence: 99%

“…However, we reported that the small GTP-binding proteins, Ras, Rab3D, Rad, and Rho are unlikely to be involved in the GLUT4 translocations with insulin, phorbol 12-myristate 13-acetate (PMA), and GTP␥S treatments, and that the signaling pathway of the GTP␥S-stimulated GLUT4 translocation is different from those of insulin and PMA treatments (22). In addition, NaF plus AlCl 3 treatment, which is known to activate heterotrimeric GTP-binding proteins, stimulates GLUT4 translocation and glucose uptake in adipocytes and in CHO cells (6,23). This suggests that heterotrimeric GTP-binding protein(s) may be involved in the GTP␥S-stimulated GLUT4 translocation.…”

mentioning

confidence: 99%

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Gq-coupled Receptors Transmit the Signal for GLUT4 Translocation via an Insulin-independent Pathway

Kishi

Hayashi

Wang

et al. 1996

Journal of Biological Chemistry

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Guanosine 5-O-(3-thiotriphosphate) (GTP␥S) induces the translocation of glucose transporter type 4 (GLUT4) from an intracellular pool to the cell surface and increases glucose uptake in adipocytes. The GTP-binding protein(s) responsible for the translocation has remained to be identified. Using a sensitive and quantitative method to assess the translocation of c-MYC epitope-tagged GLUT4, we obtained evidence that the activation of receptor-coupled G q (neither G i nor G s ) triggered GLUT4 translocation in cells, independently of insulin signaling pathway(s). Platelet-activating factor (PAF) induced GLUT4 translocation in the cells expressing the G i -and G q -coupled PAF receptor, but the translocation was induced even after pretreatment with wortmannin, an islet-activating protein and phorbol 12,13-dibutyrate. Norepinephrine triggered GLUT4 translocation in cells expressing the G q -coupled ␣ 1 -adrenergic receptor, but prostaglandin E 2 did not cause GLUT4 translocation in cells expressing the G s -coupled EP4 receptor or the G i -coupled EP3␣ receptor. The norepinephrine-stimulated GLUT4 translocation and glucose uptake via G q may possibly contribute to the fuel supply required for thermogenesis in brown adipocytes and for the enhanced contractility in cardiomyocytes, both of which have an abundant endogenous GLUT4. Glucose transporter type 4 (GLUT4)1 is expressed exclusively in adipocytes and myocytes (1, 2). Translocation of GLUT4 from an intracellular pool to the plasma membrane is thought to be a major mechanism of glucose uptake in response to insulin in these tissues (1-4). 3T3-L1 adipocytes have been recognized as an ideal model to investigate the mechanism of GLUT4 translocation and glucose uptake, because these cells have a large amount of endogenous GLUT4 and insulin receptors (5).To examine molecular mechanisms of GLUT4 translocation in 3T3-L1 adipocytes and Chinese hamster ovary (CHO) cells, we developed a highly sensitive and quantitative method to measure directly c-MYC epitope-tagged GLUT4 (GLUT4myc) on the cell surface (6). Using this system, we have found that phosphatidylinositol 3-kinase (PI 3-kinase, p85/p110 heterodimer type) is involved in signal transductions of GLUT4 translocation not only by insulin but also by platelet-derived growth factor and epidermal growth factor (7-9). Other investigators reported that PI 3-kinase plays a pivotal role in the insulin-stimulated GLUT1 and GLUT4 translocations in CHO cells and adipocytes, respectively (10 -12). Therefore, the CHO cell system as well as 3T3-L1 adipocytes are useful for studying molecular mechanisms of GLUT4 translocation (see "Discussion").On the other hand, GLUT4 translocation is also induced in permeabilized adipocytes by treatment with guanosine 5Ј-O-(3-thiotriphosphate) (GTP␥S) of nonhydrolyzable GTP analogs, as well as by insulin (13,14). The GTP␥S-induced GLUT4 translocation was also observed in 3T3-L1 adipocytes and CHO cells stably expressing the GLUT4myc, using this method of detection (6). However, the GTP-binding prote...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Gq-coupled Receptors Transmit the Signal for GLUT4 Translocation via an Insulin-independent Pathway

Kishi

Hayashi

Wang

et al. 1996

Journal of Biological Chemistry

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“…In the past few years evidence has accumulated which suggests that insulin receptor signalling may involve coupling to GTP-binding proteins [1][2][3][4][5][6][7]. This view is mainly supported by the effects of cholera and pertussis toxin on insulin action.…”

Section: Introductionmentioning

confidence: 99%

Regulation of cardiac insulin receptor function by guanosine nucleotides

1992

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The present study e.~amined the elTcct of [s-~S]GTP on the funct[ot~ of insulin receptors partially purified from adult rat eardiomyoeytes by WGA chromatography, [~'~S]GTP increased receptor autophosphorylation about two times and fully mimicked the stimulatory action of insulha on poly(Glu:Tyr) phosphorylatlon with no additional effect of the hormone. The effect of ["~S]GTP was specific, dose.dependent, and due to an increase in the Vm,,~ of the kinase. In the presence of ATP or AMP-PNP, insulin significantly enhanced the binding of [~SS]GTP to the partially purified insulin receptor. The findings suggest coupling of the insuli,a receptor to a G-protein which may be involved in the regulation of tyrosine klnase activity, Isolated cardiac myocyte; lnstdin receptor; Guanosine nucleotide binding protein; Tyrosine kinase

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“…In addition, GTP␥S can stimulate GLUT4 translocation in the absence of ATP, suggesting that ATP is required at an early step(s) in the insulin-signaling pathway and that a GTP-binding protein(s) functions at a more distal step(s) (11). The stimulatory effect of GTP␥S can also be mimicked by treatment with AlF 4 Ϫ , which is characteristic of the involvement of a heterotrimeric GTP binding protein (12,13). Consistent with this interpretation, adrenergic stimulation can induce GLUT4 translocation and glucose uptake in both cardiac myocytes (14,15) and brown adipocytes (16,17).…”

mentioning

confidence: 98%

Guanosine 5′-O-(3-Thiotriphosphate) (GTPγS) Stimulation of GLUT4 Translocation is Tyrosine Kinase-dependent

Elmendorf

Chen

Pessin

1998

Journal of Biological Chemistry

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Guanosine 5-O-(3-thiotriphosphate) (GTP␥S) treatment of permeabilized adipocytes results in GLUT4 translocation similar to that elicited by insulin treatment. However, although the selective phosphatidylinositol 3-kinase inhibitor, wortmannin, completely prevented insulin-stimulated GLUT4 translocation, it was without effect on GTP␥S-stimulated GLUT4 translocation. In addition, insulin was an effective stimulant, whereas GTP␥S was a very weak activator of the downstream Akt serine/threonine kinase. Consistent with an Akt-independent mechanism, guanosine 5-O-2-(thio) diphosphate inhibited insulin-stimulated GLUT4 translocation without any effect on the Akt kinase. Surprisingly, two functionally distinct tyrosine kinase inhibitors, genistein and herbimycin A, as well as microinjection of a monoclonal phosphotyrosine specific antibody, inhibited both GTP␥S-and insulin-stimulated GLUT4 translocation. Phosphotyrosine immunoblotting and specific immunoprecipitation demonstrated that GTP␥S did not elicit tyrosine phosphorylation of insulin receptor or insulin receptor substrate-1. In contrast to insulin, proteins in the 120 -130-kDa and 55-75-kDa range were tyrosine-phosphorylated following GTP␥S stimulation. Several of these proteins were identified and include protein-tyrosine kinase 2 (also known as CAK␤, RAFTK, and CADTK), pp125 focal adhesion tyrosine kinase, pp130 Crk-associated substrate, paxillin, and Cbl. These data demonstrate that the GTP␥S-stimulated GLUT4 translocation utilizes a novel tyrosine kinase pathway that is independent of both the phosphatidylinositol 3-kinase and the Akt kinase.

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Regulation of glucose carrier activity by AlCl3 and phospholipase C in fat-cells

Cited by 33 publications

References 29 publications

Gq-coupled Receptors Transmit the Signal for GLUT4 Translocation via an Insulin-independent Pathway

Gq-coupled Receptors Transmit the Signal for GLUT4 Translocation via an Insulin-independent Pathway

Regulation of cardiac insulin receptor function by guanosine nucleotides

Guanosine 5′-O-(3-Thiotriphosphate) (GTPγS) Stimulation of GLUT4 Translocation is Tyrosine Kinase-dependent

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