Evidence that translocation of the glucose transport activity is the major mechanism of insulin action on glucose transport in fat cells.

Kôno, Tetsuro; Robinson, F W; Blevins, Teresa; Ezaki, Osamu

doi:10.1016/s0021-9258(18)33914-0

Cited by 209 publications

(12 citation statements)

References 28 publications

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“…Since the opening of the Ca 2÷ channels by anti-GalC took as long as 6 min in some cells, this suggests that in those cells few Ca 2÷ channels are normally present in the plasma membrane, with the delay in influx reflecting the time required to recruit additional Ca 2÷ channels from intracellular membrane compartments. Similar recruitment and activation from internal compartments have been reported for glucose transporters in adipocyte membranes (Kono et al, 1982;Simpson and Cushman, 1985), ion transporters in epithelia (Schwartz and AI-Awqati;, Wade, 1986, and possibly Ca 2÷ channels in cortical astrocytes (Barres et al, 1989). This insertion and activation may depend upon a second messenger signaling system.…”

Section: Discussionsupporting

confidence: 66%

Glycolipids and transmembrane signaling: antibodies to galactocerebroside cause an influx of calcium in oligodendrocytes.

Dyer

Benjamins

1990

The Journal of Cell Biology

128

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Abstract. This is the first study to provide evidence that one function for the surface glycolipid galactocerebroside (GalC) is participation in the opening of Ca 2+ channels in oligodendroglia in culture. This glycolipid is a unique differentiation marker for myelin-producing cells; antibodies to GalC have been shown to markedly alter oligodendroglial morphology via disruption of microtubules (Dyer, C. A., and J. A. Benjamins. 1988. J. Neurosci. 8:4307--4318). This study demonstrates that extracellular EGTA blocks anti-GalC-induced disassembly of microtubules in oligodendroglial membrane sheets, demonstrating that an influx of extracellular Ca 2÷ mediates the cytoskeletal changes. The Ca 2÷ influx was examined directly by loading oligodendroglia with the fluorescent dye Indo-1 in defined medium, and measuring changes in Ca 2÷ in individual cells with a laser cytometer. Upon addition of anti-GalC IgG, a marked sustained increase in intracellular Ca 2÷ occurred in 80% of the oligodendroglia observed. EGTA blocked the increase, indicating the increase is due to an influx of extracellular Ca 2+, and not due to release from intracellular stores. The effect is specific, since Ca 2+ levels remain normal in oligodendroglia treated with nonimmune IgG; astrocytes do not respond to the anti-GalC. The Ca 2+ response in oligodendrocytes is dependent on concentration of antibody and GalC on the oligodendroglial membrane surface. The Ca 2+ influx is not mediated by voltage-sensitive Ca 2÷ channels: it is not blocked by cadmium, and depolarization with K ÷ does not mimic the response. The kinetics of the response suggest that second messenger-mediated opening of Ca 2÷ channels is involved. lvms have received increasing attention for their role in receptor-mediated signaling across cell membranes. In particular, glycolipids presumably associated with transmembrane proteins have been reported to participate in ligand binding and signaling; for example, cholera toxin binds to GMI ganglioside leading to activation of adenylate cyclase (see Fishman, 1982, for review). Glycolipids are involved in initiating such events as mitogenesis, morphogenesis, and cell recognition (Sharom and Grant, 1978;Grant and Peters, 1979;Hakomori, 1981;Spiegel and Wilchek, 1981;Thompson and Tillack, 1985;Facci et al., 1988;Curatolo, 1987;Bansal and Pfeiffer, 1989). However, little is known about the mechanisms underlying these effects.We have focused on the function of galactocerebroside (GalC), a glycolipid highly enriched on the surface of myelin-producing cells. Oligodendrocytes are the only cells in the central nervous system that express this lipid; although it is used widely as a unique marker for differentiation of oligodendrocytes, its role in the specialized membrane produced by these cells is not known. Several studies over the last decade indicate that antibodies to GalC can alter oligodendroglial morphology and myelination, providing indirect evidence that this glycolipid is involved in signal transduction (Diaz et al., 1978;Dorfman et al., ...

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Section: Discussionsupporting

confidence: 66%

Glycolipids and transmembrane signaling: antibodies to galactocerebroside cause an influx of calcium in oligodendrocytes.

Dyer

Benjamins

1990

The Journal of Cell Biology

128

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“…On the other hand, there is a considerable discrepancy between the effect of insulin on the transporter content of the plasma membrane, as assayed by these two methods, and its effect on the rate of transport. It has been reported that insulin increases the Vmax for 2-deoxyglucose uptake in 3T3-L1 adipocytes by a factor of 15, without any effect on Kin; the rate of transport of the nonphosphorylated hexose 3-0-methylglucose is also stimulated 15-fold (17). Under our conditions we typically find that 2-deoxyglucose uptake is stimulated 10-15-fold by insulin.…”

Section: Discussionsupporting

confidence: 62%

Insulin-induced translocation of glucose transporters from post-Golgi compartments to the plasma membrane of 3T3-L1 adipocytes.

Blok

Gibbs

Lienhard

et al. 1988

The Journal of Cell Biology

142

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Abstract. A semiquantitative method using immunocytochemistry on ultrathin cryosections and the protein A-gold technique was performed to study the effect of insulin on the cellular distribution of the glucose transporters in cultured 3T3-L1 adipocytes. In basal cells a substantial portion of the label was present in a tubulovesicular structure at the trans side of the Golgi apparatus, likely to represent the trans-Golgi reticulum, and in small vesicles present in the cytoplasm. Treatment with insulin induced a rapid translocation of transporters from the tubulovesicular structure to the plasma membrane. The transporter labeling of the plasma membrane increased three-fold and that of the tubulovesicular structure decreased by half. There was no effect of insulin on the degree of label in the small cytoplasmic vesicles. Removal of insulin from stimulated cells rapidly reversed the distribution of transporters to that seen in basal cells. This study thus provides the first morphological evidence for the occurrence of transporter translocation in insulin action and identifies for the first time the intracellular location of the responsive transporters.

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“…The present experiments have shown that almost all of the internal stores ofNa+/K+-ATPase seem to be recovered in fraction II, probably in the form of small and but partly sealed vesicles. It is widely accepted that insulin stimulates the translocation of glucose transporters from internal stores to the plasma membrane in adipocytes and muscles [26][27][28][29][30][31]. Furthermore, the existence of internal stores of Na+-selective channels [32] and H+-ATPase [33] has been shown.…”

Section: Discussionmentioning

confidence: 99%

Insulin stimulates the translocation of Na+/K+-dependent ATPase molecules from intracellular stores to the plasma membrane in frog skeletal muscle

Omatsu‐Kanbe

Kitasato

1990

Biochemical Journal

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The mechanism of the stimulation of Na+/K+ transport by insulin in frog skeletal muscle was studied. The ouabain-binding capacity in detergent-treated plasma membranes of insulin-exposed muscles was increased 1.9-fold compared with that of controls. Na+/K(+)-ATPase activity was found in an intracellular 'light fraction' (fraction II) prepared by using anion-exchange chromatography. Marker enzyme activities for plasma and Golgi membranes were not detected in this fraction. The specific activity of Na+/K(+)-ATPase in fraction II from insulin-exposed muscles was 58% of that in an identical fraction from control muscles. No significant difference in the protein yield of the plasma membrane preparation was observed between these two groups. In parallel with the decrease in the Na+/K(+)-ATPase activity in fraction II from insulin-exposed muscles, the ouabain-binding capacity in this fraction was also decreased. The addition of saponin to fraction II increased both Na+/K(+)-ATPase activity and ouabain binding, indicating that some of the Na+/K(+)-ATPase is located in sealed vesicles. These findings support the view that insulin stimulates the translocation of Na+/K(+)-ATPase molecules from fraction II to the plasma membrane.

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Evidence that translocation of the glucose transport activity is the major mechanism of insulin action on glucose transport in fat cells.

Cited by 209 publications

References 28 publications

Glycolipids and transmembrane signaling: antibodies to galactocerebroside cause an influx of calcium in oligodendrocytes.

Glycolipids and transmembrane signaling: antibodies to galactocerebroside cause an influx of calcium in oligodendrocytes.

Insulin-induced translocation of glucose transporters from post-Golgi compartments to the plasma membrane of 3T3-L1 adipocytes.

Insulin stimulates the translocation of Na+/K+-dependent ATPase molecules from intracellular stores to the plasma membrane in frog skeletal muscle

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