?Insulin-like? effects of lithium ion on isolated rat adipocytes I. Stimulation of glycogenesis beyond glucose transport

1983 ◽  
Vol 56 (2) ◽  
Author(s):  
Kang Cheng ◽  
Steven Creacy ◽  
Joseph Larner
Keyword(s):  
Glucose Transport ◽  
Lithium Ion ◽  
Rat Adipocytes ◽  
Isolated Rat ◽  
Stimulation Of

scholarly journals Catecholamine-induced insulin resistance of glucose transport in isolated rat adipocytes

1983 ◽  
Vol 216 (3) ◽  
pp. 737-745 ◽  
Author(s):  
D M Kirsch ◽  
M Baumgarten ◽  
T Deufel ◽  
F Rinninger ◽  
W Kemmler ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Insulin Binding ◽  
Affinity Binding ◽  
Insulin Stimulation ◽  
High Affinity Binding ◽  
Rat Adipocytes ◽  
High Affinity ◽  
Atp Levels ◽  
Isolated Rat ◽  
Stimulation Of

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 concentrations of 16 mM, in which normal ATP levels were maintained, caused a rightward-shift in sensitivity of D-glucose transport to insulin stimulation by 50% and a decrease in maximal responsiveness by 30% (2) [A14-125I]insulin binding was reduced significantly by 35% at insulin concentrations less than 100 mu-units/ml and Scatchard analysis showed that this consisted mainly of a decrease in high-affinity binding. (3) Pre-incubation with catecholamines under the same conditions but at low glucose concentrations (0-5 mM) caused a fall in intracellular ATP levels of 65 and 45% respectively. (4) The fall in ATP additionally lowered insulin binding by 50% at all insulin concentrations and a parallel shift of the binding curves in the Scatchard plot showed that this was due to a decrease in the number of receptors. (5) At low and high ATP concentrations the insulin stimulation of D-glucose transport was inhibited to a similar extent. (6) Pre-incubation with catecholamines thus inhibited insulin stimulation of D-glucose transport in rat adipocytes mainly by a decrease in high-affinity binding of insulin, which was not mediated by low ATP levels. This mechanism may play a role in the pathogenesis of catecholamine-induced insulin resistance in vivo.

Immunoelectron microscopic evidence that GLUT4 translocation explains the stimulation of glucose transport in isolated rat white adipose cells

2000 ◽  
Vol 113 (23) ◽  
pp. 4203-4210 ◽  
Author(s):  
D. Malide ◽  
G. Ramm ◽  
S.W. Cushman ◽  
J.W. Slot
Keyword(s):  
Adipose Tissue ◽  
Glucose Transport ◽  
Morphological Evidence ◽  
Glut4 Translocation ◽  
Transport Activity ◽  
Brown Adipose ◽  
Quantitative Immunoelectron Microscopy ◽  
Adipose Cells ◽  
Isolated Rat ◽  
Stimulation Of

We used an improved cryosectioning technique in combination with quantitative immunoelectron microscopy to study GLUT4 compartments in isolated rat white adipose cells. We provide clear evidence that in unstimulated cells most of the GLUT4 localizes intracellularly to tubulovesicular structures clustered near small stacks of Golgi and endosomes, or scattered throughout the cytoplasm. This localization is entirely consistent with that originally described in brown adipose tissue, strongly suggesting that the GLUT4 compartments in white and brown adipose cells are morphologically similar. Furthermore, insulin induces parallel increases (with similar magnitudes) in glucose transport activity, approximately 16-fold, and cell-surface GLUT4, approximately 12-fold. Concomitantly, insulin decreases GLUT4 equally from all intracellular locations, in agreement with the concept that the entire cellular GLUT4 pool contributes to insulin-stimulated exocytosis. In the insulin-stimulated state, GLUT4 molecules are not randomly distributed on the plasma membrane, but neither are they enriched in caveolae. Importantly, the total number of GLUT4 C-terminal epitopes detected by the immuno-gold method is not significantly different between basal and insulin-stimulated cells, thus arguing directly against a reported insulin-induced unmasking effect. These results provide strong morphological evidence (1) that GLUT4 compartments are similar in all insulin-sensitive cells and (2) for the concept that GLUT4 translocation almost fully accounts for the increase in glucose transport in response to insulin.

Effect of purified phospholipases on glucose transport, insulin binding, and insulin action in isolated rat adipocytes

1982 ◽  
Vol 4 (4) ◽  
pp. 261-271 ◽  
Author(s):  
Tj. Wieringa ◽  
G. Bruin ◽  
W. P. M. Meerwijk ◽  
H. M. J. Krans
Keyword(s):  
Glucose Transport ◽  
Insulin Action ◽  
Insulin Binding ◽  
Rat Adipocytes ◽  
Isolated Rat

Glucose transport in isolated rat adipocytes with measurements of L-arabinose uptake.

1978 ◽  
Vol 234 (2) ◽  
pp. E112 ◽  
Author(s):  
J E Foley ◽  
S W Cushman ◽  
L B Salans
Keyword(s):  
Glucose Transport ◽  
Transport System ◽  
Cytochalasin B ◽  
Competitive Inhibition ◽  
Facilitated Transport ◽  
Time Dependent ◽  
Rat Adipocytes ◽  
A Value ◽  
System Data ◽  
Isolated Rat

Data is presented suggesting that rates of L-arabinose transport, calculated from L-[1-14C]arabinose uptake measurements, can be used as indicators of changes in the rates of glucose transport in isolated rat adipocytes. L-[1-14C]arabinose, at 37 degrees C, was found to be nonmetabolizable and taken up by adipocytes exponentially with time reaching 95% of equilibrium in 30 min. When L-arabinose is corrected for background, the corrected uptake values conform to the time-dependent monoexponential uptake relationshiop predicted for a facilitated transport system and are not significantly different from 0 in the presence of 70 micron cytochalasin B. Transport rates were calculated from corrected uptake values near the half-maximal uptake of L-arabinose and from a value of the total amount of L-arabinose in the cell at equilibrium. Competitive inhibition of L-arabinose transport by glucose and countertransport of L-arabinose in the presence of glucose suggest that L-arabinose and glucose share the same transport system. Data is presented demonstrating the effect of insulin and dexamethasone on the transport system that confirms the conclusions obtained by other investigators using other methods.

scholarly journals Proteolytic cleavage of cellubrevin and vesicle-associated membrane protein (VAMP) by tetanus toxin does not impair insulin-stimulated glucose transport or GLUT4 translocation in rat adipocytes

1997 ◽  
Vol 321 (1) ◽  
pp. 233-238 ◽  
Author(s):  
Eric HAJDUCH ◽  
J. Carlos ALEDO ◽  
Colin WATTS ◽  
Harinder S. HUNDAL
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Glucose Uptake ◽  
Glucose Transport ◽  
Tetanus Toxin ◽  
Glucose Transporter ◽  
Detectable Effect ◽  
Glut4 Translocation ◽  
Rat Adipocytes ◽  
Isolated Rat

Acute insulin stimulation of glucose transport in fat and skeletal muscle occurs principally as a result of the hormonal induced translocation of the GLUT4 glucose transporter from intracellular vesicular stores to the plasma membrane. The precise mechanisms governing the fusion of GLUT4 vesicles with the plasma membrane are very poorly understood at present but may share some similarities with synaptic vesicle fusion, as vesicle-associated membrane protein (VAMP) and cellubrevin, two proteins implicated in the process of membrane fusion, are resident in GLUT4-containing vesicles isolated from rat and murine 3T3-L1 adipocytes respectively. In this study we show that proteolysis of both cellubrevin and VAMP, induced by electroporation of isolated rat adipocytes with tetanus toxin, does not impair insulin-stimulated glucose transport or GLUT4 translocation. The hormone was found to stimulate glucose uptake by approx. 16-fold in freshly isolated rat adipocytes. After a single electroporating pulse, the ability of insulin to activate glucose uptake was lowered, but the observed stimulation was nevertheless nearly 5-fold higher than the basal rate of glucose uptake. Electroporation of adipocytes with 600 nM tetanus toxin resulted in a complete loss of both cellubrevin and VAMP expression within 60 min. However, toxin-mediated proteolysis of both these proteins had no effect on the ability of insulin to stimulate glucose transport which was elevated approx. 5-fold, an activation of comparable magnitude to that observed in cells electroporated without tetanus toxin. The lack of any significant change in insulin-stimulated glucose transport was consistent with the finding that toxin-mediated proteolysis of both cellubrevin and VAMP had no detectable effect on insulin-induced translocation of GLUT4 in adipocytes. Our findings indicate that, although cellubrevin and VAMP are resident proteins in adipocyte GLUT4-containing vesicles, they are not required for the acute insulin-induced delivery of GLUT4 to the plasma membrane.

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