Insulin stimulation of glucose transport in adipose cells. An energy-dependent process

Biochemistry ◽  
1977 ◽  
Vol 16 (6) ◽  
pp. 1151-1158 ◽  
Author(s):  
Visvanathan Chandramouli ◽  
Marianne Milligan ◽  
James R. Carter
Keyword(s):  
Glucose Transport ◽  
Insulin Stimulation ◽  
Dependent Process ◽  
Energy Dependent ◽  
Adipose Cells ◽  
Stimulation Of

scholarly journals Determination of the rates of appearance and loss of glucose transporters at the cell surface of rat adipose cells

1991 ◽  
Vol 278 (1) ◽  
pp. 235-241 ◽  
Author(s):  
A E Clark ◽  
G D Holman ◽  
I J Kozka
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Glucose Transport ◽  
Time Course ◽  
Transport Activity ◽  
Insulin Stimulation ◽  
Surface Labelling ◽  
Lag Period ◽  
Adipose Cells ◽  
Stimulation Of

We have used an impermeant bis-mannose compound (2-N-[4-(1-azi-2,2,2-trifluoroethyl)benzoyl]-1,3-bis-(D-mannos+ ++- 4-yloxy)-2- propylamine; ATB-BMPA) to photolabel the glucose transporter isoforms GLUT4 and GLUT1 that are present in rat adipose cells. Plasma-membrane fractions and light-microsome membrane fractions were both labelled by ATB-BMPA. The labelling of GLUT4 in the plasma membrane fraction from insulin-treated cells was approximately 3-fold higher than that of basal cells and corresponded with a decrease in the labelling of the light-microsome fraction. In contrast with this, the cell-surface labelling of GLUT4 from insulin-treated intact adipose cells was increased approximately 15-fold above basal levels. In these adipose cell preparations, insulin stimulated glucose transport activity approximately 30-fold. Thus the cell-surface labelling, but not the labelling of membrane fractions, closely corresponded with the stimulation of transport. The remaining discrepancy may be due to an approx. 2-fold activation of GLUT4 intrinsic transport activity. We have studied the kinetics of trafficking of transporters and found the following. (1) Lowering the temperature to 18 degrees C increased basal glucose transport and levels of cell-surface glucose transporters by approximately 3-fold. This net increase in transporters probably occurs because the process of recruitment of transporters is less temperature-sensitive than the process involved in internalization of cell-surface transporters. (2) The time course for insulin stimulation of glucose transport activity occurred with a slight lag period of 47 s and a t 1/2 3.2 min. The time course of GLUT4 and GLUT1 appearance at the cell surface showed no lag and a t 1/2 of approximately 2.3 min for both isoforms. Thus at early times after insulin stimulation there was a discrepancy between transporter abundance and transport activity. The lag period in the stimulation of transport activity may represent the time required for the approximately 2-fold stimulation of transporter intrinsic activity. (3) The decrease in transport activity after insulin removal occurred with a very high activation energy of 159 kJ.mol-1. There was thus no significant decrease in transport or less of cell-surface transporters over 60 min at 18 degrees C. The decrease in transport activity occurred with a t1/2 of 9-11 min at 37 degrees C.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals Effects of ML-9 on insulin stimulation of glucose transport in 3T3-L1 adipocytes.

1993 ◽  
Vol 268 (7) ◽  
pp. 5272-5278 ◽  
Author(s):  
G. Inoue ◽  
H. Kuzuya ◽  
T. Hayashi ◽  
M. Okamoto ◽  
Y. Yoshimasa ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Insulin Stimulation ◽  
Stimulation Of

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.

Exercise training increases the number of glucose transporters in rat adipose cells

1989 ◽  
Vol 257 (4) ◽  
pp. E520-E530
Author(s):  
M. F. Hirshman ◽  
L. J. Wardzala ◽  
L. J. Goodyear ◽  
S. P. Fuller ◽  
E. D. Horton ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Glucose Transport ◽  
Glucose Transporters ◽  
Membrane Transporters ◽  
Control Group ◽  
Transport Activity ◽  
Insulin Stimulation ◽  
Adipose Cell ◽  
Adipose Cell Size ◽  
Adipose Cells

We studied the mechanism for the increase in glucose transport activity that occurs in adipose cells of exercise-trained rats. Glucose transport activity, glucose metabolism, and the subcellular distribution of glucose transporters were measured in adipose cells from rats raised in wheel cages for 6 wk (mean total exercise 350 km/rat), age-matched sedentary controls, and young sedentary controls matched for adipose cell size. Basal rates of glucose transport and metabolism were greater in cells from exercise-trained rats compared with young controls, and insulin-stimulated rates were greater in the exercise-trained rats compared with both age-matched and young controls. The numbers of plasma membrane glucose transporters were not different among groups in the basal state; however, with insulin stimulation, cells from exercise-trained animals had significantly more plasma membrane transporters than young controls or age-matched controls. Exercise-trained rats also had more low-density microsomal transporters than control rats in the basal state. When the total number of glucose transporters/cell was calculated, the exercise-trained rats had 42% more transporters than did either control group. These studies demonstrate that the increased glucose transport and metabolism observed in insulin-stimulated adipose cells from exercise-trained rats is due, primarily, to an increase in the number of plasma membrane glucose transporters translocated from an enlarged intracellular pool.

Insulin stimulation of adipocyte membrane glucose transport

1987 ◽  
Vol 36 (14) ◽  
pp. 2305-2310 ◽  
Author(s):  
Paul A. Hyslop ◽  
Christopher E. Kuhn† ◽  
Richard D. Sauerheber
Keyword(s):  
Glucose Transport ◽  
Insulin Stimulation ◽  
Stimulation Of

scholarly journals Translocation of the brain-type glucose transporter largely accounts for insulin stimulation of glucose transport in BC3H-1 myocytes

1990 ◽  
Vol 269 (3) ◽  
pp. 597-601 ◽  
Author(s):  
D M Calderhead ◽  
K Kitagawa ◽  
G E Lienhard ◽  
G W Gould
Keyword(s):  
Glucose Transport ◽  
Glucose Transporter ◽  
Fold Increase ◽  
The Other ◽  
Insulin Stimulation ◽  
Glut 1 ◽  
Glut 4 ◽  
Rat Soleus Muscle ◽  
The Brain ◽  
Stimulation Of

Insulin-stimulated glucose transport was examined in BC3H-1 myocytes. Insulin treatment lead to a 2.7 +/- 0.3-fold increase in the rate of deoxyglucose transport and, under the same conditions, a 2.1 +/- 0.1-fold increase in the amount of the brain-type glucose transporter (GLUT 1) at the cell surface. It has been shown that some insulin-responsive tissues express a second, immunologically distinct, transporter, namely GLUT 4. We report here that BC3H-1 myocytes and C2 and G8 myotubes express only GLUT 1; in contrast, rat soleus muscle and heart express 3-4 times higher levels of GLUT 4 than GLUT 1. Thus translocation of GLUT 1 can account for most, if not all, of the insulin stimulation of glucose transport in BC3H-1 myocytes. On the other, hand, neither BC3H-1 myocytes nor the other muscle-cell lines are adequate as models for the study of insulin regulation of glucose transport in muscle tissue.

scholarly journals Osmotic Shock Inhibits Insulin Signaling by Maintaining Akt/Protein Kinase B in an Inactive Dephosphorylated State

1999 ◽  
Vol 19 (7) ◽  
pp. 4684-4694 ◽  
Author(s):  
Dong Chen ◽  
Raymond V. Fucini ◽  
Ann Louise Olson ◽  
Brian A. Hemmings ◽  
Jeffrey E. Pessin
Keyword(s):  
Protein Kinase ◽  
Insulin Receptor ◽  
Glucose Transport ◽  
Protein Kinase B ◽  
Osmotic Shock ◽  
Glycogen Synthesis ◽  
Type I ◽  
Transport Activity ◽  
Insulin Stimulation ◽  
Stimulation Of

ABSTRACT We have previously reported that insulin and osmotic shock stimulate an increase in glucose transport activity and translocation of the insulin-responsive glucose transporter isoform GLUT4 to the plasma membrane through distinct pathways in 3T3L1 adipocytes (D. Chen, J. S. Elmendorf, A. L. Olson, X. Li, H. S. Earp, and J. E. Pessin, J. Biol. Chem. 272:27401–27410, 1997). In investigations of the relationships between these two signaling pathways, we have now observed that these two stimuli are not additive, and, in fact, osmotic shock pretreatment was found to completely prevent any further insulin stimulation of glucose transport activity and GLUT4 protein translocation. In addition, osmotic shock inhibited the insulin stimulation of lipogenesis and glycogen synthesis. This inhibition of insulin-stimulated downstream signaling occurred without any significant effect on insulin receptor autophosphorylation or tyrosine phosphorylation of insulin receptor substrate 1 (IRS1). Furthermore, there was no effect on either the insulin-stimulated association of the p85 type I phosphatidylinositol (PI) 3-kinase regulatory subunit with IRS1 or phosphotyrosine antibody-immunoprecipitated PI 3-kinase activity. In contrast, osmotic shock pretreatment markedly inhibited the insulin stimulation of protein kinase B (PKB) and p70S6 kinase activities. In addition, the dephosphorylation of PKB was prevented by pretreatment with the phosphatase inhibitors okadaic acid and calyculin A. These data support a model in which osmotic shock-induced insulin resistance of downstream biological responses results from an inhibition of insulin-stimulated PKB activation.

scholarly journals Affinity change of the adipocyte receptor fails to alter insulin-stimulated glucose transport

1982 ◽  
Vol 202 (1) ◽  
pp. 263-265 ◽  
Author(s):  
Michael L. McCaleb ◽  
David B. Donner
Keyword(s):  
Insulin Receptor ◽  
Glucose Transport ◽  
Maximum Response ◽  
Simple Relationship ◽  
Insulin Stimulation ◽  
Receptor Affinity ◽  
Maximal Sensitivity ◽  
Affinity Change ◽  
Stimulation Of

Occupancy increased the affinity of the insulin receptor of the adipocyte. During the affinity change the half-maximal sensitivity of glucose transport to insulin stimulation was unaltered. Decreased maximum response of transport only occurred after the affinity change. There was not a simple relationship between receptor affinity and insulin stimulation of glucose transport in the adipocyte.

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