Amine oxidase substrates mimic several of the insulin effects on adipocyte differentiation in 3T3 F442A cells

2001 ◽  
Vol 356 (3) ◽  
pp. 769-777 ◽  
Author(s):  
Emi FONTANA ◽  
Jérémie BOUCHER ◽  
Luc MARTI ◽  
José Miguel LIZCANO ◽  
Xavier TESTAR ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Glucose Transporter ◽  
Adipocyte Differentiation ◽  
Amine Oxidase ◽  
Chronic Administration ◽  
Mao Inhibitor ◽  
Amine Oxidation ◽  
Adipose Conversion ◽  
Triacylglycerol Accumulation ◽  
Stimulation Of

We have previously reported that substrates of monoamine oxidase (MAO) and semicarbazide-sensitive amine oxidase (SSAO) exert short-term insulin-like effects in rat adipocytes, such as stimulation of glucose transport. In the present work, we studied whether these substrates could also mimic long-term actions of insulin. Adipose differentiation of 3T3 F442A cells, which is highly insulin-dependent, served as a model to test the effects of sustained administration of amine oxidase substrates. Daily treatment of confluent cells with 0.75mM tyramine (a substrate of MAO and SSAO) or benzylamine (a substrate of SSAO) over 1 week caused the acquisition of typical adipocyte morphology. The stimulation of protein synthesis and triacylglycerol accumulation caused by tyramine or benzylamine reached one half of that promoted by insulin. This effect was insensitive to pargyline (an MAO inhibitor), but was inhibited by semicarbazide (an SSAO inhibitor) and by N-acetylcysteine (an antioxidant agent), suggesting the involvement of the H2O2 generated during SSAO-dependent amine oxidation. Chronic administration of amine oxidase substrates also induced the emergence of adipose conversion markers, such as aP2, glycerol-3-phosphate dehydrogenase, the glucose transporter GLUT4, and SSAO itself. Moreover, cells treated with amines acquired the same insulin sensitivity regarding glucose transport as adipocytes classically differentiated with insulin. In all, most of the adipogenic effects of amines were additive to insulin. Our data reveal that amine oxidase substrates partially mimic the adipogenic effect of insulin in cultured preadipocytes. Furthermore, they suggest that SSAO not only represents a novel late marker of adipogenesis, but could also be directly involved in the triggering of terminal adipocyte differentiation.

scholarly journals Novel Facet of an Old Dietary Molecule? Direct Influence of Caffeine on Glucose and Biogenic Amine Handling by Human Adipocytes

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 3831
Author(s):  
Wiem Haj Ahmed ◽  
Nathalie Boulet ◽  
Anaïs Briot ◽  
Barry J. Ryan ◽  
Gemma K. Kinsella ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Amine Oxidase ◽  
Human Adipose Tissue ◽  
Lipid Solubility ◽  
Human Adipocytes ◽  
Peripheral Tissues ◽  
Amine Oxidation ◽  
High Lipid ◽  
The Central Nervous System ◽  
High Lipid Solubility

Caffeine is a plant alkaloid present in food and beverages consumed worldwide. It has high lipid solubility with recognized actions in the central nervous system and in peripheral tissues, notably the adipose depots. However, the literature is scant regarding caffeine’s influence on adipocyte functions other than lipolysis, such as glucose incorporation into lipids (lipogenesis) and amine oxidation. The objective of this study was to explore the direct effects of caffeine and of isobutylmethylxanthine (IBMX) on these adipocyte functions. Glucose transport into fat cells freshly isolated from mice, rats, or humans was monitored by determining [3H]-2-deoxyglucose (2-DG) uptake, while the incorporation of radiolabeled glucose into cell lipids was used as an index of lipogenic activity. Oxidation of benzylamine by primary amine oxidase (PrAO) was inhibited by increasing doses of caffeine in human adipose tissue preparations with an inhibition constant (Ki) in the millimolar range. Caffeine inhibited basal and insulin-stimulated glucose transport as well as lipogenesis in rodent adipose cells. The antilipogenic action of caffeine was also observed in adipocytes from mice genetically invalidated for PrAO activity, indicating that PrAO activity was not required for lipogenesis inhibition. These caffeine inhibitory properties were extended to human adipocytes: relative to basal 2-DG uptake, set at 1.0 ± 0.2 for 6 individuals, 0.1 mM caffeine tended to reduce uptake to 0.83 ± 0.08. Insulin increased uptake by 3.86 ± 1.11 fold when tested alone at 100 nM, and by 3.21 ± 0.80 when combined with caffeine. Our results reinforce the recommendation of caffeine’s potential in the treatment or prevention of obesity complications.

scholarly journals The Formation of an Insulin-responsive Vesicular Cargo Compartment Is an Early Event in 3T3-L1 Adipocyte Differentiation

1999 ◽  
Vol 10 (5) ◽  
pp. 1581-1594 ◽  
Author(s):  
Amr K. El-Jack ◽  
Konstantin V. Kandror ◽  
Paul F. Pilch
Keyword(s):  
Glucose Transport ◽  
Glucose Transporter ◽  
Adipocyte Differentiation ◽  
Receptor Trafficking ◽  
Early Event ◽  
Glucose Transporter 1 ◽  
Glut4 Expression ◽  
Velocity Gradients ◽  
Dependent Inhibition ◽  
Intracellular Glucose

Differentiating 3T3-L1 cells exhibit a dramatic increase in the rate of insulin-stimulated glucose transport during their conversion from proliferating fibroblasts to nonproliferating adipocytes. On day 3 of 3T3-L1 cell differentiation, basal glucose transport and cell surface transferrin binding are markedly diminished. This occurs concomitant with the formation of a distinct insulin-responsive vesicular pool of intracellular glucose transporter 1 (GLUT1) and transferrin receptors as assessed by sucrose velocity gradients. The intracellular distribution of the insulin-responsive aminopeptidase is first readily detectable on day 3, and its gradient profile and response to insulin at this time are identical to that of GLUT1. With further time of differentiation, GLUT4 is expressed and targeted to the same insulin-responsive vesicles as the other three proteins. Our data are consistent with the notion that a distinct insulin-sensitive vesicular cargo compartment forms early during fat call differentiation and its formation precedes GLUT4 expression. The development of this compartment may result from the differentiation-dependent inhibition of constitutive GLUT1 and transferrin receptor trafficking such that there is a large increase in, or the new formation of, a population of postendosomal, insulin-responsive vesicles.

scholarly journals Trafficking of glucose transporters in 3T3-L1 cells. Inhibition of trafficking by phenylarsine oxide implicates a slow dissociation of transporters from trafficking proteins

1992 ◽  
Vol 281 (3) ◽  
pp. 809-817 ◽  
Author(s):  
J Yang ◽  
A E Clark ◽  
R Harrison ◽  
I J Kozka ◽  
G D Holman
Keyword(s):  
Cell Surface ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Fluid Phase ◽  
Transport Activity ◽  
Phenylarsine Oxide ◽  
Fluid Phase Endocytosis ◽  
Surface Labelling ◽  
Slow Dissociation ◽  
Stimulation Of

We have compared the rates of insulin stimulation of cell-surface availability of glucose-transporter isoforms (GLUT1 and GLUT4) and the stimulation of 2-deoxy-D-glucose transport in 3T3-L1 cells. The levels of cell-surface transporters have been assessed by using the bismannose compound 2-N-[4-(1-azi-2,2,2-trifluoroethyl)benzoyl]-1,3-bis(D-mannos -4-yloxy) propyl-2-amine (ATB-BMPA). At 27 degrees C the half-times for the appearance of GLUT1 and GLUT4 at the cell surface were 5.7 and 5.4 min respectively and were slightly shorter than that for the observed stimulation of transport activity (t 1/2 8.6 min). This lag may be due to a slow dissociation of surface transporters from trafficking proteins responsible for translocation. When fully-insulin-stimulated cells were subjected to a low-pH washing procedure to remove insulin at 37 degrees C, the cell-surface levels of GLUT1 and GLUT4 decreased, with half-times of 9.2 and 6.8 min respectively. These times correlated well with decrease in 2-deoxy-D-glucose transport activity that occurred during this washing procedure (t1/2 6.5 min). When fully-insulin-stimulated cells were treated with phenylarsine oxide (PAO), a similar decrease in transport activity occurred (t1/2 9.8 min). However, surface labelling showed that this corresponded with a decrease in GLUT4 only (t1/2 7.8 min). The cell-surface level of GLUT1 remained high throughout the PAO treatment. Light-microsome membranes were isolated from cells which had been cell-surface-labelled with ATB-BMPA. Internalization of both transporter isoforms to this pool occurred when cells were maintained in the presence of insulin for 60 min. In contrast with the surface-labelling results, we have shown that the transfer to the light-microsome pool of both transporters occurred in cells treated with insulin and PAO. These results suggest that both transporters are recycled by fluid-phase endocytosis and exocytosis. PAO may inhibit this recycling at a stage which involves the re-emergence of internalized transporters at the plasma membrane. The GLUT1 transporters that are recycled to the surface in insulin- and PAO-treated cells appear to have low transport activity. This may be because of a failure to dissociate fully from trafficking proteins at the cell surface. GLUT4 transporters appear to have a greater tendency to remain internalized if the normal mechanisms that commit transporters to the cell surface, such as dissociation from trafficking proteins, are uncoupled.

Effect of diet on insulin- and contraction-mediated glucose transport and uptake in rat muscle

1995 ◽  
Vol 269 (3) ◽  
pp. R544-R551 ◽  
Author(s):  
X. Han ◽  
T. Ploug ◽  
H. Galbo
Keyword(s):  
Glucose Uptake ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Fiber Types ◽  
Transport Capacity ◽  
Glut 1 ◽  
Glut 4 ◽  
Red Muscle ◽  
Muscle Glucose Transport ◽  
Stimulation Of

A diet rich in fat diminishes insulin-mediated glucose uptake in muscle. This study explored whether contraction-mediated glucose uptake is also affected. Rats were fed a diet rich in fat (FAT, 73% of energy) or carbohydrate (CHO, 66%) for 5 wk. Hindquarters were perfused, and either glucose uptake or glucose transport capacity (uptake of 3-O-[14C]-methyl-D-glucose (40 mM)) was measured. Amounts of glucose transporter isoform GLUT-1 and GLUT-4 glucose-transporting proteins were determined by Western blot. Glucose uptake was lower (P < 0.05) in hindlegs from FAT than from CHO rats at submaximum and maximum insulin [4 +/- 0.4 vs. 5 +/- 0.3 (SE) mumol.min-1.leg-1 at 150 microU/ml insulin] as well as during prolonged stimulation of the sciatic nerve (4.4 +/- 0.4 vs. 5.6 +/- 0.6 mumol.min-1.leg-1). Maximum glucose transport elicited by insulin (soleus: 1.7 +/- 0.2 vs. 2.6 +/- 0.2 mumol.g-1.5 min-1, P < 0.05) or contractions (soleus: 1.8 +/- 0.2 vs. 2.6 +/- 0.3, P < 0.05) in red muscle was decreased in parallel in FAT compared with CHO rats. GLUT-4 content was decreased by 13-29% (P < 0.05) in the various fiber types, whereas GLUT-1 content was identical in FAT compared with CHO rats. It is concluded that a FAT diet reduces both insulin and contraction stimulation of glucose uptake in muscle and that these effects are associated with diminished skeletal muscle glucose transport capacities and GLUT-4 contents.

Stimulation of glucose transport in skeletal muscle by hypoxia

1991 ◽  
Vol 70 (4) ◽  
pp. 1593-1600 ◽  
Author(s):  
G. D. Cartee ◽  
A. G. Douen ◽  
T. Ramlal ◽  
A. Klip ◽  
J. O. Holloszy
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Muscle Contraction ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Cytochalasin B ◽  
Sugar Transport ◽  
Transport Activity ◽  
Hindlimb Muscles ◽  
Stimulation Of

Hypoxia caused a progressive cytochalasin B-inhibitable increase in the rate of 3-O-methylglucose transport in rat epitrochlearis muscles to a level approximately six-fold above basal. Muscle ATP concentration was well maintained during hypoxia, and increased glucose transport activity was still present after 15 min of reoxygenation despite repletion of phosphocreatine. However, the increase in glucose transport activity completely reversed during a 180-min-long recovery in oxygenated medium. In perfused rat hindlimb muscles, hypoxia caused an increase in glucose transporters in the plasma membrane, suggesting that glucose transporter translocation plays a role in the stimulation of glucose transport by hypoxia. The maximal effects of hypoxia and insulin on glucose transport activity were additive, whereas the effects of exercise and hypoxia were not, providing evidence suggesting that hypoxia and exercise stimulate glucose transport by the same mechanism. Caffeine, at a concentration too low to cause muscle contraction or an increase in glucose transport by itself, markedly potentiated the effect of a submaximal hypoxic stimulus on sugar transport. Dantrolene significantly inhibited the hypoxia-induced increase in 3-O-methylglucose transport. These effects of caffeine and dantrolene suggest that Ca2+ plays a role in the stimulation of glucose transport by hypoxia.

Control of glucose transport by GLUT1: Regulated secretion in an unexpected environment

1995 ◽  
Vol 15 (6) ◽  
pp. 427-443 ◽  
Author(s):  
Christopher C. Widnell
Keyword(s):  
Plasma Membrane ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Standard Medium ◽  
Cytoplasmic Vesicles ◽  
Infected Cells ◽  
Vesicular Stomatitis ◽  
Cellular Stresses ◽  
Specific Membrane ◽  
Stimulation Of

Studies designed to elucidate the mechanism of regulation of the GLUT1 isoform of the glucose transporter in response to a variety of cellular stresses are reviewed. Using ts mutants of vesicular stomatitis virus, it was shown that the viral L gene was responsible for the stimulation of glucose transport in infected cells. Immunofluorescence of GLUT1 demonstrated that the increase in glucose transport was the consequence of a translocation of the transporter from a reservoir in cytoplasmic vesicles to the plasma membrane. When cells were cycled between deficient and standard medium, the change in glucose transport rates was paralleled by a cycling of the transporter between the plasma membrane and the cytoplasmic vesicles. The redistribution of GLUT1 was not a consequence of a general redistribution of recycling plasma membrane proteins. Instead, the findings focus attention on the regulated exocytosis of specific membrane constituents in cells that, until recently, were not thought to exhibit this capacity.

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.

Thyroid hormone increases the partitioning of glucose transporters to the plasma membrane in ARL 15 cells

1995 ◽  
Vol 269 (3) ◽  
pp. E605-E610
Author(s):  
R. S. Haber ◽  
C. M. Wilson ◽  
S. P. Weinstein ◽  
A. Pritsker ◽  
S. W. Cushman
Keyword(s):  
Gene Expression ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Transporter Gene ◽  
Glut 1 ◽  
Surface Partitioning ◽  
Enhanced Surface ◽  
Stimulation Of

The stimulation of glucose transport by 3,5,3'-triiodo-L-thyronine (T3) in the liver-derived ARL 15 cell line is only partly attributable to increased GLUT-1 glucose transporter gene expression. To test the hypothesis that T3 increases the partitioning of GLUT-1 to the cell surface, we quantitated surface GLUT-1 using the photolabel ATB-[3H]BMPA. In control cells only approximately 20% of total cellular GLUT-1 was present at the cell surface. T3 treatment (100 nM) for 6 h increased the rate of 2-deoxy-[3H]glucose (2-DG) uptake by 30, 92, and 95% in three experiments and increased surface GLUT-1 photolabeling by 17, 81, and 72%, respectively, with no increase in total cellular GLUT-1. T3 treatment for 48 h increased 2-DG uptake by 143, 172, and 216% in three experiments and increased cell surface GLUT-1 photolabeling by 88, 161, and 184%, respectively, with smaller increases in total cellular GLUT-1. T3 treatment for 48 h thus increased the fraction of cellular GLUT-1 at the plasma membrane from 21 +/- 2 to 35 +/- 3% (SE). We conclude that most of the early (6-h) stimulation of glucose transport by T3 in ARL 15 cells is mediated by an increase in the partitioning of GLUT-1 to the plasma membrane. With more chronic T3 treatment (48 h), the enhanced surface partitioning of GLUT-1 is persistent and is superimposed on an increase in total cellular GLUT-1, accounting for a further increase in glucose transport.

Stimulation of Glucose Transport by Hypoxia: Signals and Mechanisms

Physiology ◽  
1999 ◽  
Vol 14 (3) ◽  
pp. 105-110 ◽  
Author(s):  
Alireza Behrooz ◽  
Faramarz Ismail-Beigi
Keyword(s):  
Oxidative Phosphorylation ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Hypoxia Inducible Factor ◽  
Glut 1 ◽  
Hypoxia Inducible Factor 1 ◽  
Glut 4 ◽  
Per Se ◽  
Stimulation Of

Glucose transport is acutely stimulated by hypoxia through enhanced GLUT-1 and GLUT-4 glucose transporter function. GLUT-1 expression is also stimulated by hypoxia or azide. Moreover, hypoxia per se, acting through hypoxia-inducible factor 1, enhances GLUT-1 transcription. GLUT-1 is the first gene whose transcription is dually stimulated in response to hypoxia and inhibition of oxidative phosphorylation.

Stimulation of glucose transport by semicarbazide-sensitive amine oxidase activity in adipocytes from diabetic rats

2003 ◽  
Vol 59 (3) ◽  
pp. 153-160 ◽  
Author(s):  
A. Abella ◽  
L. Marti ◽  
C. Carpéné ◽  
M. Palacín ◽  
X. Testar ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Diabetic Rats ◽  
Amine Oxidase Activity ◽  
Stimulation Of
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