Disease relevance of 3-O-Methyl-d-glucose

• The rate of 3-O-methylglucose uptake by such cells was strongly dependent on the time taken for half the cells to undergo contracture, with low rates at low times to half contracture, and insulin-like rates at high times to half contracture [1].
• We investigated the acute effect of hyperglycemia on 3-O-methylglucose transport in isolated rat epitrochlearis muscles [2].
• The nonmetabolizable sugar, 3-O-methylglucose (3-O-MG), and 3-aminobenzamide, an inhibitor of the nuclear enzyme, polyADPribose synthetase, prevented STZ-associated damage to beta cells in islet cell cultures, but only 3-O-MG reduced CLZ-induced toxicity [3].
• C-peptide (600 pmol/l) increased 3-o-methylglucose transport 1.8 +/- 0.2-fold in skeletal muscle specimens from patients with insulin-dependent diabetes mellitus [4].
• Insulin treatment reverses the postreceptor defect in adipocyte 3-O-methylglucose transport in type II diabetes mellitus [5].

High impact information on 3-O-Methyl-d-glucose

• Uptake of 3-O-methylglucose by islet cells was less than 19% of controls [6].
• Accordingly, caffeine inhibited 3-O-methylglucose uptake during contractions only in oxidative muscle fibers that are characterized by a high sensitivity to insulin [7].
• Exposure of skin chamber granulation tissue vessels in nondiabetic rats to 11 or 15 mM D-glucose (but not L-glucose or 3-O-methylglucose) twice daily for 10 d induces vascular functional changes (increased albumin permeation and blood flow) identical to those in animals with mild or severe streptozotocin diabetes, respectively [8].
• The effects of fasting and refeeding on the glucose transport response to insulin in isolated rat adipose cells have been examined using 3-O-methylglucose transport in intact cells and cytochalasin B binding and Western blotting in subcellular membrane fractions [9].
• In contrast to insulin stimulation of 3-O-methylglucose and 2-deoxyglucose transport in muscle from normal, nonobese subjects, tissue from morbidly obese subjects, with or without NIDDM, were not responsive to insulin [10].

Chemical compound and disease context of 3-O-Methyl-d-glucose

• Glucose infusion into normal rats produced a similar decrease in 3-O-methylglucose transport constants suggesting that hyperglycemia was responsible for the early decrease in facilitated transport found in the diabetic rats [11].
• Deoxyglucose and 3-O-methylglucose transport in untreated and ATP-depleted Novikoff rat hepatoma cells. Analysis by a rapid kinetic technique, relationship to phosphorylation and effects of inhibitors [12].
• S-Trifluoracetonyl-coenzyme A and S-trifluoroacetonylmercaptoethanol form weak to moderately strong complexes with alpha-cyclodextrin and show little or no interaction with the methylglucose polysaccharide and lipopolysaccharides from Mycobacterium smegmatis [Smith, W. L., & Ballou, C. E. (1973) J. Biol. Chem. 248, 7118] [13].
• Mutants of Mycobacterium smegmatis were selected for resistance to ethionine in an effort to obtain methylation-defective strains that were altered in their ability to make methylmannose polysaccharides (MMP) or methylglucose lipopolysaccharides [14].
• Vehicle-treated control rats (CR) and rats that were injected with STZ (STZR) after pretreatment with 3-O-methylglucose (3-OMG), an agent that prevents STZ-induced hyperglycemia, were also studied [15].

Biological context of 3-O-Methyl-d-glucose

• Hagfish insulin was able to elicit the same maximal stimulation of both 3-o-methylglucose exchange and lipogenesis from glucose as pig insulin [16].
• Increased permeability to sugar following muscle contraction. Inhibitors of protein synthesis prevent reversal of the increase in 3-methylglucose transport rate [17].
• Stimulation of 3-O-methylglucose transport by anaerobiosis in rat thymocytes [18].
• Insulin stimulated glycogen synthase activity (approximately 1.7 fold), increased 3-o-methylglucose transport into human skeletal muscle strips (approximately 2 fold) and stimulated phosphorylation of the p42 ERK-2 isoform of MAP-kinase [19].
• Insulin binding and the effect of insulin on the transport of 3-O-methylglucose, lipogenesis from glucose, glucose oxidation and lipolysis was studied in fat cells of adrenalectomised rats and of a control group of sham-operated rats [20].

Anatomical context of 3-O-Methyl-d-glucose

• Photoaffinity labeling of both polypeptides in starved cell plasma membranes was inhibited by D-glucose, 3-O-methylglucose, 2-deoxyglucose, cytochalasin B, and cytochalasin A but not by D-sorbitol, L-glucose, or cytochalasin E [21].
• (iv) Mediated passive alpha-aminoisobutyric acid and 3-O-methylglucose transport were constituent oocyte membrane properties [22].
• Physical training (seven ESLC sessions/wk for 8 wk) increased whole body insulin-stimulated glucose uptake by 33+/-13%, concomitant with a 2.1-fold increase in insulin-stimulated (100 microU/ml) 3-O-methylglucose transport in isolated vastus lateralis muscle [23].
• We have previously described experimental conditions where basal methylglucose transport in adipocytes exhibited an apparent Km of approximately 35 mM [24].
• In skeletal muscle, insulin increased 3-O-methylglucose transport (1.88 +/- 0.21, 4.06 +/- 0.59, and 9.35 +/- 1.90 micromol x ml-1 x h-1, for 0, 0.6, and 12.0 nmol/l insulin, respectively) [25].

Associations of 3-O-Methyl-d-glucose with other chemical compounds

• Glucose or 3-O-methylglucose infused simultaneously with alloxan protected the alpha- and beta-cell, allowing subsequent glucose inhibition of glucagon secretion and stimulation of insulin release [26].
• Cadmium treatment decreased the apparent Km of 3T3-L1 fibroblasts for 3-O-methylglucose influx from approximately 28 to 9 mM and increased the apparent Vmax by 2-3-fold [27].
• The accumulation of both LHA4 and LHA2 mRNAs is induced by the addition of exogenous sugars and this induction appears to be dependent on sugar uptake and metabolism, because mannitol and 3-O-methylglucose do not stimulate mRNA accumulation [28].
• The uptake of sucrose, 3-O-methylglucose (3-O-MeG), and valine were studied in discs and in purified plasma membrane vesicles (PMV) prepared from sugar beet (Beta vulgaris L.) exporting leaves [29].
• Glucose appears to enter adipocytes on a single transport system whose maximum velocity is stimulated by insulin and which is competitively inhibited by cytochalasin B, 5-thioglucose, fructose, mannose and 3-O-methylglucose [30].

Gene context of 3-O-Methyl-d-glucose

• Predominant activation of IRS-2 was also observed in adult cardiomyocytes where HMR 1964 increased 3-O-methylglucose transport and the activation of Akt and glycogen synthase kinase-3 to the same extent as human insulin [31].
• This segregation of glucose uptake from GLUT4 translocation became more apparent when the two parameters were measured at 22 degrees C. Preincubation with the p38 MAPK inhibitors SB202190 and SB203580 reduced insulin-stimulated transport of either 2-deoxyglucose or 3-O-methylglucose by 40-60% [32].
• We investigated the effect of insulin-like growth factor II (IGF-II) and insulin-like growth factor binding protein-1 (IGFBP-1) on 3-O-methylglucose transport in incubated human skeletal muscle strips [33].
• GLUT1-HA-H6 confers GLUT1-specific sugar transport characteristics to transfected RE700A, including inhibition by cytochalasin B and high-affinity transport of the nonmetabolized sugar 3-O-methylglucose [34].
• Decreased transporter affinity for 2-DOG and 3-O-methylglucose was observed following IL-3 withdrawal [35].

Analytical, diagnostic and therapeutic context of 3-O-Methyl-d-glucose

• After electrical stimulation of diabetic hindquarters in the presence of insulin antiserum, insulin sensitivity of 3-O-methylglucose transport was increased to the same extent as in muscle from healthy rats stimulated in the presence of insulin at 50 microU/ml [36].
• The STZ-induced PLN response was sex independent and unaffected by prior subcutaneous injections of 3-O-methylglucose known to protect pancreatic beta-cells against STZ [37].
• Insulin caused a 15-20-fold stimulation of 3-O-methylglucose uptake and a 2-3-fold increase in the levels of GLUT-4 detected by immunoblotting of isolated plasma membranes; okadaic acid caused a 2-fold increase in 3-O-methylglucose uptake, and a 1.5-fold increase in plasma membrane GLUT-4 [38].
• In the cell culture experiments, a dose-dependent increase of FDG (up to 178%) and 3-O-methylglucose uptake (up to 305%) was demonstrated [39].
• The anomeric protons for all of the alpha 1----4-linked hexose units in the mycobacterial methylglucose polysaccharide occur in an envelope centered at delta 5.40, and, on titration with hexadecyltrimethylammonium bromide, the majority of these resonances move upfield to about delta 5.15 [40].

References