• Title/Summary/Keyword: GLUT

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The change GLUT-4 and muscle fiber type in Streptozotocin-diabetic rats (Streptozotocin 유발 당뇨백서에서의 골격근의 GLUT-4와 근섬유의 변화)

  • Heo, Myoung;Kim, Kye-Yoep;Oh, Myung-Hwa;Park, Seung-Kyu
    • Journal of the Korean Academy of Clinical Electrophysiology
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    • v.1 no.1
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    • pp.73-85
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    • 2003
  • The purpose of this study is to discuss and analyze the change of GLUT-4 and muscle fiber type of streptozotocin(STZ)-diabetic rats over a period of 6 weeks. We divided into four groups; I(aquatic exercise and feeding of Cordyceps militaris; n=6), test group II(feeding of Cordyceps miliaris; n=6), test group III(aquatic exercise; n=6), control group IV(non-treatment; n=6). After experimenting we measured the blood glucose, body weight, muscle fiber type and GLUT-4 protein content. The change of glucose levels decreased greater in group I than the other group. The body weight gain was lower in the all groups. The change femoris muscle fiber type, the size of muscle fiber TypeII lessened more than the one of Type I in group IV. Decrease of muscle fiber size more diminishment in group I than the other group. GLUT-4 protein quantity decrease in group IV compared to normal group. It was significantly increased in group. I, III compared to group IV. But there was more increase in group I (p<.001). These results suggest that GLUT-4 and muscle fiber type II decrease in STZ-diabetic rats and that when we apply aquatic exercise and feeding of Cordyceps militaris in diabetic rats over a period 6 weeks, it is increase GLUT-4 and the increase of insulin sensitivity of peripheral tissue. So it is considered to be helpful in improvement of glucose homeostasis and in prevent from muscle atrophy resulted from complication.

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Cloning and Distribution of Facilitative Glucose Transporter 2 (SLC2A2) in Pigs

  • Zuo, Jianjun;Huang, Zhiyi;Zhi, Aimin;Zou, Shigeng;Zhou, Xiangyan;Dai, Fawen;Ye, Hui;Feng, Dingyuan
    • Asian-Australasian Journal of Animal Sciences
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    • v.23 no.9
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    • pp.1159-1165
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    • 2010
  • Glucose is the main energy source for mammalian cells and its absorption is co-mediated by two different families of glucose transporters, sodium/glucose co-transporters (SGLTs) and facilitative glucose transporters (GLUTs). Here, we report the cloning and tissue distribution of porcine GLUT2. The GLUT2 was cloned by RACE and its cDNA was 2,051 bp long (GenBank accession no. EF140874). An AAATAA consensus sequence at nucleotide positions 1936-1941 was located upstream of the poly $(A)^+$ tail. Open reading frame analysis suggested that porcine GLUT2 contained 524 amino acids, with molecular weight of 57 kDa. The amino acid sequence of porcine GLUT2 was 87% and 79.4% identical with human and mouse GLUT2, respectively. GLUT2 mRNA was detected at highest level in porcine liver, at moderate levels in the small intestine and kidney, and at low levels in the brain, lung, muscle and heart. In the small intestine, the highest level was in the jejunum. In conclusion, the mRNA expression of GLUT2 was not only differentially regulated by age, but also differentially distributed along the small intestine of piglets, which may be related to availability of different intestinal luminal substrate concentrations resulting from different food sources and digestibility.

Compartmental Analysis of the Insulin-induced GLUT4 Recruitment in Adipocytes

  • Ryu, Ji-Won;Jung, Chan-Y.
    • BMB Reports
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    • v.34 no.4
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    • pp.285-292
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    • 2001
  • Insulin stimulates glucose uptake in muscle and adipose tissue and thus maintains normal blood glucose level in our body. Derangement of this process causes many grave health problems. Insulin stimulates glucose transport primarily by recruiting GLUT4 from its intracellular storage sites to the plasma membrane. The process is complex and involves GLUT4 trafficking through multiple subcellular compartments (organelles) and many protein functions, details of which are poorly understood. This review summarizes a recent development to isolate and characterize the individual intracellular GLUT4 compartments and to illustrate how this compartmental analysis will help to identify the insulin-sensitive step or steps in the insulin-induced GLUT4 recruitment in rat adipocytes. The review does not cover the recent exciting development in identification of many proteins implicated in this process.

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Effects of Gut Extract Protein and Insulin on Glucose Uptake and GLUT 1 Expression in HC 11 Mouse Mammary Epithelial Cells

  • Myung, K.H.;Ahn, B.J.
    • Asian-Australasian Journal of Animal Sciences
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    • v.15 no.8
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    • pp.1210-1214
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    • 2002
  • The large and rapid changes of glucose utilization in lactating mammary tissue in response to changes in nutritional state must be largely related by external signal of insulin. This also must be related with the quantity and composition of the diet in vivo. To characterize the mode of gut extract protein with insulin, in vitro experiment was conducted with HC11 cells. The gut extract protein has not only the same effect as insulin alone but also the synergistic effect with insulin in 2-Deoxy[3H] glucose uptake. Although the gut extract did not modulates glucose uptake via increasing the rate of translation of the GLUT1 protein, northern blot analysis indicated that the gut extract protein increased the expression of GLUT1 mRNA by a threefold and also there was a dose-dependent increase in the expression of GLUT1 mRNA. The gut extract protein is therefore shown to be capable of modulating glucose uptake by transcription level with insulin in HC 11 cells.

Studies on the Interaction of Glut4 and Cytoskeletal Protein (Glut4와 Cytoskeletal Protein의 상호작용에 관한 연구)

  • 김미영;이경림
    • Biomolecules & Therapeutics
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    • v.4 no.4
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    • pp.398-401
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    • 1996
  • The glucose transporters found in the plasma membrane of all animal cells are known to have 12 putative transmembrane domains. Among 7 cytoplasmic loops, the fourth loop is the largest one. Since previous studies showed that cofilin, an actin-modulating protein, was found to interact with the largest cytoplasmic loop of (Na, K)ATPase, we tested if cofilin interacts with the largest cytoplasmic loop of Glut4. We demonstrated by the two-hybrid system that the largest cytoplasmic loop of Glut4 did not show any interaction with cofilin, suggesting that cofilin is not required for the membrane targeting process of other membrane proteins but only for a P-type ATPase.

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Molecular Association of Glucose Transporter in the Plasma Membrane of Rat Adipocyte

  • Hah, Jong-Sik
    • The Korean Journal of Physiology
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    • v.25 no.2
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    • pp.115-123
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    • 1991
  • Molecular association of glucose transporters with the other proteins in the plasma membrane was assessed by gel electrophoresis and immunoblot techniques. Approximately $31.5{\pm}5.1%$ of GLUT-4, $64.8{\pm}2.7%$ of clathrin, 48.7% of total protein in the plasma membrane (PM) were found insoluble upon extraction with 1% Tx-100. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that the Tx-100 insoluble PM fraction contained about 4 major polypeptides with apparent molecular weight of above 200, 100-120, 80 and 30-35 KDa that were readily removed upon wash with a high pH buffer which is known to remove clathrin and 0.5 M Tris-buffer which is known to remove assembly proteins (AP). Immunoblotting of GLUT4 and clathrin against specific antibodies showed that GLUT-4 and clathrin were co-solubilized up to 84.6% and 82.7% respectively by wash with a high pH buffer and 1% Tx-100. When the membrane was pre-washed with a high pH buffer and 0.5 M Tris solution, GLUT4 and clathrin were not solubilized further suggesting that GLUT4 molecules are in molecular association with clathrin, AP and/or other extrinsic membrane proteins in plasma membrane and the formation of clathrin-coated structures might be involved in insulin stimulated glucose transporter translocation mechanism.

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Effect of Ganglioside $G_{M3}$ on the Erythrocyte Glucose Transporter (GLUT1): Conformational Changes Measured by Steady-State and Time-Resolved Fluorescence Spectroscopy

  • Yoon, Hae-Jung;Lee, Min-Yung;Jhon, GiI-Ja
    • BMB Reports
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    • v.30 no.4
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    • pp.240-245
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    • 1997
  • Interactions between ganglioside $G_{M3}$ and glucose transporter, GLUT1 were studied by measuring the effect of $G_{M3}$ on steady-state and time-resolved fluorescence of purified GLUT1 in synthetic lipids and on the 3-O-methylglucose uptake by human erythrocytes. The intrinsic tryptophan fluorescence showed a GLUT 1 emission maximum of 335 nm, and increased in the presence of $G_{M3}$ by 12% without shifting the emission maximum, The fluorescence lifetimes of intrinsic tryptophan on GLUT1 consisted of a long component of 7.8 ns and a short component of 2,3 ns and $G_{M3}$ increased both lifetime components. Lifetime components were quenched by acrylamide and KI. Acrylarnide-mduced quenching of long-lifetime components was partly recovered by $G_{M3}$ However. KI-induccd quenching of short- and long-lifetime components was not rescued by $G_{M3}$. The anisotropy of 1.6-diphenyl-1.3.5-hexatriene (DPH)-probed dimyristoylphosphatidylcholine (DMPC) model membrane was also increased with $G_{M3}$ incorporation, The transport rate of 3-O-methylglucose increased by 20% with $G_{M3}$ incorporation on the erythrocytes, Therefore, $G_{M3}$ altered the environment of lipid membrane and induced the conformational change of GLUT1.

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Effects of Antidiabetic and GLUT4 gene Expression of Acanthopanax senticosus Extracts (가시오가피 추출물의 항당뇨 활성 및 GLUT4 유전자 발현에 미치는 영향)

  • Choung, Eui-Su;Park, Jong-Phil;Choi, Han;Jang, Gyeong-Sun;Kang, Shin-Ho;Kang, Se-Chan;Zee, Ok-Pyo
    • Korean Journal of Pharmacognosy
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    • v.39 no.3
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    • pp.228-232
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    • 2008
  • Antidiabetic effects of an aqueous and solvent extract prepared from the root, stem and fruit parts of Acanthopanax senticosus, were investigated in experimental Streptozotocin (STZ)-induced diabetic rats model. The n-butanol and water extracts of A. senticosus were orally administrated once a day for 6 days. The n-butanol extracts of fruit (FB) showed highest efficiency than other groups (water extracts of stem, root and fruit; butanol extracts of stem, root) on serum glucose values in the STZ-induced diabetic rats. We have studied gene expression of glucose transporter genes in C2C12 skeletal muscle cell line during differentiation treated by the n-butanol and water extracts of A. senticosus, SW, RW, FW, SB, RB and FB. The GLUT4 gene was high expressed by FB treatment. These findings suggest that FB of A. senticosus have GLUT4 gene expression activity for glucose homeostasis and may have beneficial effects on blood glucose lowering in the diabetic patients.

Mechanisms of Glucose Uptake in Cancer Tissue (악성종양의 포도당 섭취 기전)

  • Chung, June-Key
    • The Korean Journal of Nuclear Medicine
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    • v.33 no.1
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    • pp.1-10
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    • 1999
  • Cancer cells are known to show increased rates of glycolysis metabolism. Based on this, PET studies using F-18-fluorodeoxyglucose have been used for the detection of primary and metastatic tumors. To account for this increased glucose uptake, a variety of mechanisms has been proposed. Glucose influx across the cell membrane is mediated by a family of structurally related proteins known as glucose transporters (Gluts). Among 6 isoforms of Gluts, Glut-1 and/or Glut-3 have been reported to show increased expression in various tumors. Increased level of Glut mRNA transcription is supposed to be the basic mechanism of Glut overexpression at the protein level. Some oncogens such as src or ras intensely stimulate Glut-1 by means of increased Glut-1 mRNA levels. Hexokinase activity is another important factor in glucose uptake in cancer cells. Especially hexokinase type II is considered to be involved in glycolysis of cancer cells. Much of the hexokinase of tumor cells is bound to outer membrane of mitochondria by the porin, a hexokinase receptor. Through this interaction, hexokinase may gain preferred access to ATP synthesized via oxidative phosphorylation in the inner mitochondria compartment. Other biologic factors such as tumor blood flow, blood volume, hypoxia, and infiltrating cells in tumor tissue are involved. Relative hypoxia may activate the anaerobic glycotytic pathway. Surrounding macrophages and newly formed granulation tissue in tumor showed greater glucose uptake than did viable cancer cells. To expand the application of FDG PET in oncology, it is important for nuclear medicine physicians to understand the related mechanisms of glucose uptake in cancer tissue.

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Nutritional Regulation of GLUT Expression, Glucose Metabolism, and Intramuscular Fat Content in Porcine Muscle

  • Katsumata, M.;Kaji, Y.;Takada, R.;Dauncey, M.J.
    • Asian-Australasian Journal of Animal Sciences
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    • v.20 no.8
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    • pp.1297-1304
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    • 2007
  • We conducted a series of investigations in order to elucidate role of nutritional status in regulating GLUT expression and energy metabolism in porcine muscle. Firstly, the role of mild undernutrition in regulating muscle GLUT gene expression and function was studied in growing pigs (3 wk of age) on a high (H) or low (L) food intake (H = 2L) at $35^{\circ}C$ or $26^{\circ}C$. Low food intake selectively upregulates GLUT1 and GLUT4 gene expression; mRNA levels were elevated in longissimus dorsi (L. dorsi) and rhomboideus muscles but not in diaphragm or cardiac muscles. Our next step was to determine whether dietary lysine, a major primary limiting amino acid in diets for pigs, affects muscle GLUT4 expression. Pigs of 6 wk of age were pair-fed a control or low lysine (LL) diet. The control diet contained optimal amounts of all essential amino acids, including 1.15% lysine. The LL diet was similar but contained only 0.70% lysine. GLUT4 mRNA expression was upregulated by the LL diet in L. dorsi and rhomboideus muscles, whereas that in cardiac muscle was unaffected. GLUT4 protein abundance was also higher in rhomboideus muscle of animals on the LL diet. We conducted another investigation in order to elucidate effects of the LL diet on post-GLUT4 glucose metabolism. Activity of hexokinase was unaffected by dietary lysine levels while that of citrate synthase was higher both in L. dorsi and rhomboideus muscles of pigs fed on the LL diet. Glucose 6-phosphate content was higher in L. dorsi msucle in the LL group. Glycogen content was higher both in L. dorsi and rhomboideus muscles in the LL group. Further, we determined the effects of dietary lysine levels on accumulation of intramuscular fat (IMF) in L. dorsi muscle of finishing pigs. A low lysine diet (lysine content was 0.40%) meeting approximately 70% of the requirement of lysine was given to finishing pigs for two months. IMF contents in L. dorsi of the pigs given the low lysine diet were twice higher than those of the pigs fed on a control diet (lysine content was 0.65%). Finally, we proved that a well known effect of breadcrumbs feeding to enhance IMF of finishing pigs could be attributed to shortage of amino acids in diets including breadcrumbs.