Comparison of GLUT1, GLUT3, and GLUT4 mRNA and the subcellular distribution of their proteins in normal human muscle
Basal, “insulin-independent” glucose uptake into skeletal muscle is provided by glucose transporters positioned at the plasma membrane. The relative amount of the three glucose transporters expressed in muscle has not been previously quantified. Using a combination of qualitative and quantitative ri...
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| Veröffentlicht in: | Metabolism, clinical and experimental clinical and experimental, 2000-12, Vol.49 (12), p.1604-1609 |
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| creator | Stuart, Charles A. Wen, Gary Gustafson, W.Clay Thompson, E.Aubrey |
| description | Basal, “insulin-independent” glucose uptake into skeletal muscle is provided by glucose transporters positioned at the plasma membrane. The relative amount of the three glucose transporters expressed in muscle has not been previously quantified. Using a combination of qualitative and quantitative ribonuclease protection assay (RPA) methods, we found in normal human muscle that GLUT1, GLUT3, and GLUT4 mRNA were expressed at 90 ± 10, 46 ± 4, and 156 ± 12 copies/ng RNA, respectively. Muscle was fractionated by DNase digestion and differential sedimentation into membrane fractions enriched in plasma membranes (PM) or low-density microsomes (LDM). GLUT1 and GLUT4 proteins were distributed 57% to 67% in LDM, whereas GLUT3 protein was at least 88% in the PM-enriched fractions. These data suggest that basal glucose uptake into resting human muscle could be provided in part by each of these three isoforms. |
| doi_str_mv | 10.1053/meta.2000.18559 |
| format | Article |
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The relative amount of the three glucose transporters expressed in muscle has not been previously quantified. Using a combination of qualitative and quantitative ribonuclease protection assay (RPA) methods, we found in normal human muscle that GLUT1, GLUT3, and GLUT4 mRNA were expressed at 90 ± 10, 46 ± 4, and 156 ± 12 copies/ng RNA, respectively. Muscle was fractionated by DNase digestion and differential sedimentation into membrane fractions enriched in plasma membranes (PM) or low-density microsomes (LDM). GLUT1 and GLUT4 proteins were distributed 57% to 67% in LDM, whereas GLUT3 protein was at least 88% in the PM-enriched fractions. 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Psychology ; Glucose Transporter Type 1 ; Glucose Transporter Type 2 ; Glucose Transporter Type 3 ; Humans ; Life Sciences (General) ; Male ; Membrane and intracellular transports ; Molecular and cellular biology ; Monosaccharide Transport Proteins - genetics ; Monosaccharide Transport Proteins - metabolism ; Muscle, Skeletal - metabolism ; Nerve Tissue Proteins ; Reference Values ; RNA, Messenger - metabolism ; Space life sciences ; Subcellular Fractions - metabolism</subject><ispartof>Metabolism, clinical and experimental, 2000-12, Vol.49 (12), p.1604-1609</ispartof><rights>2000</rights><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-c18f1e034b66fdb9d9c41c37d5e9498cf4f2f25bdbec75882cdb1beb80daa67d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1053/meta.2000.18559$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=829395$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11145124$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stuart, Charles A.</creatorcontrib><creatorcontrib>Wen, Gary</creatorcontrib><creatorcontrib>Gustafson, W.Clay</creatorcontrib><creatorcontrib>Thompson, E.Aubrey</creatorcontrib><title>Comparison of GLUT1, GLUT3, and GLUT4 mRNA and the subcellular distribution of their proteins in normal human muscle</title><title>Metabolism, clinical and experimental</title><addtitle>Metabolism</addtitle><description>Basal, “insulin-independent” glucose uptake into skeletal muscle is provided by glucose transporters positioned at the plasma membrane. The relative amount of the three glucose transporters expressed in muscle has not been previously quantified. Using a combination of qualitative and quantitative ribonuclease protection assay (RPA) methods, we found in normal human muscle that GLUT1, GLUT3, and GLUT4 mRNA were expressed at 90 ± 10, 46 ± 4, and 156 ± 12 copies/ng RNA, respectively. Muscle was fractionated by DNase digestion and differential sedimentation into membrane fractions enriched in plasma membranes (PM) or low-density microsomes (LDM). GLUT1 and GLUT4 proteins were distributed 57% to 67% in LDM, whereas GLUT3 protein was at least 88% in the PM-enriched fractions. These data suggest that basal glucose uptake into resting human muscle could be provided in part by each of these three isoforms.</description><subject>Adult</subject><subject>Biological and medical sciences</subject><subject>Cell physiology</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucose Transporter Type 1</subject><subject>Glucose Transporter Type 2</subject><subject>Glucose Transporter Type 3</subject><subject>Humans</subject><subject>Life Sciences (General)</subject><subject>Male</subject><subject>Membrane and intracellular transports</subject><subject>Molecular and cellular biology</subject><subject>Monosaccharide Transport Proteins - genetics</subject><subject>Monosaccharide Transport Proteins - metabolism</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Nerve Tissue Proteins</subject><subject>Reference Values</subject><subject>RNA, Messenger - metabolism</subject><subject>Space life sciences</subject><subject>Subcellular Fractions - metabolism</subject><issn>0026-0495</issn><issn>1532-8600</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>CYI</sourceid><sourceid>EIF</sourceid><recordid>eNp1kE2LFDEQhoMo7rh69iISEDxt7ybppDs5LoOuwqAgu-eQj2o20p0ek_SC_9709KAnT5WinlS9PAi9peSaEtHeTFDMNSOktlII9QztqGhZIztCnqMdIaxrCFfiAr3K-WfF-l52L9EFpZQLyvgOlf08HU0KeY54HvDd4eGeXp1Ke4VN9Kcnx9OPb7entjwCzot1MI7LaBL2IZcU7FLCtqDOQ8LHNBcIMeMQcZzTZEb8uEwm4mnJboTX6MVgxgxvzvUSPXz-dL__0hy-333d3x4a1ypWGkflQIG03Hbd4K3yynHq2t4LUFxJN_CBDUxYb8H1QkrmvKUWrCTemK737SX6uO2teX4tkIueQl6jmwjzknXPqgTJSQVvNtClOecEgz6mMJn0W1OiV9F6Fa1X0fokuv54f1692An8P_5stgIfzoDJzoxDMtGF_JeTTLVKVOrdRkWTjY4l5fUIJ5SyrqV1rLYxVEtPAZLOLkB04EMCV7Sfw38T_gFU7aIE</recordid><startdate>20001201</startdate><enddate>20001201</enddate><creator>Stuart, Charles A.</creator><creator>Wen, Gary</creator><creator>Gustafson, W.Clay</creator><creator>Thompson, E.Aubrey</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>CYE</scope><scope>CYI</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20001201</creationdate><title>Comparison of GLUT1, GLUT3, and GLUT4 mRNA and the subcellular distribution of their proteins in normal human muscle</title><author>Stuart, Charles A. ; Wen, Gary ; Gustafson, W.Clay ; Thompson, E.Aubrey</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-c18f1e034b66fdb9d9c41c37d5e9498cf4f2f25bdbec75882cdb1beb80daa67d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adult</topic><topic>Biological and medical sciences</topic><topic>Cell physiology</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. 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The relative amount of the three glucose transporters expressed in muscle has not been previously quantified. Using a combination of qualitative and quantitative ribonuclease protection assay (RPA) methods, we found in normal human muscle that GLUT1, GLUT3, and GLUT4 mRNA were expressed at 90 ± 10, 46 ± 4, and 156 ± 12 copies/ng RNA, respectively. Muscle was fractionated by DNase digestion and differential sedimentation into membrane fractions enriched in plasma membranes (PM) or low-density microsomes (LDM). GLUT1 and GLUT4 proteins were distributed 57% to 67% in LDM, whereas GLUT3 protein was at least 88% in the PM-enriched fractions. These data suggest that basal glucose uptake into resting human muscle could be provided in part by each of these three isoforms.</abstract><cop>Legacy CDMS</cop><pub>Elsevier Inc</pub><pmid>11145124</pmid><doi>10.1053/meta.2000.18559</doi><tpages>6</tpages></addata></record> |
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| ispartof | Metabolism, clinical and experimental, 2000-12, Vol.49 (12), p.1604-1609 |
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| source | MEDLINE; Elsevier ScienceDirect Journals; NASA Technical Reports Server |
| subjects | Adult Biological and medical sciences Cell physiology Female Fundamental and applied biological sciences. Psychology Glucose Transporter Type 1 Glucose Transporter Type 2 Glucose Transporter Type 3 Humans Life Sciences (General) Male Membrane and intracellular transports Molecular and cellular biology Monosaccharide Transport Proteins - genetics Monosaccharide Transport Proteins - metabolism Muscle, Skeletal - metabolism Nerve Tissue Proteins Reference Values RNA, Messenger - metabolism Space life sciences Subcellular Fractions - metabolism |
| title | Comparison of GLUT1, GLUT3, and GLUT4 mRNA and the subcellular distribution of their proteins in normal human muscle |
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