AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle
D. Grahame Hardie 1 and Kei Sakamoto 2 1 Division of Molecular Physiology and 2 MRC Protein Phosphorylation Unit, University of Dundee, Dundee, Scotland d.g.hardie{at}dundee.ac.uk Contraction induces marked metabolic changes in muscle, and the AMP-activated protein kinase (AMPK) is a good candidate...
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| Veröffentlicht in: | Physiology (Bethesda, Md.) Md.), 2006-02, Vol.21 (1), p.48-60 |
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| container_title | Physiology (Bethesda, Md.) |
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| creator | Hardie, D. Grahame Sakamoto, Kei |
| description | D. Grahame Hardie 1 and
Kei Sakamoto 2
1 Division of Molecular Physiology and
2 MRC Protein Phosphorylation Unit, University of Dundee, Dundee, Scotland
d.g.hardie{at}dundee.ac.uk
Contraction induces marked metabolic changes in muscle, and the AMP-activated protein kinase (AMPK) is a good candidate to explain these effects. Recent work using a muscle-specific knockout of the upstream kinase, LKB1, has confirmed that the LKB1 AMPK cascade is the signaling pathway responsible for many of these effects. |
| doi_str_mv | 10.1152/physiol.00044.2005 |
| format | Article |
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Kei Sakamoto 2
1 Division of Molecular Physiology and
2 MRC Protein Phosphorylation Unit, University of Dundee, Dundee, Scotland
d.g.hardie{at}dundee.ac.uk
Contraction induces marked metabolic changes in muscle, and the AMP-activated protein kinase (AMPK) is a good candidate to explain these effects. Recent work using a muscle-specific knockout of the upstream kinase, LKB1, has confirmed that the LKB1 AMPK cascade is the signaling pathway responsible for many of these effects.</description><identifier>ISSN: 1548-9213</identifier><identifier>EISSN: 1548-9221</identifier><identifier>DOI: 10.1152/physiol.00044.2005</identifier><identifier>PMID: 16443822</identifier><language>eng</language><publisher>United States: Am Physiological Soc</publisher><subject>AMP-Activated Protein Kinase Kinases ; AMP-Activated Protein Kinases ; Animals ; Energy Metabolism ; Glucose - metabolism ; Glycogen - physiology ; Humans ; Mice ; Mice, Knockout ; Mice, Transgenic ; Multienzyme Complexes - genetics ; Multienzyme Complexes - physiology ; Muscle Contraction ; Muscle, Skeletal - enzymology ; Muscle, Skeletal - physiology ; Mutation ; Protein Serine-Threonine Kinases - genetics ; Protein Serine-Threonine Kinases - physiology ; Signal Transduction</subject><ispartof>Physiology (Bethesda, Md.), 2006-02, Vol.21 (1), p.48-60</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-9b75295223cd8e2ab6a675e39ec065dec678e3e7695ae9cf2977a5bc3c883a953</citedby><cites>FETCH-LOGICAL-c455t-9b75295223cd8e2ab6a675e39ec065dec678e3e7695ae9cf2977a5bc3c883a953</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3025,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16443822$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hardie, D. Grahame</creatorcontrib><creatorcontrib>Sakamoto, Kei</creatorcontrib><title>AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle</title><title>Physiology (Bethesda, Md.)</title><addtitle>Physiology (Bethesda)</addtitle><description>D. Grahame Hardie 1 and
Kei Sakamoto 2
1 Division of Molecular Physiology and
2 MRC Protein Phosphorylation Unit, University of Dundee, Dundee, Scotland
d.g.hardie{at}dundee.ac.uk
Contraction induces marked metabolic changes in muscle, and the AMP-activated protein kinase (AMPK) is a good candidate to explain these effects. Recent work using a muscle-specific knockout of the upstream kinase, LKB1, has confirmed that the LKB1 AMPK cascade is the signaling pathway responsible for many of these effects.</description><subject>AMP-Activated Protein Kinase Kinases</subject><subject>AMP-Activated Protein Kinases</subject><subject>Animals</subject><subject>Energy Metabolism</subject><subject>Glucose - metabolism</subject><subject>Glycogen - physiology</subject><subject>Humans</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mice, Transgenic</subject><subject>Multienzyme Complexes - genetics</subject><subject>Multienzyme Complexes - physiology</subject><subject>Muscle Contraction</subject><subject>Muscle, Skeletal - enzymology</subject><subject>Muscle, Skeletal - physiology</subject><subject>Mutation</subject><subject>Protein Serine-Threonine Kinases - genetics</subject><subject>Protein Serine-Threonine Kinases - physiology</subject><subject>Signal Transduction</subject><issn>1548-9213</issn><issn>1548-9221</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1PwjAYgBujEUT_gAfTk56G_Vi31QshBNQI0QQ8N6V7B9OyzXWL8u8dMj8unt7m7fM-hwehc0r6lAp2Xay3Ls1tnxDi-31GiDhAXSr8yJOM0cOfN-UddOLcCyFcRIIdow4NfJ9HjHXRYDh7erjBQ_wAWzyHzOUlzhM8qcFincV4nEG5an4qXdUOpxmev4KFSls8q52xcIqOEm0dnLWzh54n48Xozps-3t6PhlPP-EJUnlyGgknBGDdxBEwvAx2EArgEQwIRgwnCCDiEgRQapEmYDEMtloabKOJaCt5Dl3tvUeZvNbhKbVJnwFqdQV47FZKQc8lIA7I9aMrcuRISVZTpRpdbRYnaZVNtNvWVTe2yNUcXrb1ebiD-PWk7NcBgD6zT1fo9LeHbkq-2alJbu4CP6s8uz2yaAaOKKj9SRZw0hqv_DVlaONXS_BPxhY73</recordid><startdate>20060201</startdate><enddate>20060201</enddate><creator>Hardie, D. Grahame</creator><creator>Sakamoto, Kei</creator><general>Am Physiological Soc</general><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>20060201</creationdate><title>AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle</title><author>Hardie, D. Grahame ; Sakamoto, Kei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c455t-9b75295223cd8e2ab6a675e39ec065dec678e3e7695ae9cf2977a5bc3c883a953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>AMP-Activated Protein Kinase Kinases</topic><topic>AMP-Activated Protein Kinases</topic><topic>Animals</topic><topic>Energy Metabolism</topic><topic>Glucose - metabolism</topic><topic>Glycogen - physiology</topic><topic>Humans</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Mice, Transgenic</topic><topic>Multienzyme Complexes - genetics</topic><topic>Multienzyme Complexes - physiology</topic><topic>Muscle Contraction</topic><topic>Muscle, Skeletal - enzymology</topic><topic>Muscle, Skeletal - physiology</topic><topic>Mutation</topic><topic>Protein Serine-Threonine Kinases - genetics</topic><topic>Protein Serine-Threonine Kinases - physiology</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hardie, D. Grahame</creatorcontrib><creatorcontrib>Sakamoto, Kei</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Physiology (Bethesda, Md.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hardie, D. Grahame</au><au>Sakamoto, Kei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle</atitle><jtitle>Physiology (Bethesda, Md.)</jtitle><addtitle>Physiology (Bethesda)</addtitle><date>2006-02-01</date><risdate>2006</risdate><volume>21</volume><issue>1</issue><spage>48</spage><epage>60</epage><pages>48-60</pages><issn>1548-9213</issn><eissn>1548-9221</eissn><abstract>D. Grahame Hardie 1 and
Kei Sakamoto 2
1 Division of Molecular Physiology and
2 MRC Protein Phosphorylation Unit, University of Dundee, Dundee, Scotland
d.g.hardie{at}dundee.ac.uk
Contraction induces marked metabolic changes in muscle, and the AMP-activated protein kinase (AMPK) is a good candidate to explain these effects. Recent work using a muscle-specific knockout of the upstream kinase, LKB1, has confirmed that the LKB1 AMPK cascade is the signaling pathway responsible for many of these effects.</abstract><cop>United States</cop><pub>Am Physiological Soc</pub><pmid>16443822</pmid><doi>10.1152/physiol.00044.2005</doi><tpages>13</tpages></addata></record> |
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| ispartof | Physiology (Bethesda, Md.), 2006-02, Vol.21 (1), p.48-60 |
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| source | MEDLINE; American Physiological Society |
| subjects | AMP-Activated Protein Kinase Kinases AMP-Activated Protein Kinases Animals Energy Metabolism Glucose - metabolism Glycogen - physiology Humans Mice Mice, Knockout Mice, Transgenic Multienzyme Complexes - genetics Multienzyme Complexes - physiology Muscle Contraction Muscle, Skeletal - enzymology Muscle, Skeletal - physiology Mutation Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - physiology Signal Transduction |
| title | AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle |
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