Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.
Identifieur interne : 001051 ( PubMed/Checkpoint ); précédent : 001050; suivant : 001052Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.
Auteurs : Sheila R. Costford [Canada] ; Nihan Kavaslar ; Nadav Ahituv ; Shehla N. Chaudhry ; Wendy S. Schackwitz ; Robert Dent ; Len A. Pennacchio ; Ruth Mcpherson ; Mary-Ellen HarperSource :
- PloS one [ 1932-6203 ] ; 2007.
English descriptors
- KwdEn :
- AMP-Activated Protein Kinases (genetics), AMP-Activated Protein Kinases (metabolism), Base Sequence, Blotting, Western, DNA Primers, Female, Glycogen (metabolism), Humans, Male, Muscle, Skeletal (metabolism), Mutation, Pedigree, Reverse Transcriptase Polymerase Chain Reaction, Triglycerides (metabolism).
- MESH :
- chemical , genetics : AMP-Activated Protein Kinases.
- chemical , metabolism : AMP-Activated Protein Kinases, Glycogen, Triglycerides.
- metabolism : Muscle, Skeletal.
- Base Sequence, Blotting, Western, DNA Primers, Female, Humans, Male, Mutation, Pedigree, Reverse Transcriptase Polymerase Chain Reaction.
Abstract
AMP-activated protein kinase (AMPK) is a heterotrimeric enzyme that is evolutionarily conserved from yeast to mammals and functions to maintain cellular and whole body energy homeostasis. Studies in experimental animals demonstrate that activation of AMPK in skeletal muscle protects against insulin resistance, type 2 diabetes and obesity. The regulatory gamma(3) subunit of AMPK is expressed exclusively in skeletal muscle; however, its importance in controlling overall AMPK activity is unknown. While evidence is emerging that gamma subunit mutations interfere specifically with AMP activation, there remains some controversy regarding the impact of gamma subunit mutations. Here we report the first gain-of-function mutation in the muscle-specific regulatory gamma(3) subunit in humans.
DOI: 10.1371/journal.pone.0000903
PubMed: 17878938
Affiliations:
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Links to Exploration step
pubmed:17878938Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.</title><author><name sortKey="Costford, Sheila R" sort="Costford, Sheila R" uniqKey="Costford S" first="Sheila R" last="Costford">Sheila R. Costford</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author><author><name sortKey="Kavaslar, Nihan" sort="Kavaslar, Nihan" uniqKey="Kavaslar N" first="Nihan" last="Kavaslar">Nihan Kavaslar</name></author><author><name sortKey="Ahituv, Nadav" sort="Ahituv, Nadav" uniqKey="Ahituv N" first="Nadav" last="Ahituv">Nadav Ahituv</name></author><author><name sortKey="Chaudhry, Shehla N" sort="Chaudhry, Shehla N" uniqKey="Chaudhry S" first="Shehla N" last="Chaudhry">Shehla N. Chaudhry</name></author><author><name sortKey="Schackwitz, Wendy S" sort="Schackwitz, Wendy S" uniqKey="Schackwitz W" first="Wendy S" last="Schackwitz">Wendy S. Schackwitz</name></author><author><name sortKey="Dent, Robert" sort="Dent, Robert" uniqKey="Dent R" first="Robert" last="Dent">Robert Dent</name></author><author><name sortKey="Pennacchio, Len A" sort="Pennacchio, Len A" uniqKey="Pennacchio L" first="Len A" last="Pennacchio">Len A. Pennacchio</name></author><author><name sortKey="Mcpherson, Ruth" sort="Mcpherson, Ruth" uniqKey="Mcpherson R" first="Ruth" last="Mcpherson">Ruth Mcpherson</name></author><author><name sortKey="Harper, Mary Ellen" sort="Harper, Mary Ellen" uniqKey="Harper M" first="Mary-Ellen" last="Harper">Mary-Ellen Harper</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17878938</idno><idno type="pmid">17878938</idno><idno type="doi">10.1371/journal.pone.0000903</idno><idno type="wicri:Area/PubMed/Corpus">001046</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001046</idno><idno type="wicri:Area/PubMed/Curation">001046</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001046</idno><idno type="wicri:Area/PubMed/Checkpoint">001046</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001046</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.</title><author><name sortKey="Costford, Sheila R" sort="Costford, Sheila R" uniqKey="Costford S" first="Sheila R" last="Costford">Sheila R. Costford</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author><author><name sortKey="Kavaslar, Nihan" sort="Kavaslar, Nihan" uniqKey="Kavaslar N" first="Nihan" last="Kavaslar">Nihan Kavaslar</name></author><author><name sortKey="Ahituv, Nadav" sort="Ahituv, Nadav" uniqKey="Ahituv N" first="Nadav" last="Ahituv">Nadav Ahituv</name></author><author><name sortKey="Chaudhry, Shehla N" sort="Chaudhry, Shehla N" uniqKey="Chaudhry S" first="Shehla N" last="Chaudhry">Shehla N. Chaudhry</name></author><author><name sortKey="Schackwitz, Wendy S" sort="Schackwitz, Wendy S" uniqKey="Schackwitz W" first="Wendy S" last="Schackwitz">Wendy S. Schackwitz</name></author><author><name sortKey="Dent, Robert" sort="Dent, Robert" uniqKey="Dent R" first="Robert" last="Dent">Robert Dent</name></author><author><name sortKey="Pennacchio, Len A" sort="Pennacchio, Len A" uniqKey="Pennacchio L" first="Len A" last="Pennacchio">Len A. Pennacchio</name></author><author><name sortKey="Mcpherson, Ruth" sort="Mcpherson, Ruth" uniqKey="Mcpherson R" first="Ruth" last="Mcpherson">Ruth Mcpherson</name></author><author><name sortKey="Harper, Mary Ellen" sort="Harper, Mary Ellen" uniqKey="Harper M" first="Mary-Ellen" last="Harper">Mary-Ellen Harper</name></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>AMP-Activated Protein Kinases (genetics)</term><term>AMP-Activated Protein Kinases (metabolism)</term><term>Base Sequence</term><term>Blotting, Western</term><term>DNA Primers</term><term>Female</term><term>Glycogen (metabolism)</term><term>Humans</term><term>Male</term><term>Muscle, Skeletal (metabolism)</term><term>Mutation</term><term>Pedigree</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Triglycerides (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>AMP-Activated Protein Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>AMP-Activated Protein Kinases</term><term>Glycogen</term><term>Triglycerides</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Muscle, Skeletal</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Blotting, Western</term><term>DNA Primers</term><term>Female</term><term>Humans</term><term>Male</term><term>Mutation</term><term>Pedigree</term><term>Reverse Transcriptase Polymerase Chain Reaction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">AMP-activated protein kinase (AMPK) is a heterotrimeric enzyme that is evolutionarily conserved from yeast to mammals and functions to maintain cellular and whole body energy homeostasis. Studies in experimental animals demonstrate that activation of AMPK in skeletal muscle protects against insulin resistance, type 2 diabetes and obesity. The regulatory gamma(3) subunit of AMPK is expressed exclusively in skeletal muscle; however, its importance in controlling overall AMPK activity is unknown. While evidence is emerging that gamma subunit mutations interfere specifically with AMP activation, there remains some controversy regarding the impact of gamma subunit mutations. Here we report the first gain-of-function mutation in the muscle-specific regulatory gamma(3) subunit in humans.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17878938</PMID><DateCreated><Year>2007</Year><Month>09</Month><Day>19</Day></DateCreated><DateCompleted><Year>2010</Year><Month>01</Month><Day>19</Day></DateCompleted><DateRevised><Year>2014</Year><Month>09</Month><Day>04</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>2</Volume><Issue>9</Issue><PubDate><Year>2007</Year><Month>Sep</Month><Day>19</Day></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.</ArticleTitle><Pagination><MedlinePgn>e903</MedlinePgn></Pagination><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">AMP-activated protein kinase (AMPK) is a heterotrimeric enzyme that is evolutionarily conserved from yeast to mammals and functions to maintain cellular and whole body energy homeostasis. Studies in experimental animals demonstrate that activation of AMPK in skeletal muscle protects against insulin resistance, type 2 diabetes and obesity. The regulatory gamma(3) subunit of AMPK is expressed exclusively in skeletal muscle; however, its importance in controlling overall AMPK activity is unknown. While evidence is emerging that gamma subunit mutations interfere specifically with AMP activation, there remains some controversy regarding the impact of gamma subunit mutations. Here we report the first gain-of-function mutation in the muscle-specific regulatory gamma(3) subunit in humans.</AbstractText><AbstractText Label="METHODS AND FINDINGS" NlmCategory="RESULTS">We sequenced the exons and splice junctions of the AMPK gamma(3) gene (PRKAG3) in 761 obese and 759 lean individuals, identifying 87 sequence variants including a novel R225W mutation in subjects from two unrelated families. The gamma(3) R225W mutation is homologous in location to the gamma(2)R302Q mutation in patients with Wolf-Parkinson-White syndrome and to the gamma(3)R225Q mutation originally linked to an increase in muscle glycogen content in purebred Hampshire Rendement Napole (RN-) pigs. We demonstrate in differentiated muscle satellite cells obtained from the vastus lateralis of R225W carriers that the mutation is associated with an approximate doubling of both basal and AMP-activated AMPK activities. Moreover, subjects bearing the R225W mutation exhibit a approximately 90% increase of skeletal muscle glycogen content and a approximately 30% decrease in intramuscular triglyceride (IMTG).</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">We have identified for the first time a mutation in the skeletal muscle-specific regulatory gamma(3) subunit of AMPK in humans. The gamma(3)R225W mutation has significant functional effects as demonstrated by increases in basal and AMP-activated AMPK activities, increased muscle glycogen and decreased IMTG. Overall, these findings are consistent with an important regulatory role for AMPK gamma(3) in human muscle energy metabolism.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Costford</LastName><ForeName>Sheila R</ForeName><Initials>SR</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kavaslar</LastName><ForeName>Nihan</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Ahituv</LastName><ForeName>Nadav</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Chaudhry</LastName><ForeName>Shehla N</ForeName><Initials>SN</Initials></Author><Author ValidYN="Y"><LastName>Schackwitz</LastName><ForeName>Wendy S</ForeName><Initials>WS</Initials></Author><Author ValidYN="Y"><LastName>Dent</LastName><ForeName>Robert</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Pennacchio</LastName><ForeName>Len A</ForeName><Initials>LA</Initials></Author><Author ValidYN="Y"><LastName>McPherson</LastName><ForeName>Ruth</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Harper</LastName><ForeName>Mary-Ellen</ForeName><Initials>ME</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>09</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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Version="1">11748095</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D055372" MajorTopicYN="N">AMP-Activated Protein Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006003" MajorTopicYN="N">Glycogen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018482" MajorTopicYN="N">Muscle, Skeletal</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="Y">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010375" MajorTopicYN="N">Pedigree</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014280" MajorTopicYN="N">Triglycerides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC1964808</OtherID><GeneralNote Owner="NLM">Original DateCompleted: 20071101</GeneralNote></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2007</Year><Month>07</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>08</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>9</Month><Day>20</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>9</Month><Day>20</Day><Hour>9</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>9</Month><Day>20</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17878938</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0000903</ArticleId><ArticleId IdType="pmc">PMC1964808</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Ahituv, Nadav" sort="Ahituv, Nadav" uniqKey="Ahituv N" first="Nadav" last="Ahituv">Nadav Ahituv</name><name sortKey="Chaudhry, Shehla N" sort="Chaudhry, Shehla N" uniqKey="Chaudhry S" first="Shehla N" last="Chaudhry">Shehla N. Chaudhry</name><name sortKey="Dent, Robert" sort="Dent, Robert" uniqKey="Dent R" first="Robert" last="Dent">Robert Dent</name><name sortKey="Harper, Mary Ellen" sort="Harper, Mary Ellen" uniqKey="Harper M" first="Mary-Ellen" last="Harper">Mary-Ellen Harper</name><name sortKey="Kavaslar, Nihan" sort="Kavaslar, Nihan" uniqKey="Kavaslar N" first="Nihan" last="Kavaslar">Nihan Kavaslar</name><name sortKey="Mcpherson, Ruth" sort="Mcpherson, Ruth" uniqKey="Mcpherson R" first="Ruth" last="Mcpherson">Ruth Mcpherson</name><name sortKey="Pennacchio, Len A" sort="Pennacchio, Len A" uniqKey="Pennacchio L" first="Len A" last="Pennacchio">Len A. Pennacchio</name><name sortKey="Schackwitz, Wendy S" sort="Schackwitz, Wendy S" uniqKey="Schackwitz W" first="Wendy S" last="Schackwitz">Wendy S. Schackwitz</name></noCountry><country name="Canada"><noRegion><name sortKey="Costford, Sheila R" sort="Costford, Sheila R" uniqKey="Costford S" first="Sheila R" last="Costford">Sheila R. 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