The role of nNOS and PGC-1α in skeletal muscle cells.
Identifieur interne : 000150 ( PubMed/Checkpoint ); précédent : 000149; suivant : 000151The role of nNOS and PGC-1α in skeletal muscle cells.
Auteurs : Sara Baldelli [Italie] ; Daniele Lettieri Barbato [Italie] ; Giuseppe Tatulli [Italie] ; Katia Aquilano [Italie] ; Maria Rosa Ciriolo [Italie]Source :
- Journal of cell science [ 1477-9137 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Humains, Muscles squelettiques (enzymologie), Muscles squelettiques (métabolisme), Nitric oxide synthase type I (génétique), Nitric oxide synthase type I (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Transduction du signal.
- MESH :
- enzymologie : Muscles squelettiques.
- génétique : Facteurs de transcription, Nitric oxide synthase type I, Protéines recombinantes.
- métabolisme : Facteurs de transcription, Muscles squelettiques, Nitric oxide synthase type I, Protéines recombinantes.
- Animaux, Humains, Transduction du signal.
English descriptors
- KwdEn :
- Animals, Humans, Muscle, Skeletal (enzymology), Muscle, Skeletal (metabolism), Nitric Oxide Synthase Type I (genetics), Nitric Oxide Synthase Type I (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Signal Transduction, Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : Nitric Oxide Synthase Type I, Recombinant Proteins, Transcription Factors.
- enzymology : Muscle, Skeletal.
- metabolism : Muscle, Skeletal, Nitric Oxide Synthase Type I, Recombinant Proteins, Transcription Factors.
- Animals, Humans, Signal Transduction.
Abstract
Neuronal nitric oxide synthase (nNOS) and peroxisome proliferator activated receptor γ co-activator 1α (PGC-1α) are two fundamental factors involved in the regulation of skeletal muscle cell metabolism. nNOS exists as several alternatively spliced variants, each having a specific pattern of subcellular localisation. Nitric oxide (NO) functions as a second messenger in signal transduction pathways that lead to the expression of metabolic genes involved in oxidative metabolism, vasodilatation and skeletal muscle contraction. PGC-1α is a transcriptional coactivator and represents a master regulator of mitochondrial biogenesis by promoting the transcription of mitochondrial genes. PGC-1α can be induced during physical exercise, and it plays a key role in coordinating the oxidation of intracellular fatty acids with mitochondrial remodelling. Several lines of evidence demonstrate that NO could act as a key regulator of PGC-1α expression; however, the link between nNOS and PGC-1α in skeletal muscle remains only poorly understood. In this Commentary, we review important metabolic pathways that are governed by nNOS and PGC-1α, and aim to highlight how they might intersect and cooperatively regulate skeletal muscle mitochondrial and lipid energetic metabolism and contraction.
DOI: 10.1242/jcs.154229
PubMed: 25217629
Affiliations:
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last="Lettieri Barbato">Daniele Lettieri Barbato</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biology, University of Rome 'Tor Vergata', Via della Ricerca Scientifica, 00133 Rome, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biology, University of Rome 'Tor Vergata', Via della Ricerca Scientifica, 00133 Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Tatulli, Giuseppe" sort="Tatulli, Giuseppe" uniqKey="Tatulli G" first="Giuseppe" last="Tatulli">Giuseppe Tatulli</name><affiliation wicri:level="3"><nlm:affiliation>Scientific Institute for Research, Hospitalization and Health Care, Università Telematica San Raffaele Roma, Via di Val Cannuta, 00167, Rome, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Scientific Institute for Research, Hospitalization and Health Care, Università Telematica San Raffaele Roma, Via di Val Cannuta, 00167, Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Aquilano, Katia" sort="Aquilano, Katia" uniqKey="Aquilano K" first="Katia" last="Aquilano">Katia Aquilano</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biology, University of Rome 'Tor Vergata', Via della Ricerca Scientifica, 00133 Rome, Italy katia.aquilano@uniroma2.it ciriolo@bio.uniroma2.it.</nlm:affiliation><country wicri:rule="url">Italie</country><wicri:regionArea>Department of Biology, University of Rome 'Tor Vergata', Via della Ricerca Scientifica, 00133 Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Ciriolo, Maria Rosa" sort="Ciriolo, Maria Rosa" uniqKey="Ciriolo M" first="Maria Rosa" last="Ciriolo">Maria Rosa Ciriolo</name><affiliation wicri:level="3"><nlm:affiliation>IRCCS San Raffaele 'La Pisana', Via di Val Cannuta, 00166, Rome, Italy katia.aquilano@uniroma2.it ciriolo@bio.uniroma2.it.</nlm:affiliation><country wicri:rule="url">Italie</country><wicri:regionArea>IRCCS San Raffaele 'La Pisana', Via di Val Cannuta, 00166, Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author></analytic><series><title level="j">Journal of cell science</title><idno type="eISSN">1477-9137</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Humans</term><term>Muscle, Skeletal (enzymology)</term><term>Muscle, Skeletal (metabolism)</term><term>Nitric Oxide Synthase Type I (genetics)</term><term>Nitric Oxide Synthase Type I (metabolism)</term><term>Recombinant Proteins 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squelettiques</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Muscle, Skeletal</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteurs de transcription</term><term>Nitric oxide synthase type I</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Muscle, Skeletal</term><term>Nitric Oxide Synthase Type I</term><term>Recombinant Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de transcription</term><term>Muscles squelettiques</term><term>Nitric oxide synthase type I</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Neuronal nitric oxide synthase (nNOS) and peroxisome proliferator activated receptor γ co-activator 1α (PGC-1α) are two fundamental factors involved in the regulation of skeletal muscle cell metabolism. nNOS exists as several alternatively spliced variants, each having a specific pattern of subcellular localisation. Nitric oxide (NO) functions as a second messenger in signal transduction pathways that lead to the expression of metabolic genes involved in oxidative metabolism, vasodilatation and skeletal muscle contraction. PGC-1α is a transcriptional coactivator and represents a master regulator of mitochondrial biogenesis by promoting the transcription of mitochondrial genes. PGC-1α can be induced during physical exercise, and it plays a key role in coordinating the oxidation of intracellular fatty acids with mitochondrial remodelling. Several lines of evidence demonstrate that NO could act as a key regulator of PGC-1α expression; however, the link between nNOS and PGC-1α in skeletal muscle remains only poorly understood. In this Commentary, we review important metabolic pathways that are governed by nNOS and PGC-1α, and aim to highlight how they might intersect and cooperatively regulate skeletal muscle mitochondrial and lipid energetic metabolism and contraction.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">25217629</PMID><DateCreated><Year>2014</Year><Month>11</Month><Day>15</Day></DateCreated><DateCompleted><Year>2015</Year><Month>11</Month><Day>04</Day></DateCompleted><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9137</ISSN><JournalIssue CitedMedium="Internet"><Volume>127</Volume><Issue>Pt 22</Issue><PubDate><Year>2014</Year><Month>Nov</Month><Day>15</Day></PubDate></JournalIssue><Title>Journal of cell science</Title><ISOAbbreviation>J. Cell. Sci.</ISOAbbreviation></Journal><ArticleTitle>The role of nNOS and PGC-1α in skeletal muscle cells.</ArticleTitle><Pagination><MedlinePgn>4813-20</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1242/jcs.154229</ELocationID><Abstract><AbstractText>Neuronal nitric oxide synthase (nNOS) and peroxisome proliferator activated receptor γ co-activator 1α (PGC-1α) are two fundamental factors involved in the regulation of skeletal muscle cell metabolism. nNOS exists as several alternatively spliced variants, each having a specific pattern of subcellular localisation. Nitric oxide (NO) functions as a second messenger in signal transduction pathways that lead to the expression of metabolic genes involved in oxidative metabolism, vasodilatation and skeletal muscle contraction. PGC-1α is a transcriptional coactivator and represents a master regulator of mitochondrial biogenesis by promoting the transcription of mitochondrial genes. PGC-1α can be induced during physical exercise, and it plays a key role in coordinating the oxidation of intracellular fatty acids with mitochondrial remodelling. Several lines of evidence demonstrate that NO could act as a key regulator of PGC-1α expression; however, the link between nNOS and PGC-1α in skeletal muscle remains only poorly understood. In this Commentary, we review important metabolic pathways that are governed by nNOS and PGC-1α, and aim to highlight how they might intersect and cooperatively regulate skeletal muscle mitochondrial and lipid energetic metabolism and contraction.</AbstractText><CopyrightInformation>© 2014. Published by The Company of Biologists Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Baldelli</LastName><ForeName>Sara</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Scientific Institute for Research, Hospitalization and Health Care, Università Telematica San Raffaele Roma, Via di Val Cannuta, 00167, Rome, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lettieri Barbato</LastName><ForeName>Daniele</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Rome 'Tor Vergata', Via della Ricerca Scientifica, 00133 Rome, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tatulli</LastName><ForeName>Giuseppe</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Scientific Institute for Research, Hospitalization and Health Care, Università Telematica San Raffaele Roma, Via di Val Cannuta, 00167, Rome, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aquilano</LastName><ForeName>Katia</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Rome 'Tor Vergata', Via della Ricerca Scientifica, 00133 Rome, Italy katia.aquilano@uniroma2.it ciriolo@bio.uniroma2.it.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ciriolo</LastName><ForeName>Maria Rosa</ForeName><Initials>MR</Initials><AffiliationInfo><Affiliation>IRCCS San Raffaele 'La Pisana', Via di Val Cannuta, 00166, Rome, Italy katia.aquilano@uniroma2.it ciriolo@bio.uniroma2.it.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>09</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Cell Sci</MedlineTA><NlmUniqueID>0052457</NlmUniqueID><ISSNLinking>0021-9533</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C486497">PPARGC1A protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.13.39</RegistryNumber><NameOfSubstance UI="C496320">NOS1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.13.39</RegistryNumber><NameOfSubstance UI="D052248">Nitric Oxide Synthase Type I</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D000818">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D006801">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D018482">Muscle, Skeletal</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D052248">Nitric Oxide Synthase Type I</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D011994">Recombinant Proteins</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName><QualifierName MajorTopicYN="N" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D015398">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D014157">Transcription Factors</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Lipid metabolism</Keyword><Keyword MajorTopicYN="N">Mitochondrial biogenesis</Keyword><Keyword MajorTopicYN="N">Mitochondrial metabolism</Keyword><Keyword MajorTopicYN="N">Nitric oxide</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="aheadofprint"><Year>2014</Year><Month>9</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>11</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25217629</ArticleId><ArticleId IdType="pii">jcs.154229</ArticleId><ArticleId IdType="doi">10.1242/jcs.154229</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country><region><li>Latium</li></region><settlement><li>Rome</li></settlement></list><tree><country name="Italie"><region name="Latium"><name sortKey="Baldelli, Sara" sort="Baldelli, Sara" uniqKey="Baldelli S" first="Sara" last="Baldelli">Sara Baldelli</name></region><name sortKey="Aquilano, Katia" sort="Aquilano, Katia" uniqKey="Aquilano K" first="Katia" last="Aquilano">Katia Aquilano</name><name sortKey="Ciriolo, Maria Rosa" sort="Ciriolo, Maria Rosa" uniqKey="Ciriolo M" first="Maria Rosa" last="Ciriolo">Maria Rosa Ciriolo</name><name sortKey="Lettieri Barbato, Daniele" sort="Lettieri Barbato, Daniele" uniqKey="Lettieri Barbato D" first="Daniele" last="Lettieri Barbato">Daniele Lettieri Barbato</name><name sortKey="Tatulli, Giuseppe" sort="Tatulli, Giuseppe" uniqKey="Tatulli G" first="Giuseppe" last="Tatulli">Giuseppe Tatulli</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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