Molecular regulation of high muscle mass in developing Blonde d'Aquitaine cattle foetuses.
Identifieur interne : 000782 ( PubMed/Checkpoint ); précédent : 000781; suivant : 000783Molecular regulation of high muscle mass in developing Blonde d'Aquitaine cattle foetuses.
Auteurs : Isabelle Cassar-Malek [France] ; Céline Boby [France] ; Brigitte Picard [France] ; Antonio Reverter [Australie] ; Nicholas J. Hudson [Australie]Source :
- Biology open [ 2046-6390 ] ; 2017.
Abstract
The Blonde d'Aquitaine (BA) is a French cattle breed with enhanced muscularity, partly attributable to a MSTN mutation. The BA m. Semitendinosus has a faster muscle fibre isoform phenotype comprising a higher proportion of fast type IIX fibres compared to age-matched Charolais (CH). To better understand the molecular network of modifications in BA compared to CH muscle, we assayed the transcriptomes of the m. Semitendinosus at 110, 180, 210 and 260 days postconception (dpc). We used a combination of differential expression (DE) and regulatory impact factors (RIF) to compare and contrast muscle gene expression between the breeds. Prominently developmentally regulated genes in both breeds reflected the replacement of embryonic myosin isoforms (MYL4, MYH3) with adult isoforms (MYH1) and the upregulation of mitochondrial metabolism (CKMT2, AGXT2L1) in preparation for birth. However, the transition to a fast, glycolytic muscle phenotype in the MSTN mutant BA is detectable through downregulation of various slow twitch subunits (TNNC1, MYH7, TPM3, CSRP3) beyond 210 dpc, and a small but consistent genome-wide reduction in mRNA encoding the mitoproteome. Across the breeds, NRIP2 is the regulatory gene possessing a network change most similar to that of MSTN.
DOI: 10.1242/bio.024950
PubMed: 28838967
Affiliations:
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Hudson</name><affiliation wicri:level="1"><nlm:affiliation>School of Agriculture and Food Sciences, University of Queensland, Brisbane 4075, Australia n.hudson@uq.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country><wicri:regionArea>School of Agriculture and Food Sciences, University of Queensland, Brisbane 4075</wicri:regionArea><wicri:noRegion>Brisbane 4075</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biology open</title><idno type="ISSN">2046-6390</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Blonde d'Aquitaine (BA) is a French cattle breed with enhanced muscularity, partly attributable to a MSTN mutation. The BA m. Semitendinosus has a faster muscle fibre isoform phenotype comprising a higher proportion of fast type IIX fibres compared to age-matched Charolais (CH). To better understand the molecular network of modifications in BA compared to CH muscle, we assayed the transcriptomes of the m. Semitendinosus at 110, 180, 210 and 260 days postconception (dpc). We used a combination of differential expression (DE) and regulatory impact factors (RIF) to compare and contrast muscle gene expression between the breeds. Prominently developmentally regulated genes in both breeds reflected the replacement of embryonic myosin isoforms (MYL4, MYH3) with adult isoforms (MYH1) and the upregulation of mitochondrial metabolism (CKMT2, AGXT2L1) in preparation for birth. However, the transition to a fast, glycolytic muscle phenotype in the MSTN mutant BA is detectable through downregulation of various slow twitch subunits (TNNC1, MYH7, TPM3, CSRP3) beyond 210 dpc, and a small but consistent genome-wide reduction in mRNA encoding the mitoproteome. Across the breeds, NRIP2 is the regulatory gene possessing a network change most similar to that of MSTN.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">28838967</PMID><DateCreated><Year>2017</Year><Month>08</Month><Day>25</Day></DateCreated><DateRevised><Year>2017</Year><Month>11</Month><Day>08</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2046-6390</ISSN><JournalIssue CitedMedium="Print"><Volume>6</Volume><Issue>10</Issue><PubDate><Year>2017</Year><Month>Oct</Month><Day>15</Day></PubDate></JournalIssue><Title>Biology open</Title><ISOAbbreviation>Biol Open</ISOAbbreviation></Journal><ArticleTitle>Molecular regulation of high muscle mass in developing Blonde d'Aquitaine cattle foetuses.</ArticleTitle><Pagination><MedlinePgn>1483-1492</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1242/bio.024950</ELocationID><Abstract><AbstractText>The Blonde d'Aquitaine (BA) is a French cattle breed with enhanced muscularity, partly attributable to a MSTN mutation. The BA m. Semitendinosus has a faster muscle fibre isoform phenotype comprising a higher proportion of fast type IIX fibres compared to age-matched Charolais (CH). To better understand the molecular network of modifications in BA compared to CH muscle, we assayed the transcriptomes of the m. Semitendinosus at 110, 180, 210 and 260 days postconception (dpc). We used a combination of differential expression (DE) and regulatory impact factors (RIF) to compare and contrast muscle gene expression between the breeds. Prominently developmentally regulated genes in both breeds reflected the replacement of embryonic myosin isoforms (MYL4, MYH3) with adult isoforms (MYH1) and the upregulation of mitochondrial metabolism (CKMT2, AGXT2L1) in preparation for birth. However, the transition to a fast, glycolytic muscle phenotype in the MSTN mutant BA is detectable through downregulation of various slow twitch subunits (TNNC1, MYH7, TPM3, CSRP3) beyond 210 dpc, and a small but consistent genome-wide reduction in mRNA encoding the mitoproteome. Across the breeds, NRIP2 is the regulatory gene possessing a network change most similar to that of MSTN.</AbstractText><CopyrightInformation>© 2017. Published by The Company of Biologists Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cassar-Malek</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>UMR1213 Herbivores, Institut National de la Recherche Agronomique, VetAgro Sup, 63122 Saint Genès Champanelle, Clermont-Ferrand F-63122, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boby</LastName><ForeName>Céline</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>UMR1213 Herbivores, Institut National de la Recherche Agronomique, VetAgro Sup, 63122 Saint Genès Champanelle, Clermont-Ferrand F-63122, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Picard</LastName><ForeName>Brigitte</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>UMR1213 Herbivores, Institut National de la Recherche Agronomique, VetAgro Sup, 63122 Saint Genès Champanelle, Clermont-Ferrand F-63122, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reverter</LastName><ForeName>Antonio</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Agriculture, Commonwealth Science and Industrial Research Organisation, Queensland Bioscience Precinct, St. Lucia, Brisbane 4075, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hudson</LastName><ForeName>Nicholas J</ForeName><Initials>NJ</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-3549-9396</Identifier><AffiliationInfo><Affiliation>School of Agriculture and Food Sciences, University of Queensland, Brisbane 4075, Australia n.hudson@uq.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate 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Version="1">23419240</PMID></CommentsCorrections></CommentsCorrectionsList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Genomics</Keyword><Keyword MajorTopicYN="N">Mitochondria</Keyword><Keyword MajorTopicYN="N">Myogenesis</Keyword><Keyword MajorTopicYN="N">Myostatin</Keyword><Keyword MajorTopicYN="N">Skeletal muscle</Keyword></KeywordList><CoiStatement>Competing interestsThe authors declare no competing or financial interests.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>8</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>8</Month><Day>26</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>8</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28838967</ArticleId><ArticleId IdType="pii">bio.024950</ArticleId><ArticleId IdType="doi">10.1242/bio.024950</ArticleId><ArticleId IdType="pmc">PMC5665461</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>France</li></country><region><li>Auvergne (région administrative)</li><li>Auvergne-Rhône-Alpes</li></region></list><tree><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Cassar Malek, Isabelle" sort="Cassar Malek, Isabelle" uniqKey="Cassar Malek I" first="Isabelle" last="Cassar-Malek">Isabelle Cassar-Malek</name></region><name sortKey="Boby, Celine" sort="Boby, Celine" uniqKey="Boby C" first="Céline" last="Boby">Céline Boby</name><name sortKey="Picard, Brigitte" sort="Picard, Brigitte" uniqKey="Picard B" first="Brigitte" last="Picard">Brigitte Picard</name></country><country name="Australie"><noRegion><name sortKey="Reverter, Antonio" sort="Reverter, Antonio" uniqKey="Reverter A" first="Antonio" last="Reverter">Antonio Reverter</name></noRegion><name sortKey="Hudson, Nicholas J" sort="Hudson, Nicholas J" uniqKey="Hudson N" first="Nicholas J" last="Hudson">Nicholas J. 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