Molecular-level characterization of elastin-like constructs and human aortic elastin.
Identifieur interne : 001C68 ( Ncbi/Merge ); précédent : 001C67; suivant : 001C69Molecular-level characterization of elastin-like constructs and human aortic elastin.
Auteurs : Andrea Heinz [Allemagne] ; Christoph U. Schr Der [Allemagne] ; Stéphanie Baud [France] ; Fred W. Keeley [Canada] ; Suzanne M. Mithieux [Australie] ; Anthony S. Weiss [Australie] ; Reinhard H H. Neubert [Allemagne] ; Christian E H. Schmelzer [Allemagne]Source :
- Matrix biology : journal of the International Society for Matrix Biology [ 1569-1802 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- Amino Acid Sequence, Aorta (chemistry), Cross-Linking Reagents (metabolism), Elastin (analysis), Humans, Microscopy, Electron, Scanning, Models, Molecular, Molecular Conformation, Molecular Dynamics Simulation, Molecular Sequence Data, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
- MESH :
- chemical , analysis : Elastin.
- chemical , metabolism : Cross-Linking Reagents.
- chemistry : Aorta.
- Amino Acid Sequence, Humans, Microscopy, Electron, Scanning, Models, Molecular, Molecular Conformation, Molecular Dynamics Simulation, Molecular Sequence Data, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
Abstract
This study aimed to characterize the structures of two elastin-like constructs, one composed of a cross-linked elastin-like polypeptide and the other one of cross-linked tropoelastin, and native aortic elastin. The structures of the insoluble materials and human aortic elastin were investigated using scanning electron microscopy. Additionally, all samples were digested with enzymes of different specificities, and the resultant peptide mixtures were characterized by ESI mass spectrometry and MALDI mass spectrometry. The MS(2) data was used to sequence linear peptides, and cross-linked species were analyzed with the recently developed software PolyLinX. This enabled the identification of two intramolecularly cross-linked peptides containing allysine aldols in the two constructs. The presence of the tetrafunctional cross-link desmosine was shown for all analyzed materials and its quantification revealed that the cross-linking degree of the two in vitro cross-linked materials was significantly lower than that of native elastin. Molecular dynamics simulations were performed, based on molecular species identified in the samples, to follow the formation of elastin cross-links. The results provide evidence for the significance of the GVGTP hinge region of domain 23 for the formation of elastin cross-links. Overall, this work provides important insight into structural similarities and differences between elastin-like constructs and native elastin. Furthermore, it represents a step toward the elucidation of the complex cross-linking pattern of mature elastin.
DOI: 10.1016/j.matbio.2014.07.006
PubMed: 25068896
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Keeley</name><affiliation wicri:level="1"><nlm:affiliation>Molecular Structure and Function, Hospital for Sick Children, Toronto, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Molecular Structure and Function, Hospital for Sick Children, Toronto</wicri:regionArea><wicri:noRegion>Toronto</wicri:noRegion></affiliation></author><author><name sortKey="Mithieux, Suzanne M" sort="Mithieux, Suzanne M" uniqKey="Mithieux S" first="Suzanne M" last="Mithieux">Suzanne M. Mithieux</name><affiliation wicri:level="4"><nlm:affiliation>School of Molecular Bioscience, University of Sydney, Sydney, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Molecular Bioscience, University of Sydney, Sydney</wicri:regionArea><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region><settlement type="city">Sydney</settlement></placeName><orgName type="university">Université de Sydney</orgName></affiliation></author><author><name sortKey="Weiss, Anthony S" sort="Weiss, Anthony S" uniqKey="Weiss A" first="Anthony S" last="Weiss">Anthony S. Weiss</name><affiliation wicri:level="4"><nlm:affiliation>School of Molecular Bioscience, University of Sydney, Sydney, Australia; Bosch Institute, University of Sydney, Sydney, Australia; Charles Perkins Centre, University of Sydney, Sydney, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Molecular Bioscience, University of Sydney, Sydney, Australia; Bosch Institute, University of Sydney, Sydney, Australia; Charles Perkins Centre, University of Sydney, Sydney</wicri:regionArea><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region><settlement type="city">Sydney</settlement></placeName><orgName type="university">Université de Sydney</orgName></affiliation></author><author><name sortKey="Neubert, Reinhard H H" sort="Neubert, Reinhard H H" uniqKey="Neubert R" first="Reinhard H H" last="Neubert">Reinhard H H. Neubert</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale)</wicri:regionArea><wicri:noRegion>Halle (Saale)</wicri:noRegion><wicri:noRegion>Halle (Saale)</wicri:noRegion><wicri:noRegion>Halle (Saale)</wicri:noRegion></affiliation></author><author><name sortKey="Schmelzer, Christian E H" sort="Schmelzer, Christian E H" uniqKey="Schmelzer C" first="Christian E H" last="Schmelzer">Christian E H. Schmelzer</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale)</wicri:regionArea><wicri:noRegion>Halle (Saale)</wicri:noRegion><wicri:noRegion>Halle (Saale)</wicri:noRegion><wicri:noRegion>Halle (Saale)</wicri:noRegion></affiliation></author></analytic><series><title level="j">Matrix biology : journal of the International Society for Matrix Biology</title><idno type="eISSN">1569-1802</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Aorta (chemistry)</term><term>Cross-Linking Reagents (metabolism)</term><term>Elastin (analysis)</term><term>Humans</term><term>Microscopy, Electron, Scanning</term><term>Models, Molecular</term><term>Molecular Conformation</term><term>Molecular Dynamics Simulation</term><term>Molecular Sequence Data</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aorte ()</term><term>Conformation moléculaire</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Microscopie électronique à balayage</term><term>Modèles moléculaires</term><term>Réactifs réticulants (métabolisme)</term><term>Simulation de dynamique moléculaire</term><term>Spectrométrie de masse MALDI</term><term>Séquence d'acides aminés</term><term>Élastine (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Elastin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cross-Linking Reagents</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Élastine</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Aorta</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Réactifs réticulants</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term><term>Microscopy, Electron, Scanning</term><term>Models, Molecular</term><term>Molecular Conformation</term><term>Molecular Dynamics Simulation</term><term>Molecular Sequence Data</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Aorte</term><term>Conformation moléculaire</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Microscopie électronique à balayage</term><term>Modèles moléculaires</term><term>Simulation de dynamique moléculaire</term><term>Spectrométrie de masse MALDI</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">This study aimed to characterize the structures of two elastin-like constructs, one composed of a cross-linked elastin-like polypeptide and the other one of cross-linked tropoelastin, and native aortic elastin. The structures of the insoluble materials and human aortic elastin were investigated using scanning electron microscopy. Additionally, all samples were digested with enzymes of different specificities, and the resultant peptide mixtures were characterized by ESI mass spectrometry and MALDI mass spectrometry. The MS(2) data was used to sequence linear peptides, and cross-linked species were analyzed with the recently developed software PolyLinX. This enabled the identification of two intramolecularly cross-linked peptides containing allysine aldols in the two constructs. The presence of the tetrafunctional cross-link desmosine was shown for all analyzed materials and its quantification revealed that the cross-linking degree of the two in vitro cross-linked materials was significantly lower than that of native elastin. Molecular dynamics simulations were performed, based on molecular species identified in the samples, to follow the formation of elastin cross-links. The results provide evidence for the significance of the GVGTP hinge region of domain 23 for the formation of elastin cross-links. Overall, this work provides important insight into structural similarities and differences between elastin-like constructs and native elastin. Furthermore, it represents a step toward the elucidation of the complex cross-linking pattern of mature elastin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25068896</PMID><DateCreated><Year>2014</Year><Month>10</Month><Day>04</Day></DateCreated><DateCompleted><Year>2015</Year><Month>06</Month><Day>08</Day></DateCompleted><DateRevised><Year>2014</Year><Month>10</Month><Day>04</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1569-1802</ISSN><JournalIssue CitedMedium="Internet"><Volume>38</Volume><PubDate><Year>2014</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Matrix biology : journal of the International Society for Matrix Biology</Title><ISOAbbreviation>Matrix Biol.</ISOAbbreviation></Journal><ArticleTitle>Molecular-level characterization of elastin-like constructs and human aortic elastin.</ArticleTitle><Pagination><MedlinePgn>12-21</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.matbio.2014.07.006</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0945-053X(14)00125-5</ELocationID><Abstract><AbstractText>This study aimed to characterize the structures of two elastin-like constructs, one composed of a cross-linked elastin-like polypeptide and the other one of cross-linked tropoelastin, and native aortic elastin. The structures of the insoluble materials and human aortic elastin were investigated using scanning electron microscopy. Additionally, all samples were digested with enzymes of different specificities, and the resultant peptide mixtures were characterized by ESI mass spectrometry and MALDI mass spectrometry. The MS(2) data was used to sequence linear peptides, and cross-linked species were analyzed with the recently developed software PolyLinX. This enabled the identification of two intramolecularly cross-linked peptides containing allysine aldols in the two constructs. The presence of the tetrafunctional cross-link desmosine was shown for all analyzed materials and its quantification revealed that the cross-linking degree of the two in vitro cross-linked materials was significantly lower than that of native elastin. Molecular dynamics simulations were performed, based on molecular species identified in the samples, to follow the formation of elastin cross-links. The results provide evidence for the significance of the GVGTP hinge region of domain 23 for the formation of elastin cross-links. Overall, this work provides important insight into structural similarities and differences between elastin-like constructs and native elastin. Furthermore, it represents a step toward the elucidation of the complex cross-linking pattern of mature elastin.</AbstractText><CopyrightInformation>Copyright © 2014. Published by Elsevier B.V.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Heinz</LastName><ForeName>Andrea</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany. Electronic address: andrea.heinz@pharmazie.uni-halle.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schräder</LastName><ForeName>Christoph U</ForeName><Initials>CU</Initials><AffiliationInfo><Affiliation>Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Baud</LastName><ForeName>Stéphanie</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Laboratoire SiRMa, FRE CNRS/URCA 3481, Université de Reims Champagne-Ardenne, Reims, France; Plateforme de Modélisation Moléculaire Multi-échelle, UFR Sciences Exactes et Naturelles, Université de Reims Champagne-Ardenne, Reims, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Keeley</LastName><ForeName>Fred W</ForeName><Initials>FW</Initials><AffiliationInfo><Affiliation>Molecular Structure and Function, Hospital for Sick Children, Toronto, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mithieux</LastName><ForeName>Suzanne M</ForeName><Initials>SM</Initials><AffiliationInfo><Affiliation>School of Molecular Bioscience, University of Sydney, Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Weiss</LastName><ForeName>Anthony S</ForeName><Initials>AS</Initials><AffiliationInfo><Affiliation>School of Molecular Bioscience, University of Sydney, Sydney, Australia; Bosch Institute, University of Sydney, Sydney, Australia; Charles Perkins Centre, University of Sydney, Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Neubert</LastName><ForeName>Reinhard H H</ForeName><Initials>RH</Initials><AffiliationInfo><Affiliation>Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schmelzer</LastName><ForeName>Christian E H</ForeName><Initials>CE</Initials><AffiliationInfo><Affiliation>Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.</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></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>07</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Matrix Biol</MedlineTA><NlmUniqueID>9432592</NlmUniqueID><ISSNLinking>0945-053X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003432">Cross-Linking Reagents</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-58-3</RegistryNumber><NameOfSubstance UI="D004549">Elastin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001011" MajorTopicYN="N">Aorta</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003432" MajorTopicYN="N">Cross-Linking Reagents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004549" MajorTopicYN="N">Elastin</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008855" MajorTopicYN="N">Microscopy, Electron, Scanning</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="Y">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008968" MajorTopicYN="N">Molecular Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D056004" MajorTopicYN="N">Molecular Dynamics Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019032" MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Allysine aldol</Keyword><Keyword MajorTopicYN="N">Cross-links</Keyword><Keyword MajorTopicYN="N">Desmosine</Keyword><Keyword MajorTopicYN="N">Mass spectrometry</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>07</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>07</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>07</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>7</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>7</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>6</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25068896</ArticleId><ArticleId IdType="pii">S0945-053X(14)00125-5</ArticleId><ArticleId IdType="doi">10.1016/j.matbio.2014.07.006</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li><li>Australie</li><li>Canada</li><li>France</li></country><region><li>Champagne-Ardenne</li><li>Grand Est</li><li>Nouvelle-Galles du Sud</li></region><settlement><li>Reims</li><li>Sydney</li></settlement><orgName><li>Université de Reims Champagne-Ardenne</li><li>Université de Sydney</li></orgName></list><tree><country name="Allemagne"><noRegion><name sortKey="Heinz, Andrea" sort="Heinz, Andrea" uniqKey="Heinz A" first="Andrea" last="Heinz">Andrea Heinz</name></noRegion><name sortKey="Neubert, Reinhard H H" sort="Neubert, Reinhard H H" uniqKey="Neubert R" first="Reinhard H H" last="Neubert">Reinhard H H. Neubert</name><name sortKey="Schmelzer, Christian E H" sort="Schmelzer, Christian E H" uniqKey="Schmelzer C" first="Christian E H" last="Schmelzer">Christian E H. Schmelzer</name><name sortKey="Schr Der, Christoph U" sort="Schr Der, Christoph U" uniqKey="Schr Der C" first="Christoph U" last="Schr Der">Christoph U. Schr Der</name></country><country name="France"><region name="Grand Est"><name sortKey="Baud, Stephanie" sort="Baud, Stephanie" uniqKey="Baud S" first="Stéphanie" last="Baud">Stéphanie Baud</name></region></country><country name="Canada"><noRegion><name sortKey="Keeley, Fred W" sort="Keeley, Fred W" uniqKey="Keeley F" first="Fred W" last="Keeley">Fred W. Keeley</name></noRegion></country><country name="Australie"><region name="Nouvelle-Galles du Sud"><name sortKey="Mithieux, Suzanne M" sort="Mithieux, Suzanne M" uniqKey="Mithieux S" first="Suzanne M" last="Mithieux">Suzanne M. 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