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dc.contributor.authorGrau-Bové, Xavier-
dc.contributor.authorRuiz-Trillo, Iñaki-
dc.contributor.authorRodríguez Pascual, Fernando-
dc.date.accessioned2015-11-05T11:09:17Z-
dc.date.available2015-11-05T11:09:17Z-
dc.date.issued2015-05-29-
dc.identifierissn: 2045-2322-
dc.identifier.citationScientific Reports 5: 10568 (2015)-
dc.identifier.urihttp://hdl.handle.net/10261/124525-
dc.description.abstractLysyl oxidases (LOX) are copper-dependent enzymes that oxidize primary amine substrates to reactive aldehydes. The best-studied role of LOX enzymes is the remodeling of the extracellular matrix (ECM) in animals by cross-linking collagens and elastin, although intracellular functions have been reported as well. Five different LOX enzymes have been identified in mammals, LOX and LOX-like (LOXL) 1 to 4, showing a highly conserved catalytic carboxy terminal domain and more divergence in the rest of the sequence. Here we have surveyed a wide selection of genomes in order to infer the evolutionary history of LOX. We identified LOX proteins not only in animals, but also in many other eukaryotes, as well as in bacteria and archaea - which reveals a pre-metazoan origin for this gene family. LOX genes expanded during metazoan evolution resulting in two superfamilies, LOXL2/L3/L4 and LOX/L1/L5. Considering the current knowledge on the function of mammalian LOX isoforms in ECM remodeling, we propose that LOXL2/L3/L4 members might have preferentially been involved in making cross-linked collagen IV-based basement membrane, whereas the diversification of LOX/L1/L5 forms contributed to chordate/vertebrate-specific ECM innovations, such as elastin and fibronectin. Our work provides a novel view on the evolution of this family of enzymes.-
dc.description.sponsorshipThis work was supported by grants from Ministerio de Economía y Competitividad (MINECO; Plan Nacional de I+ D+ I: SAF2012-34916 to F.R-P., BFU2011-23434 to I.R.-T.); Comunidad Autónoma de Madrid (2010-BMD2321, FIBROTEAM Consortium to F.R-P.); Secretaria d’Universitats i Recerca del Departament d’Economia i Coneixement de la Generalitat de Catalunya (2014 SGR 619 to I.R.-T.) and European Research Council Starting Grant (ERC-2012-Co-616960 to I.R.-T.). X.G.-B. is supported by a pregraduate Formación del Personal Investigador grant from MINECO.-
dc.publisherNature Publishing Group-
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/616960-
dc.relation.isversionofPublisher's version-
dc.rightsopenAccess-
dc.titleOrigin and evolution of lysyl oxidases-
dc.typeartículo-
dc.identifier.doi10.1038/srep10568-
dc.relation.publisherversionhttp://doi.org/10.1038/srep10568-
dc.date.updated2015-11-05T11:09:17Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.rights.licensehttp://creativecommons.org/licenses/by/4.0/-
dc.contributor.funderEuropean Research Council-
dc.contributor.funderGeneralitat de Catalunya-
dc.contributor.funderComunidad de Madrid-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000781es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100002809es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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