Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development

Lysyl oxidase‐like 2 (LOXL2) and 3 (LOXL3) are members of the lysyl oxidase family of enzymes involved in the maturation of the extracellular matrix. Both enzymes share a highly conserved catalytic domain, but it is unclear whether they perform redundant functions in vivo. In this study, we show tha...

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Autores: Santamaria, Patricia G., Dubus, Pierre, Bustos tauler, José, Floristan, Alfredo, Morales, Saleta, Cano, Amparo, Vázquez Naharro, Alberto, Portillo Pérez, Francisco
Tipo de recurso: artículo
Fecha de publicación:2022
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/713851
Acceso en línea:http://hdl.handle.net/10486/713851
https://dx.doi.org/10.3390/ijms23105730
Access Level:acceso abierto
Palabra clave:embryonic lethality
epistasis analysis
Loxl2
Loxl3
lysyl oxidases
Medicina
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spelling Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse DevelopmentSantamaria, Patricia G.Dubus, PierreBustos tauler, JoséFloristan, AlfredoMorales, SaletaCano, AmparoVázquez Naharro, AlbertoPortillo Pérez, Franciscoembryonic lethalityepistasis analysisLoxl2Loxl3lysyl oxidasesMedicinaLysyl oxidase‐like 2 (LOXL2) and 3 (LOXL3) are members of the lysyl oxidase family of enzymes involved in the maturation of the extracellular matrix. Both enzymes share a highly conserved catalytic domain, but it is unclear whether they perform redundant functions in vivo. In this study, we show that mice lacking Loxl3 exhibit perinatal lethality and abnormal skeletal development. Additionally, analysis of the genotype of embryos carrying double knockout of Loxl2 and Loxl3 genes suggests that both enzymes have overlapping functions during mouse development. Furthermore, we also show that ubiquitous expression of Loxl2 suppresses the lethality associated with Loxl3 knockout miceThis research was funded by grants from the Spanish Ministry of Science and Innovation MCIN SAF2016-76504-R (to A.C. and F.P.), PID2019-111052RB-100 (to F.P.) and from the Spanish Institute of Health Carlos III CIBERONC CCB16/12/00295 (to A.C.), all of them partly supported from EU-FEDER funds, and Worldwide Cancer Research (16–0295 to A.C., F.P. and P.G.S.)Departamento de Bioquímica20222022-05-01research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10486/713851https://dx.doi.org/10.3390/ijms23105730reponame:Biblos-e Archivo. Repositorio Institucional de la UAMinstname:Universidad Autónoma de MadridInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repositorio.uam.es:10486/7138512026-06-23T12:46:27Z
dc.title.none.fl_str_mv Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
title Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
spellingShingle Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
Santamaria, Patricia G.
embryonic lethality
epistasis analysis
Loxl2
Loxl3
lysyl oxidases
Medicina
title_short Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
title_full Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
title_fullStr Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
title_full_unstemmed Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
title_sort Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
dc.creator.none.fl_str_mv Santamaria, Patricia G.
Dubus, Pierre
Bustos tauler, José
Floristan, Alfredo
Morales, Saleta
Cano, Amparo
Vázquez Naharro, Alberto
Portillo Pérez, Francisco
author Santamaria, Patricia G.
author_facet Santamaria, Patricia G.
Dubus, Pierre
Bustos tauler, José
Floristan, Alfredo
Morales, Saleta
Cano, Amparo
Vázquez Naharro, Alberto
Portillo Pérez, Francisco
author_role author
author2 Dubus, Pierre
Bustos tauler, José
Floristan, Alfredo
Morales, Saleta
Cano, Amparo
Vázquez Naharro, Alberto
Portillo Pérez, Francisco
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Departamento de Bioquímica
dc.subject.none.fl_str_mv embryonic lethality
epistasis analysis
Loxl2
Loxl3
lysyl oxidases
Medicina
topic embryonic lethality
epistasis analysis
Loxl2
Loxl3
lysyl oxidases
Medicina
description Lysyl oxidase‐like 2 (LOXL2) and 3 (LOXL3) are members of the lysyl oxidase family of enzymes involved in the maturation of the extracellular matrix. Both enzymes share a highly conserved catalytic domain, but it is unclear whether they perform redundant functions in vivo. In this study, we show that mice lacking Loxl3 exhibit perinatal lethality and abnormal skeletal development. Additionally, analysis of the genotype of embryos carrying double knockout of Loxl2 and Loxl3 genes suggests that both enzymes have overlapping functions during mouse development. Furthermore, we also show that ubiquitous expression of Loxl2 suppresses the lethality associated with Loxl3 knockout mice
publishDate 2022
dc.date.none.fl_str_mv 2022
2022-05-01
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10486/713851
https://dx.doi.org/10.3390/ijms23105730
url http://hdl.handle.net/10486/713851
https://dx.doi.org/10.3390/ijms23105730
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Biblos-e Archivo. Repositorio Institucional de la UAM
instname:Universidad Autónoma de Madrid
instname_str Universidad Autónoma de Madrid
reponame_str Biblos-e Archivo. Repositorio Institucional de la UAM
collection Biblos-e Archivo. Repositorio Institucional de la UAM
repository.name.fl_str_mv
repository.mail.fl_str_mv
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