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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 principales: Santamaría, Patricia G., Dubus, Pierre, Bustos-Tauler, José, Floristán, Alfredo, Vázquez-Naharro, Alberto, Morales, Saleta, Cano, Amparo, Portillo, Francisco
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9144032/
https://www.ncbi.nlm.nih.gov/pubmed/35628534
http://dx.doi.org/10.3390/ijms23105730
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author Santamaría, Patricia G.
Dubus, Pierre
Bustos-Tauler, José
Floristán, Alfredo
Vázquez-Naharro, Alberto
Morales, Saleta
Cano, Amparo
Portillo, Francisco
author_facet Santamaría, Patricia G.
Dubus, Pierre
Bustos-Tauler, José
Floristán, Alfredo
Vázquez-Naharro, Alberto
Morales, Saleta
Cano, Amparo
Portillo, Francisco
author_sort Santamaría, Patricia G.
collection PubMed
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.
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spelling pubmed-91440322022-05-29 Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development Santamaría, Patricia G. Dubus, Pierre Bustos-Tauler, José Floristán, Alfredo Vázquez-Naharro, Alberto Morales, Saleta Cano, Amparo Portillo, Francisco Int J Mol Sci Article 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. MDPI 2022-05-20 /pmc/articles/PMC9144032/ /pubmed/35628534 http://dx.doi.org/10.3390/ijms23105730 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Santamaría, Patricia G.
Dubus, Pierre
Bustos-Tauler, José
Floristán, Alfredo
Vázquez-Naharro, Alberto
Morales, Saleta
Cano, Amparo
Portillo, Francisco
Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
title 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_short Loxl2 and Loxl3 Paralogues Play Redundant Roles during Mouse Development
title_sort loxl2 and loxl3 paralogues play redundant roles during mouse development
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9144032/
https://www.ncbi.nlm.nih.gov/pubmed/35628534
http://dx.doi.org/10.3390/ijms23105730
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