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Human disease-associated extracellular matrix orthologs ECM3 and QBRICK regulate primary mesenchymal cell migration in sea urchin embryos

Sea urchin embryos have been one of model organisms to investigate cellular behaviors because of their simple cell composition and transparent body. They also give us an opportunity to investigate molecular functions of human proteins of interest that are conserved in sea urchin. Here we report that...

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Autores principales: Kiyozumi, Daiji, Yaguchi, Shunsuke, Yaguchi, Junko, Yamazaki, Atsuko, Sekiguchi, Kiyotoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Japanese Association for Laboratory Animal Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8390315/
https://www.ncbi.nlm.nih.gov/pubmed/33828019
http://dx.doi.org/10.1538/expanim.21-0001
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author Kiyozumi, Daiji
Yaguchi, Shunsuke
Yaguchi, Junko
Yamazaki, Atsuko
Sekiguchi, Kiyotoshi
author_facet Kiyozumi, Daiji
Yaguchi, Shunsuke
Yaguchi, Junko
Yamazaki, Atsuko
Sekiguchi, Kiyotoshi
author_sort Kiyozumi, Daiji
collection PubMed
description Sea urchin embryos have been one of model organisms to investigate cellular behaviors because of their simple cell composition and transparent body. They also give us an opportunity to investigate molecular functions of human proteins of interest that are conserved in sea urchin. Here we report that human disease-associated extracellular matrix orthologues ECM3 and QBRICK are necessary for mesenchymal cell migration during sea urchin embryogenesis. Immunofluorescence has visualized the colocalization of QBRICK and ECM3 on both apical and basal surface of ectoderm. On the basal surface, QBRICK and ECM3 constitute together a mesh-like fibrillar structure along the blastocoel wall. When the expression of ECM3 was knocked down by antisense-morpholino oligonucleotides, the ECM3-QBRICK fibrillar structure completely disappeared. When QBRICK was knocked down, the ECM3 was still present, but the basally localized fibers became fragmented. The ingression and migration of primary mesenchymal cells were not critically affected, but their migration at later stages was severely affected in both knock-down embryos. As a consequence of impaired primary mesenchymal cell migration, improper spicule formation was observed. These results indicate that ECM3 and QBRICK are components of extracellular matrix, which play important role in primary mesenchymal cell migration, and that sea urchin is a useful experimental animal model to investigate human disease-associated extracellular matrix proteins.
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spelling pubmed-83903152021-08-31 Human disease-associated extracellular matrix orthologs ECM3 and QBRICK regulate primary mesenchymal cell migration in sea urchin embryos Kiyozumi, Daiji Yaguchi, Shunsuke Yaguchi, Junko Yamazaki, Atsuko Sekiguchi, Kiyotoshi Exp Anim Original Sea urchin embryos have been one of model organisms to investigate cellular behaviors because of their simple cell composition and transparent body. They also give us an opportunity to investigate molecular functions of human proteins of interest that are conserved in sea urchin. Here we report that human disease-associated extracellular matrix orthologues ECM3 and QBRICK are necessary for mesenchymal cell migration during sea urchin embryogenesis. Immunofluorescence has visualized the colocalization of QBRICK and ECM3 on both apical and basal surface of ectoderm. On the basal surface, QBRICK and ECM3 constitute together a mesh-like fibrillar structure along the blastocoel wall. When the expression of ECM3 was knocked down by antisense-morpholino oligonucleotides, the ECM3-QBRICK fibrillar structure completely disappeared. When QBRICK was knocked down, the ECM3 was still present, but the basally localized fibers became fragmented. The ingression and migration of primary mesenchymal cells were not critically affected, but their migration at later stages was severely affected in both knock-down embryos. As a consequence of impaired primary mesenchymal cell migration, improper spicule formation was observed. These results indicate that ECM3 and QBRICK are components of extracellular matrix, which play important role in primary mesenchymal cell migration, and that sea urchin is a useful experimental animal model to investigate human disease-associated extracellular matrix proteins. Japanese Association for Laboratory Animal Science 2021-04-06 2021 /pmc/articles/PMC8390315/ /pubmed/33828019 http://dx.doi.org/10.1538/expanim.21-0001 Text en ©2021 Japanese Association for Laboratory Animal Science https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial No Derivatives (by-nc-nd) License. (CC-BY-NC-ND 4.0: https://creativecommons.org/licenses/by-nc-nd/4.0/)
spellingShingle Original
Kiyozumi, Daiji
Yaguchi, Shunsuke
Yaguchi, Junko
Yamazaki, Atsuko
Sekiguchi, Kiyotoshi
Human disease-associated extracellular matrix orthologs ECM3 and QBRICK regulate primary mesenchymal cell migration in sea urchin embryos
title Human disease-associated extracellular matrix orthologs ECM3 and QBRICK regulate primary mesenchymal cell migration in sea urchin embryos
title_full Human disease-associated extracellular matrix orthologs ECM3 and QBRICK regulate primary mesenchymal cell migration in sea urchin embryos
title_fullStr Human disease-associated extracellular matrix orthologs ECM3 and QBRICK regulate primary mesenchymal cell migration in sea urchin embryos
title_full_unstemmed Human disease-associated extracellular matrix orthologs ECM3 and QBRICK regulate primary mesenchymal cell migration in sea urchin embryos
title_short Human disease-associated extracellular matrix orthologs ECM3 and QBRICK regulate primary mesenchymal cell migration in sea urchin embryos
title_sort human disease-associated extracellular matrix orthologs ecm3 and qbrick regulate primary mesenchymal cell migration in sea urchin embryos
topic Original
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8390315/
https://www.ncbi.nlm.nih.gov/pubmed/33828019
http://dx.doi.org/10.1538/expanim.21-0001
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