An ATX-LPA6-Gα13-ROCK axis shapes and maintains caudal vein plexus in zebrafish

Summary: Lysophosphatidic acid (LPA) is a potential regulator of vascular formation derived from blood. In this study, we utilized zebrafish as a model organism to monitor the blood vessel formation in detail. Zebrafish mutant of ATX, an LPA-producing enzyme, had a defect in the caudal vein plexus (...

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Autores principales: Ryohei Okasato, Kuniyuki Kano, Ryoji Kise, Asuka Inoue, Shigetomo Fukuhara, Junken Aoki
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Lenguaje:EN
Publicado: Elsevier 2021
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Acceso en línea:https://doaj.org/article/2cf2ab3e8a0a4343aebf61f02039d2ba
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spelling oai:doaj.org-article:2cf2ab3e8a0a4343aebf61f02039d2ba2021-11-20T05:08:54ZAn ATX-LPA6-Gα13-ROCK axis shapes and maintains caudal vein plexus in zebrafish2589-004210.1016/j.isci.2021.103254https://doaj.org/article/2cf2ab3e8a0a4343aebf61f02039d2ba2021-11-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2589004221012232https://doaj.org/toc/2589-0042Summary: Lysophosphatidic acid (LPA) is a potential regulator of vascular formation derived from blood. In this study, we utilized zebrafish as a model organism to monitor the blood vessel formation in detail. Zebrafish mutant of ATX, an LPA-producing enzyme, had a defect in the caudal vein plexus (CVP). Pharmacological inhibition of ATX resulted in a fusion of the delicate vessels in the CVP to form large sac-like vessels. Mutant embryos of LPA6 receptor and downstream Gα13 showed the same phenotype. Administration of OMPT, a stable LPA-analog, induced rapid CVP constriction, which was attenuated significantly in the LPA6 mutant. We also found that blood flow-induced CVP formation was dependent on ATX. The present study demonstrated that the ATX-LPA6 axis acts cooperatively with blood flow and contributes to the formation and maintenance of the CVP by generating contractive force in endothelial cells.Ryohei OkasatoKuniyuki KanoRyoji KiseAsuka InoueShigetomo FukuharaJunken AokiElsevierarticleCell biologyDevelopmental biologyScienceQENiScience, Vol 24, Iss 11, Pp 103254- (2021)
institution DOAJ
collection DOAJ
language EN
topic Cell biology
Developmental biology
Science
Q
spellingShingle Cell biology
Developmental biology
Science
Q
Ryohei Okasato
Kuniyuki Kano
Ryoji Kise
Asuka Inoue
Shigetomo Fukuhara
Junken Aoki
An ATX-LPA6-Gα13-ROCK axis shapes and maintains caudal vein plexus in zebrafish
description Summary: Lysophosphatidic acid (LPA) is a potential regulator of vascular formation derived from blood. In this study, we utilized zebrafish as a model organism to monitor the blood vessel formation in detail. Zebrafish mutant of ATX, an LPA-producing enzyme, had a defect in the caudal vein plexus (CVP). Pharmacological inhibition of ATX resulted in a fusion of the delicate vessels in the CVP to form large sac-like vessels. Mutant embryos of LPA6 receptor and downstream Gα13 showed the same phenotype. Administration of OMPT, a stable LPA-analog, induced rapid CVP constriction, which was attenuated significantly in the LPA6 mutant. We also found that blood flow-induced CVP formation was dependent on ATX. The present study demonstrated that the ATX-LPA6 axis acts cooperatively with blood flow and contributes to the formation and maintenance of the CVP by generating contractive force in endothelial cells.
format article
author Ryohei Okasato
Kuniyuki Kano
Ryoji Kise
Asuka Inoue
Shigetomo Fukuhara
Junken Aoki
author_facet Ryohei Okasato
Kuniyuki Kano
Ryoji Kise
Asuka Inoue
Shigetomo Fukuhara
Junken Aoki
author_sort Ryohei Okasato
title An ATX-LPA6-Gα13-ROCK axis shapes and maintains caudal vein plexus in zebrafish
title_short An ATX-LPA6-Gα13-ROCK axis shapes and maintains caudal vein plexus in zebrafish
title_full An ATX-LPA6-Gα13-ROCK axis shapes and maintains caudal vein plexus in zebrafish
title_fullStr An ATX-LPA6-Gα13-ROCK axis shapes and maintains caudal vein plexus in zebrafish
title_full_unstemmed An ATX-LPA6-Gα13-ROCK axis shapes and maintains caudal vein plexus in zebrafish
title_sort atx-lpa6-gα13-rock axis shapes and maintains caudal vein plexus in zebrafish
publisher Elsevier
publishDate 2021
url https://doaj.org/article/2cf2ab3e8a0a4343aebf61f02039d2ba
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