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Amyloid precursor protein-b facilitates cell adhesion during early development in zebrafish

Banote, RK; Chebli, J; Şatır, TM; Varshney, GK; Camacho, R; Ledin, J; Burgess, SM; ... Zetterberg, H; + view all (2020) Amyloid precursor protein-b facilitates cell adhesion during early development in zebrafish. Scientific Reports , 10 , Article 10127. 10.1038/s41598-020-66584-8. Green open access

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Abstract

Understanding the biological function of amyloid beta (Aβ) precursor protein (APP) beyond its role in Alzheimer’s disease is emerging. Yet, its function during embryonic development is poorly understood. The zebrafsh APP orthologue, Appb, is strongly expressed during early development but thus far has only been studied via morpholino-mediated knockdown. Zebrafsh enables analysis of cellular processes in an ontogenic context, which is limited in many other vertebrates. We characterized zebrafsh carrying a homozygous mutation that introduces a premature stop in exon 2 of the appb gene. We report that appb mutants are signifcantly smaller until 2 dpf and display perturbed enveloping layer (EVL) integrity and cell protrusions at the blastula stage. Moreover, appb mutants surviving beyond 48 hpf exhibited no behavioral defects at 6 dpf and developed into healthy and fertile adults. The expression of the app family member, appa, was also found to be altered in appb mutants. Taken together, we show that appb is involved in the initial development of zebrafsh by supporting the integrity of the EVL, likely by mediating cell adhesion properties. The loss of Appb might then be compensated for by other app family members to maintain normal development.

Type: Article
Title: Amyloid precursor protein-b facilitates cell adhesion during early development in zebrafish
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1038/s41598-020-66584-8
Publisher version: https://doi.org/10.1038/s41598-020-66584-8
Language: English
Additional information: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology > Neurodegenerative Diseases
URI: https://discovery.ucl.ac.uk/id/eprint/10103824
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