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Identification of multiple integrin β1 homologs in zebrafish (Danio rerio)

BACKGROUND: Integrins comprise a large family of α,β heterodimeric, transmembrane cell adhesion receptors that mediate diverse essential biological functions. Higher vertebrates possess a single β1 gene, and the β1 subunit associates with a large number of α subunits to form the major class of extra...

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Autores principales: Mould, A Paul, McLeish, Jennifer A, Huxley-Jones, Julie, Goonesinghe, Alexander C, Hurlstone, Adam FL, Boot-Handford, Raymond P, Humphries, Martin J
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1538996/
https://www.ncbi.nlm.nih.gov/pubmed/16787535
http://dx.doi.org/10.1186/1471-2121-7-24
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author Mould, A Paul
McLeish, Jennifer A
Huxley-Jones, Julie
Goonesinghe, Alexander C
Hurlstone, Adam FL
Boot-Handford, Raymond P
Humphries, Martin J
author_facet Mould, A Paul
McLeish, Jennifer A
Huxley-Jones, Julie
Goonesinghe, Alexander C
Hurlstone, Adam FL
Boot-Handford, Raymond P
Humphries, Martin J
author_sort Mould, A Paul
collection PubMed
description BACKGROUND: Integrins comprise a large family of α,β heterodimeric, transmembrane cell adhesion receptors that mediate diverse essential biological functions. Higher vertebrates possess a single β1 gene, and the β1 subunit associates with a large number of α subunits to form the major class of extracellular matrix (ECM) receptors. Despite the fact that the zebrafish (Danio rerio) is a rapidly emerging model organism of choice for developmental biology and for models of human disease, little is currently known about β1 integrin sequences and functions in this organism. RESULTS: Using RT-PCR, complete coding sequences of zebrafish β1 paralogs were obtained from zebrafish embryos or adult tissues. The results show that zebrafish possess two β1 paralogs (β1–1 and β1–2) that have a high degree of identity to other vertebrate β1 subunits. In addition, a third, more divergent, β1 paralog is present (β1–3), which may have altered ligand-binding properties. Zebrafish also have other divergent β1-like transcripts, which are C-terminally truncated forms lacking the transmembrane and cytoplasmic domains. Together with β1–3 these truncated forms comprise a novel group of β1 paralogs, all of which have a mutation in the ADMIDAS cation-binding site. Phylogenetic and genomic analyses indicate that the duplication that gave rise to β1–1 and β1–2 occurred after the divergence of the tetrapod and fish lineages, while a subsequent duplication of the ancestor of β1–2 may have given rise to β1–3 and an ancestral truncated paralog. A very recent tandem duplication of the truncated β1 paralogs appears to have taken place. The different zebrafish β1 paralogs have varied patterns of temporal expression during development. β1–1 and β1–2 are ubiquitously expressed in adult tissues, whereas the other β1 paralogs generally show more restricted patterns of expression. CONCLUSION: Zebrafish have a large set of integrin β1 paralogs. β1–1 and β1–2 may share the roles of the solitary β1 subunit found in other vertebrates, whereas β1–3 and the truncated β1 paralogs may have acquired novel functions.
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spelling pubmed-15389962006-08-11 Identification of multiple integrin β1 homologs in zebrafish (Danio rerio) Mould, A Paul McLeish, Jennifer A Huxley-Jones, Julie Goonesinghe, Alexander C Hurlstone, Adam FL Boot-Handford, Raymond P Humphries, Martin J BMC Cell Biol Research Article BACKGROUND: Integrins comprise a large family of α,β heterodimeric, transmembrane cell adhesion receptors that mediate diverse essential biological functions. Higher vertebrates possess a single β1 gene, and the β1 subunit associates with a large number of α subunits to form the major class of extracellular matrix (ECM) receptors. Despite the fact that the zebrafish (Danio rerio) is a rapidly emerging model organism of choice for developmental biology and for models of human disease, little is currently known about β1 integrin sequences and functions in this organism. RESULTS: Using RT-PCR, complete coding sequences of zebrafish β1 paralogs were obtained from zebrafish embryos or adult tissues. The results show that zebrafish possess two β1 paralogs (β1–1 and β1–2) that have a high degree of identity to other vertebrate β1 subunits. In addition, a third, more divergent, β1 paralog is present (β1–3), which may have altered ligand-binding properties. Zebrafish also have other divergent β1-like transcripts, which are C-terminally truncated forms lacking the transmembrane and cytoplasmic domains. Together with β1–3 these truncated forms comprise a novel group of β1 paralogs, all of which have a mutation in the ADMIDAS cation-binding site. Phylogenetic and genomic analyses indicate that the duplication that gave rise to β1–1 and β1–2 occurred after the divergence of the tetrapod and fish lineages, while a subsequent duplication of the ancestor of β1–2 may have given rise to β1–3 and an ancestral truncated paralog. A very recent tandem duplication of the truncated β1 paralogs appears to have taken place. The different zebrafish β1 paralogs have varied patterns of temporal expression during development. β1–1 and β1–2 are ubiquitously expressed in adult tissues, whereas the other β1 paralogs generally show more restricted patterns of expression. CONCLUSION: Zebrafish have a large set of integrin β1 paralogs. β1–1 and β1–2 may share the roles of the solitary β1 subunit found in other vertebrates, whereas β1–3 and the truncated β1 paralogs may have acquired novel functions. BioMed Central 2006-06-20 /pmc/articles/PMC1538996/ /pubmed/16787535 http://dx.doi.org/10.1186/1471-2121-7-24 Text en Copyright © 2006 Mould et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Mould, A Paul
McLeish, Jennifer A
Huxley-Jones, Julie
Goonesinghe, Alexander C
Hurlstone, Adam FL
Boot-Handford, Raymond P
Humphries, Martin J
Identification of multiple integrin β1 homologs in zebrafish (Danio rerio)
title Identification of multiple integrin β1 homologs in zebrafish (Danio rerio)
title_full Identification of multiple integrin β1 homologs in zebrafish (Danio rerio)
title_fullStr Identification of multiple integrin β1 homologs in zebrafish (Danio rerio)
title_full_unstemmed Identification of multiple integrin β1 homologs in zebrafish (Danio rerio)
title_short Identification of multiple integrin β1 homologs in zebrafish (Danio rerio)
title_sort identification of multiple integrin β1 homologs in zebrafish (danio rerio)
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1538996/
https://www.ncbi.nlm.nih.gov/pubmed/16787535
http://dx.doi.org/10.1186/1471-2121-7-24
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