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Modelling the early evolution of extracellular matrix from modern Ctenophores and Sponges

Research output: Contribution to journalReview article

Original languageEnglish
Pages (from-to)389-405
Number of pages17
JournalEssays in Biochemistry
Volume63
Issue number3
DOIs
DateAccepted/In press - 1 Aug 2019
DatePublished (current) - 13 Aug 2019

Abstract

Animals (metazoans) include some of the most complex living organisms on Earth, with regard to their multicellularity, numbers of differentiated cell types, and lifecycles. The metazoan extracellular matrix (ECM) is well-known to have major roles in the development of tissues during embryogenesis and in maintaining homoeostasis throughout life, yet insight into the ECM proteins which may have contributed to the transition from unicellular eukaryotes to multicellular animals remains sparse. Recent phylogenetic studies place either ctenophores or poriferans as the closest modern relatives of the earliest emerging metazoans. Here, we review the literature and representative genomic and transcriptomic databases for evidence of ECM and ECM-affiliated components known to be conserved in bilaterians, that are also present in ctenophores and/or poriferans. Whereas an extensive set of related proteins are identifiable in poriferans, there is a strikingly lack of conservation in ctenophores. From this perspective, much remains to be learnt about the composition of ctenophore mesoglea. The principal ECM-related proteins conserved between ctenophores, poriferans, and bilaterians include collagen IV, laminin-like proteins, thrombospondin superfamily members, integrins, membrane-associated proteoglycans, and tissue transglutaminase. These are candidates for a putative ancestral ECM that may have contributed to the emergence of the metazoans.

    Research areas

  • Ctenophora, Integrins, Protein Domains, Multicellularity, Porifera, Metazoa

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via Portland Press at https://portlandpress.com/essaysbiochem/article-lookup/doi/10.1042/EBC20180048 . Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 9 MB, PDF document

    Embargo ends: 13/08/20

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DOI

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