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Collagen cross-linking: insights on the evolution of metazoan extracellular matrix

Rodriguez-Pascual, Fernando and Slatter, David Anthony 2016. Collagen cross-linking: insights on the evolution of metazoan extracellular matrix. Scientific Reports 6 (1) , 37374. 10.1038/srep37374

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Abstract

Collagens constitute a large family of extracellular matrix (ECM) proteins that play a fundamental role in supporting the structure of various tissues in multicellular animals. The mechanical strength of fibrillar collagens is highly dependent on the formation of covalent cross-links between individual fibrils, a process initiated by the enzymatic action of members of the lysyl oxidase (LOX) family. Fibrillar collagens are present in a wide variety of animals, therefore often being associated with metazoan evolution, where the emergence of an ancestral collagen chain has been proposed to lead to the formation of different clades. While LOX-generated collagen cross-linking metabolites have been detected in different metazoan families, there is limited information about when and how collagen acquired this particular modification. By analyzing telopeptide and helical sequences, we identified highly conserved, potential cross-linking sites throughout the metazoan tree of life. Based on this analysis, we propose that they have importantly contributed to the formation and further expansion of fibrillar collagens.

Item Type: Article
Date Type: Published Online
Status: Published
Schools: Medicine
Publisher: Nature Publishing Group
ISSN: 2045-2322
Date of First Compliant Deposit: 5 July 2017
Date of Acceptance: 28 October 2016
Last Modified: 17 Jul 2017 13:57
URI: http://orca-mwe.cf.ac.uk/id/eprint/102078

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