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The Evolution of Elastin

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Evolution of Extracellular Matrix

Part of the book series: Biology of Extracellular Matrix ((BEM))

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Abstract

Elastin is the matrix protein imparting the physiologically essential properties of extensibility and elastic recoil to large arteries, lung parenchyma and other vertebrate tissues. Elastin is a polymeric protein formed from tropoelastin monomers and cross-linked, like collagens, through the side chains of lysine residues by the action of lysyl oxidase. Unlike many matrix proteins, elastin appeared relatively late in evolution, present in all species from sharks to humans, but absent at least as a vascular protein from lampreys, hagfish and other lower chordates and invertebrates. As an entropic elastomer, the polypeptide chains of elastin must remain disordered even in the polymeric state. Like many other disordered structural proteins, elastin has a low complexity, highly nonpolar and highly repetitive sequence, with the conservation of an unusual ‘style’ of sequence but an apparently relaxed requirement for precise sequence conservation, even between closely related species. Here, using both full-length and partial tropoelastin sequences representing the full range of phylogeny over which this protein is found, we describe the sequence elements and domain arrangements that are shared by all tropoelastins and are therefore likely to be required for its fundamental properties as an entropic elastomer. We then examine differences in sequence and domain arrangements between species perhaps representing adaptations to species- or tissue-specific functional requirements that may drive evolutionary changes. Finally, we consider the relationship of tropoelastins to other glycine-rich, nonpolar structural proteins that have been described in lower chordates and invertebrates and the possible evolutionary roots of this unusual protein.

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Acknowledgements

The author acknowledges the essential contributions to this work by present and former members of his research laboratory, including Richard Stahl, Lisa Muiznieks, Ming Miao, Eva Sitarz, Sean Reichheld and Martin Chung. Noeleen Loughran provided valuable assistance in the production of phylogenetic trees. This work was supported by operational grants from the Heart and Stroke Foundation of Ontario, the Canadian Institutes of Health Research and the Natural Sciences and Engineering Research Council of Canada. The author holds the Heart and Stroke Foundation of Ontario/Robert M. Freedom Chair in Cardiovascular Science at the Hospital for Sick Children.

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  1. Molecular Structure and Function Program, Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto, Canada

    Fred W. Keeley

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Correspondence to Fred W. Keeley .

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  1. Hospital for Sick Children, Toronto, Ontario, Canada

    Fred W. Keeley

  2. Dept. Cell Biology & Physiology, Washington University School of Medicine, St. Louis, Missouri, USA

    Robert P. Mecham

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Keeley, F.W. (2013). The Evolution of Elastin. In: Keeley, F., Mecham, R. (eds) Evolution of Extracellular Matrix. Biology of Extracellular Matrix. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-36002-2_4

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