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Evolution of collagens
Article first published online: 14 OCT 2002
DOI: 10.1002/ar.10162
Copyright © 2002 Wiley-Liss, Inc.
Issue
1932-8494/asset/cover.gif?v=1&s=f95bde22395f72795e3dd8e55db6c7f940a1a957 "The Anatomical Record")
The Anatomical Record
Special Issue: Astrobiology
Volume 268, Issue 3, pages 302–316, 1 November 2002
Additional Information
How to Cite
Exposito, J.-Y., Cluzel, C., Garrone, R. and Lethias, C. (2002), Evolution of collagens. Anat. Rec., 268: 302–316. doi: 10.1002/ar.10162
Publication History
- Issue published online: 14 OCT 2002
- Article first published online: 14 OCT 2002
- Manuscript Accepted: 28 FEB 2002
- Manuscript Received: 14 DEC 2001
- Abstract
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- References
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Keywords:
- collagen;
- extracellular matrix;
- evolution
Abstract
The extracellular matrix is often defined as the substance that gives multicellular organisms (from plants to vertebrates) their structural integrity, and is intimately involved in their development. Although the general functions of extracellular matrices are comparable, their compositions are quite distinct. One of the specific components of metazoan extracellular matrices is collagen, which is present in organisms ranging from sponges to humans. By comparing data obtained in diploblastic, protostomic, and deuterostomic animals, we have attempted to trace the evolution of collagens and collagen-like proteins. Moreover, the collagen story is closely involved with the emergence and evolution of metazoa. The collagen triple helix is one of numerous modules that arose during the metazoan radiation which permit the formation of large multimodular proteins. One of the advantages of this module is its involvement in oligomerization, in which it acts as a structural organizer that is not only relatively resistant to proteases but also permits the creation of multivalent supramolecular networks. Anat Rec 268:302–316, 2002. © 2002 Wiley-Liss, Inc.