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3 - Elastin as a Self-Assembling Biomaterial

Published online by Cambridge University Press:  13 August 2009

Peter R. Shewry
Affiliation:
University of Bristol
Arthur S. Tatham
Affiliation:
University of Bristol
Allen J. Bailey
Affiliation:
University of Bristol
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Summary

INTRODUCTION

Elastin is the major extracellular matrix protein in tissues – such as the large arterial blood vessels, lung parenchyma, elastic ligaments, and skin – where it is accepted to be principally responsible for the physical properties of extensibility and elastic recoil which are particularly important for the function of these tissues. Elastin is also the major matrix protein in some cartilaginous tissues – such as ear cartilage – where the functional role of this protein is less evident.

Elastic fibres are made up of two major components: an elastin component and a microfibrillar component. The microfibrillar component, consisting of 10–12 nm filaments, is made up of at least five distinct proteins but thought to be predominantly composed of fibrillin, a 350 kDa protein which exists in two forms: fibrillin-1 and fibrillin-2 (Sakai et al., 1986; Zhang et al., 1994) (see also chapter 5 by Kielty et al., in this volume). The microfibrils also include two microfibril-associated glycoproteins (MAGP-1 and MAGP-2) (Gibson et al., 1991, 1996). Elastic fibres may also include a number of other components, including a 67 kDa chaperone protein known as the elastin binding protein (EBP) (Hinek et al., 1988; Hinek and Rabinovitch, 1994), and lysyl oxidase, the enzyme that catalyzes oxidative deamination of lysine residues in preparation for crosslink formation (Kagan and Trackman, 1991).

Type
Chapter
Information
Elastomeric Proteins
Structures, Biomechanical Properties, and Biological Roles
, pp. 39 - 53
Publisher: Cambridge University Press
Print publication year: 2003

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