Book contents
- Frontmatter
- Contents
- Preface
- Contributors
- Elastomeric Proteins
- 1 Functions of Elastomeric Proteins in Animals
- 2 Elastic Proteins: Biological Roles and Mechanical Properties
- 3 Elastin as a Self-Assembling Biomaterial
- 4 Ideal Protein Elasticity: The Elastin Models
- 5 Fibrillin: From Microfibril Assembly to Biomechanical Function
- 6 Spinning an Elastic Ribbon of Spider Silk
- 7 Sequences, Structures, and Properties of Spider Silks
- 8 The Nature of Some Spiders' Silks
- 9 Collagen: Hierarchical Structure and Viscoelastic Properties of Tendon
- 10 Collagens with Elastin- and Silk-like Domains
- 11 Conformational Compliance of Spectrins in Membrane Deformation, Morphogenesis, and Signalling
- 12 Giant Protein Titin: Structural and Functional Aspects
- 13 Structure and Function of Resilin
- 14 Gluten, the Elastomeric Protein of Wheat Seeds
- 15 Biological Liquid Crystal Elastomers
- 16 Restraining Cross-Links in Elastomeric Proteins
- 17 Comparative Structures and Properties of Elastic Proteins
- 18 Mechanical Applications of Elastomeric Proteins – A Biomimetic Approach
- 19 Biomimetics of Elastomeric Proteins in Medicine
- Index
5 - Fibrillin: From Microfibril Assembly to Biomechanical Function
Published online by Cambridge University Press: 13 August 2009
- Frontmatter
- Contents
- Preface
- Contributors
- Elastomeric Proteins
- 1 Functions of Elastomeric Proteins in Animals
- 2 Elastic Proteins: Biological Roles and Mechanical Properties
- 3 Elastin as a Self-Assembling Biomaterial
- 4 Ideal Protein Elasticity: The Elastin Models
- 5 Fibrillin: From Microfibril Assembly to Biomechanical Function
- 6 Spinning an Elastic Ribbon of Spider Silk
- 7 Sequences, Structures, and Properties of Spider Silks
- 8 The Nature of Some Spiders' Silks
- 9 Collagen: Hierarchical Structure and Viscoelastic Properties of Tendon
- 10 Collagens with Elastin- and Silk-like Domains
- 11 Conformational Compliance of Spectrins in Membrane Deformation, Morphogenesis, and Signalling
- 12 Giant Protein Titin: Structural and Functional Aspects
- 13 Structure and Function of Resilin
- 14 Gluten, the Elastomeric Protein of Wheat Seeds
- 15 Biological Liquid Crystal Elastomers
- 16 Restraining Cross-Links in Elastomeric Proteins
- 17 Comparative Structures and Properties of Elastic Proteins
- 18 Mechanical Applications of Elastomeric Proteins – A Biomimetic Approach
- 19 Biomimetics of Elastomeric Proteins in Medicine
- Index
Summary
INTRODUCTION
Fibrillin-rich microfibrils are thin filamentous connective tissue assemblies present in virtually all dynamic connective tissues (Fig. 5.1) (Kielty and Shuttleworth, 1995; Handford et al., 2000; Sherratt et al., 2000). In elastic tissues – such as aorta, lung, skin, and elastic cartilage – preformed bundles of microfibrils form a template for tropoelastin deposition during elastic fibre formation and are retained as an outer mantle of mature elastic fibres (Mecham and Heuser, 1991). Microfibril arrays are often abundant in tissues which do not express elastin, such as the ciliary zonules of the eye which hold the lens in dynamic equilibrium (Ashworth et al., 2000).
Several recent studies, based on whole tissues and isolated fibrillin-rich microfibrils, have highlighted their unique elastic properties that are critical to their biological function alone or in association with elastin. The extensibility of lobster aorta was accounted for by microfibril arrays that intersperse medial smooth muscle cells (McConnell et al., 1996). Extracted sea cucumber microfibrils exhibited long-range elastomeric properties (Thurmond and Trotter, 1996). X-ray diffraction, tensile testing, and stress-relaxation tests demonstrated that hydrated mammalian ciliary zonules and microfibril bundles are reversibly extensible in the presence or absence of calcium (Wess et al., 1998a; Wright et al., 1999; Eriksen et al., 2001). Isolated human microfibrils tangled in debris during preparation for electron microscopy can become stretched to periodicities up to ∼ 165 nm (Keene et al., 1991). Extended microfibrils, often observed in matrix metalloproteinase-treated preparations, may reflect pathological loss of elastic recoil (Ashworth et al., 1999a).
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- Elastomeric ProteinsStructures, Biomechanical Properties, and Biological Roles, pp. 94 - 114Publisher: Cambridge University PressPrint publication year: 2003
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