Elastin

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Abstract

Elastin is a key extracellular matrix protein that is critical to the elasticity and resilience of many vertebrate tissues including large arteries, lung, ligament, tendon, skin, and elastic cartilage. Tropoelastin associates with multiple tropoelastin molecules during the major phase of elastogenesis through coacervation, where this process is directed by the precise patterning of mostly alternating hydrophobic and hydrophilic sequences that dictate intermolecular alignment. Massively crosslinked arrays of tropoelastin (typically in association with microfibrils) contribute to tissue structural integrity and biomechanics through persistent flexibility, allowing for repeated stretch and relaxation cycles that critically depend on hydrated environments. Elastin sequences interact with multiple proteins found in or colocalized with microfibrils, and bind to elastogenic cell surface receptors. Knowledge of the major stages in elastin assembly has facilitated the construction of in vitro models of elastogenesis, leading to the identification of precise molecular regions that are critical to elastin-based protein interactions.

Section snippets

Elastic Fiber

The extracellular matrix imparts structural integrity on the tissues and organs of the body. It also acts as a dynamic modulator of a variety of biological processes. An important component of the extracellular matrix is the elastic fiber. Elastic fibers confer the properties of elastic recoil and resilience on all vertebrate elastic tissues, with the exception of lower vertebrates such as the lamprey (Debelle and Tamburro, 1999). Such properties are critical to the long-term function of these

Elastogenesis

In vivo elastin fiber formation requires the coordination of a number of important processes. These include the control of intracellular transcription and translation of tropoelastin, intracellular processing of the protein, secretion of the protein into the extracellular space, delivery of tropoelastin monomers to sites of elastogenesis, alignment of the monomers with previously accreted tropoelastin through associating microfibrillar proteins, and finally, the conversion to the insoluble

Physical Properties

Purified elastin is pale yellow and has a characteristic blue fluorescence in ultraviolet light (Partridge, 1962). When dry, it is a hard, brittle glassy solid. On wetting, it becomes flexible and elastic. The water content of elastin is affected by temperature; a large increase is seen in the swollen volume of elastin with decreasing temperature (Lillie and Gosline, 2002). At 36 °C, purified bovine ligamentum nuchae (which is primarily composed of elastin) contains 0.46 g water⧸g protein; at

Mechanism of Elasticity

The fundamental driving force behind the remarkable elastic properties of the elastin polymer is believed to be entropic, where stretching decreases the entropy of the system and elastic recoil is driven by a spontaneous return to maximum entropy. The precise molecular basis for elasticity has not been fully elucidated and a number of models exist. Two main categories of structure-function models have been proposed: those in which elastin is considered to be isotropic and devoid of structure,

Biomaterials

In healthy individuals, the mature elastin molecule is a stable, insoluble protein. Degradation of elastin is extremely slow due to the extensive crosslinking of tropoelastin within the elastic fiber. However, with aging, injury, or the onset of a variety of acquired diseases, the degradation and excessive or aberrant remodeling of elastic fibers becomes apparent in arteries, lung, skin, and ligament (Osakabe et al., 2001). The correct assembly of the elastin polymer is critical for proper

Acknowledgements

ASW is a recipient of grants from the Australian Research Council and the University of Sydney Vice Chancellor's Development Fund.

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