Function–structure relationship of elastic arteries in evolution: from microfibrils to elastin and elastic fibres

Faury, Gilles

doi:10.1016/s0369-8114(01)00147-x

Cited by 156 publications

(135 citation statements)

References 93 publications

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“…Megill and co-workers therefore suggest that the stress-strain curve of individual microfibrils is unlikely to be linear, and that microfibril stiffness will be less than our estimate at low strains and greater than our estimate at high strains. This scenario strengthens the hypothesis that fibrillin microfibrils are stiffer than elastin at the higher strains (0.22 in human aorta) which are experienced during normal physiological function (Faury 2001). The resistance of microfibrils to axial tension is further emphasised by recent X-ray diffraction studies of zonular microfibrils during extension which demonstrated that microfibril periodicity and diameter remain unchanged even at strains approaching 2 (Glab and Wess 2008).…”

Section: Structure and Functionsupporting

confidence: 74%

“…The nature of the contribution made by fibrillin microfibrils to tissue biomechanical properties remains, however, controversial. Elastin is not expressed in the tissues of invertebrates and it is thought that fibrillin microfibrils mediate elastic recoil in the low-pressure closed circulatory system of the lobster, and in the jellyfish mesoglea and sea cucumber dermis (Faury 2001;Megill et al 2005;Thurmond and Trotter 1996). The stiffness, or conversely, the compliance, of a material is quantified by determination of the elastic modulus (also known as Young's modulus) (Fig.…”

Section: Structure and Functionmentioning

confidence: 99%

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Tissue elasticity and the ageing elastic fibre

Sherratt

2009

AGE

265

189

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The ability of elastic tissues to deform under physiological forces and to subsequently release stored energy to drive passive recoil is vital to the function of many dynamic tissues. Within vertebrates, elastic fibres allow arteries and lungs to expand and contract, thus controlling variations in blood pressure and returning the pulmonary system to a resting state. Elastic fibres are composite structures composed of a cross-linked elastin core and an outer layer of fibrillin microfibrils. These two components perform distinct roles; elastin stores energy and drives passive recoil, whilst fibrillin microfibrils direct elastogenesis, mediate cell signalling, maintain tissue homeostasis via TGFβ sequestration and potentially act to reinforce the elastic fibre. In many tissues reduced elasticity, as a result of compromised elastic fibre function, becomes increasingly prevalent with age and contributes significantly to the burden of human morbidity and mortality. This review considers how the unique molecular structure, tissue distribution and longevity of elastic fibres pre-disposes these abundant extracellular matrix structures to the accumulation of damage in ageing dermal, pulmonary and vascular tissues. As compromised elasticity is a common feature of ageing dynamic tissues, the development of strategies to prevent, limit or reverse this loss of function will play a key role in reducing age-related morbidity and mortality.

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Section: Structure and Functionsupporting

confidence: 74%

Section: Structure and Functionmentioning

confidence: 99%

Tissue elasticity and the ageing elastic fibre

Sherratt

2009

AGE

265

189

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“…The addition of elastin is an evolutionary adaptation in vertebrate animals to handle the high pulsatile pressures of a closed circulatory system (Faury, 2001). Fibrillin-1 and -2 bind tropoelastin in solid phase binding assays (Trask et al, 2000b).…”

Section: Fibrillinsmentioning

confidence: 99%

New insights into elastic fiber assembly

Wagenseil

Mecham

2007

Birth Defects Research Pt C

355

354

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Elastic fibers provide recoil to tissues that undergo repeated stretch, such as the large arteries and lung. These large extracellular matrix (ECM) structures contain numerous components, and our understanding of elastic fiber assembly is changing as we learn more about the various molecules associated with the assembly process. The main components of elastic fibers are elastin and microfibrils. Elastin makes up the bulk of the mature fiber and is encoded by a single gene. Microfibrils consist mainly of fibrillin, but also contain or associate with proteins such as microfibril associated glycoproteins (MAGPs), fibulins, and EMILIN-1. Microfibrils were thought to facilitate alignment of elastin monomers prior to cross-linking by lysyl oxidase (LOX). We now know that their role, as well as the overall assembly process, is more complex. Elastic fiber formation involves elaborate spatial and temporal regulation of all of the involved proteins and is difficult to recapitulate in adult tissues. This report summarizes the known interactions between elastin and the microfibrillar proteins and their role in elastic fiber assembly based on in vitro studies and evidence from knockout mice. We also propose a model of elastic fiber assembly based on the current data that incorporates interactions between elastin, LOXs, fibulins and the microfibril, as well as the pivotal role played by cells in structuring the final functional fiber. Birth Defects Research (Part C) 81:229-240,

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“…Currently, researchers have hypothesized the mechanism of cardiovascular disease (CVD) is arterial dysfunction characterized by "premature aging" (27). This theory is based upon extracellular matrix (ECM) formation during the fetal and neonatal period with protein depositions of collagen and elastin, the largest contributors to vessel compliance, highest during this developmental window (9,15,42,43) and glycosaminoglycans (GAGs), important proteins in vessel ECM development and viscoelastic strength, also deposited during this period (13,35). Disruption of the synthesis and deposition of vascular collagen, elastin, and GAGs in utero is thought to be a major mechanism in adult CVD in previously IUGR individuals.…”

mentioning

confidence: 99%