Microscale mechanical properties of single elastic fibers: The role of fibrillin–microfibrils

Koenders, Mieke M J F; Yang, Lanti; Wismans, Ronnie G.; Werf, Kees O. van der; Reinhardt, Dieter P.; Daamen, Willeke F.; Bennink, Martin L.; Dijkstra, Pieter J.; Kuppevelt, Toin H. Van; Feijén, Jan

doi:10.1016/j.biomaterials.2009.01.038

Cited by 38 publications

(27 citation statements)

References 45 publications

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“…Hence, our fitted k crit value of 2.17 represents the combined effect of the two proteins. Our fitted value (2.51 MPa) of small strain Young's modulus is within the range of values reported for elastin (estimated 0.3-10 MPa) in vessel walls [26,36,37].…”

Section: Discussionsupporting

confidence: 88%

Prefailure and Failure Mechanics of the Porcine Ascending Thoracic Aorta: Experiments and a Multiscale Model

Shah

Witzenburg

Hadi

et al. 2014

Journal of Biomechanical Engineering

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Ascending thoracic aortic aneurysms (ATAA) have a high propensity for dissection, which occurs when the hemodynamic load exceeds the mechanical strength of the aortic media. Despite our recognition of this essential fact, the complex architecture of the media has made a predictive model of medial failure-even in the relatively simple case of the healthy vessel-difficult to achieve. As a first step towards a general model of ATAA failure, we characterized the mechanical behavior of healthy ascending thoracic aorta (ATA) media using uniaxial stretch-to-failure in both circumferential (n ¼ 11) and axial (n ¼ 11) orientations and equibiaxial extensions (n ¼ 9). Both experiments demonstrated anisotropy, with higher tensile strength in the circumferential direction (2510 6 439.3 kPa) compared to the axial direction (750 6 102.6 kPa) for the uniaxial tests, and a ratio of 1.44 between the peak circumferential and axial loads in equibiaxial extension. Uniaxial tests for both orientations showed macroscopic tissue failure at a stretch of 1.9. A multiscale computational model, consisting of a realistically aligned interconnected fiber network in parallel with a neo-Hookean solid, was used to describe the data; failure was modeled at the fiber level, with an individual fiber failing when stretched beyond a critical threshold. The best-fit model results were within the 95% confidence intervals for uniaxial and biaxial experiments, including both prefailure and failure, and were consistent with properties of the components of the ATA media.

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Section: Discussionsupporting

confidence: 88%

Prefailure and Failure Mechanics of the Porcine Ascending Thoracic Aorta: Experiments and a Multiscale Model

Shah

Witzenburg

Hadi

et al. 2014

Journal of Biomechanical Engineering

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“…We speculated that this arises because the microfibrils influence the realignment of the elastin under applied load or through their binding to and altering the physico-chemical properties of the elastin monomer. However, the demonstration of the similarity of mechanical properties of the two components indicates that a more direct mechanical function of the fibrillin is possible, and this is supported by recent measurements on the mechanics of ligament elastic fibres with and without glycoproteins [32]. Resolution of this question requires knowledge of the organization of the microfibrillar network and the strains to which it is exposed.…”

Section: Fibre and Molecular Mechanicsmentioning

confidence: 87%

The structure and micromechanics of elastic tissue

et al. 2014

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Elastin is a major component of tissues such as lung and blood vessels, and endows them with the long-range elasticity necessary for their physiological functions. Recent research has revealed the complexity of these elastin structures and drawn attention to the existence of extensive networks of fine elastin fibres in tissues such as articular cartilage and the intervertebral disc. Nonlinear microscopy, allowing the visualization of these structures in living tissues, is informing analysis of their mechanical properties. Elastic fibres are complex in composition and structure containing, in addition to elastin, an array of microfibrillar proteins, principally fibrillin. Raman microspectrometry and X-ray scattering have provided new insights into the mechanisms of elasticity of the individual component proteins at the molecular and fibrillar levels, but more remains to be done in understanding their mechanical interactions in composite matrices. Elastic tissue is one of the most stable components of the extracellular matrix, but impaired mechanical function is associated with ageing and diseases such as atherosclerosis and diabetes. Efforts to understand these associations through studying the effects of processes such as calcium and lipid binding and glycation on the mechanical properties of elastin preparations in vitro have produced a confusing picture, and further efforts are required to determine the molecular basis of such effects.

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“…Even in populations of collagenase-digested microfibrils, most periods are between 46 and 66 nm, and only 10% of the population exceeds 70 nm (Wang et al 2009). The question of microfibril elasticity and the contribution of microfibrils to the elasticity of elastic fibers have been directly addressed by Koenders et al (2009), but these studies have also been hampered by the difficulties in separating elastin fibers from microfibrils.…”

Section: Fibrillin Assembliesmentioning

confidence: 99%

Biogenesis and function of fibrillin assemblies

2009

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Fibrillin-1 and fibrillin-2 are large cysteine-rich glycoproteins that serve two key physiological functions: as supporting structures that impart tissue integrity and as regulators of signaling events that instruct cell performance. The structural role of fibrillins is exerted through the temporal and hierarchical assembly of microfibrils and elastic fibers, whereas the instructive role reflects the ability of fibrillins to sequester transforming growth factor β (TGFβ) and bone morphogenetic protein (BMP) complexes in the extracellular matrix. Characterization of fibrillin mutations in human patients and in genetically engineered mice has demonstrated that perturbation of either function manifests in disease. More generally, these studies have indicated that fibrillins are integral components of a broader biological network of extracellular, cell surface, and signaling molecules that orchestrate morphogenetic and homeostatic programs in multiple organ systems. They have also suggested that the relative composition of fibrillin-rich microfibrils imparts contextual specificity to TGFβ and BMP signaling by concentrating the ligands locally so as to regulate cell differentiation within a spatial context during organ formation (positive regulation) and by restricting their bioavailability so as to modulate cell performance in a timely fashion during tissue remodeling/ repair (negative regulation). Correlative evidence suggests functional coupling of the cell-directed assembly of micro-fibrils and targeting of TGFβ and BMP complexes to fibrillins. Hence, the emerging view is that fibrillin-rich microfibrils are molecular integrators of structural and instructive signals, with TGFβ and BMPs as the nodal points that convert extracellular inputs into discrete and context-dependent cellular responses.

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Microscale mechanical properties of single elastic fibers: The role of fibrillin–microfibrils

Cited by 38 publications

References 45 publications

Prefailure and Failure Mechanics of the Porcine Ascending Thoracic Aorta: Experiments and a Multiscale Model

Prefailure and Failure Mechanics of the Porcine Ascending Thoracic Aorta: Experiments and a Multiscale Model

The structure and micromechanics of elastic tissue

Biogenesis and function of fibrillin assemblies

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