Structural studies of elastic fibre and microfibrillar proteins

Singh, Mukti; Becker, Mark; Godwin, Alan R.; Baldock, Clair

doi:10.1016/j.mbplus.2021.100078

Cited by 4 publications

(4 citation statements)

References 148 publications

(185 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…FBN1 is the main component of elastic fiber assembly scaffold microfiber, and it is the basis for the final formation of fiber bundle shape of elastic fiber. Knockdown of FBN1 in mice, the elastic fibers showed fragmentation, accompanied by arterial bending and active phenotypic defects such as aneurysm (Singh et al, 2021). It is suggested that CDH11 increases the expression of ELN, LOX and FBN1, to promote the formation of reticular cross-linked collagen and elastic fiber bundles and increase the mechanical properties of the engineered cartilage.…”

Section: Discussionmentioning

confidence: 99%

Cadherin‐11 promotes the mechanical strength of engineered elastic cartilage by enhancing extracellular matrix synthesis and microstructure

Cao

Wang

et al. 2021

J Tissue Eng Regen Med

View full text Add to dashboard Cite

Limitations of current treatments for auricular cartilage defects have prompted the field of auricular cartilage tissue engineering. To date, inducing the formation of cartilaginous constructs with biochemical and biomechanical properties of native tissue is the final aim. Through hematoxylin-eosin and immunohistochemistry staining, Cadherin-11(CDH11) was confirmed highly expressed in the auricular cartilage tissue and chondrocytes. In vitro, by knockdown and overexpression of CDH11 in chondrocytes, CDH11 was demonstrated to promote the expression of collagen type II (COL2A), elastin (ELN), aggrecan (ACAN), and cartilage oligomeric matrix protein (COMP). In addition, the CDH11 overexpressed chondrocytes promoted neo-cartilage formation and its biomechanical property by increasing the key transcription factor of chondrogenesis SOX9 expression and cartilage extracellular matrix (ECM) production. The young's modulus and yield stress of the neo-cartilage in CDH11 overexpression group were about 1.7 times (p = 0.0152) and 2 times (p = 0.0428) higher than those in control group, respectively. Then, the immunohistochemistry staining, qRT-PCR and western blot examination results showed that the expression of COL2A and ELN were significantly increased. Notably, the electron microscopy results showed that the collagen and elastic fibers of the neo-cartilage in CDH11-OV group arranged in bunches and were more uniform and compact compared to the control group. Furthermore, CDH11 promoted elastic fiber assembly by increasing lysyl oxidase (LOX), fibrillin-1 (FBN1) expression. Taken together, our results demonstrated that CDH11 improves the mechanical strength of tissueengineered elastic cartilage by promoting ECM synthesis and elastic fiber assembly.

show abstract

Section: Discussionmentioning

confidence: 99%

Cadherin‐11 promotes the mechanical strength of engineered elastic cartilage by enhancing extracellular matrix synthesis and microstructure

Cao

Wang

et al. 2021

J Tissue Eng Regen Med

View full text Add to dashboard Cite

show abstract

“…Fibrillin is the major component of microfibrils. There are species- and tissue-dependent differences in the expression levels of three isotypes of fibrillin, with fibrillin-1 being the predominant isotype found in adult human tissues [ 9 , 88 , 89 , 90 ]. Although fibrillin is the major component of the microfibrils, an array of other less abundant molecules is necessary, including latent transforming growth factor-β binding proteins (LTBPs), matrix-associated glycoproteins (MAGPs), members of the fibulin family, and PGs.…”

Section: Elasticity Of Soft Tissuesmentioning

confidence: 99%

“…They play an essential role in the organization of fibers, but also their complex hierarchical assembly supports the biological functions of microfibrils, including induction of cellular responses to mechanical forces derived from the matrix microenvironment [ 10 , 14 , 87 , 91 ]. Therefore, the two basic components of an elastic fiber have distinct tasks in the tissue ECM; elastin stores energy of deformation and provides passive recoil, whilst fibrillin microfibrils direct elastogenesis, mediate cell signaling, and maintain tissue homeostasis [ 9 , 11 , 14 , 89 , 90 ].…”

Section: Elasticity Of Soft Tissuesmentioning

confidence: 99%

Mechanical Properties and Functions of Elastin: An Overview

Trębacz

Barzycka

2023

Biomolecules

View full text Add to dashboard Cite

Human tissues must be elastic, much like other materials that work under continuous loads without losing functionality. The elasticity of tissues is provided by elastin, a unique protein of the extracellular matrix (ECM) of mammals. Its function is to endow soft tissues with low stiffness, high and fully reversible extensibility, and efficient elastic–energy storage. Depending on the mechanical functions, the amount and distribution of elastin-rich elastic fibers vary between and within tissues and organs. The article presents a concise overview of the mechanical properties of elastin and its role in the elasticity of soft tissues. Both the occurrence of elastin and the relationship between its spatial arrangement and mechanical functions in a given tissue or organ are overviewed. As elastin in tissues occurs only in the form of elastic fibers, the current state of knowledge about their mechanical characteristics, as well as certain aspects of degradation of these fibers and their mechanical performance, is presented. The overview also outlines the latest understanding of the molecular basis of unique physical characteristics of elastin and, in particular, the origin of the driving force of elastic recoil after stretching.

show abstract

“…In mature tissues, elastic fibres are formed by a central component, elastin, surrounded by a mantle of microfibrils, mostly composed of fibrillin-1 and other glycoproteins (Singh et al, 2021). While microfibrils appear to act as a protective scaffold, the central elastin core, which represents about 90% of the fibre, is responsible for resilience as well as elastic recoil.…”

Section: Introductionmentioning

confidence: 99%

Structural and physical basis for the elasticity of elastin

Depenveiller,

Baud,

Belloy

et al. 2024

Quart. Rev. Biophys.

View full text Add to dashboard Cite

Elastin function is to endow vertebrate tissues with elasticity so that they can adapt to local mechanical constraints. The hydrophobicity and insolubility of the mature elastin polymer have hampered studies of its molecular organisation and structure-elasticity relationships. Nevertheless, a growing number of studies from a broad range of disciplines have provided invaluable insights, and several structural models of elastin have been proposed. However, many questions remain regarding how the primary sequence of elastin (and the soluble precursor tropoelastin) governs the molecular structure, its organisation into a polymeric network, and the mechanical properties of the resulting material. The elasticity of elastin is known to be largely entropic in origin, a property that is understood to arise from both its disordered molecular structure and its hydrophobic character. Despite a high degree of hydrophobicity, elastin does not form compact, water-excluding domains and remains highly disordered. However, elastin contains both stable and labile secondary structure elements. Current models of elastin structure and function are drawn from data collected on tropoelastin and on elastin-like peptides (ELPs) but at the tissue level, elasticity is only achieved after polymerisation of the mature elastin. In tissues, the reticulation of tropoelastin chains in water defines the polymer elastin that bears elasticity. Similarly, ELPs require polymerisation to become elastic. There is considerable interest in elastin especially in the biomaterials and cosmetic fields where ELPs are widely used. This review aims to provide an up-to-date survey of/perspective on current knowledge about the interplay between elastin structure, solvation, and entropic elasticity.

show abstract

Structural studies of elastic fibre and microfibrillar proteins

Cited by 4 publications

References 148 publications

Cadherin‐11 promotes the mechanical strength of engineered elastic cartilage by enhancing extracellular matrix synthesis and microstructure

Cadherin‐11 promotes the mechanical strength of engineered elastic cartilage by enhancing extracellular matrix synthesis and microstructure

Mechanical Properties and Functions of Elastin: An Overview

Structural and physical basis for the elasticity of elastin

Contact Info

Product

Resources

About