Collagens at a glance

Kadler, Karl E.; Baldock, Clair; Bella, Jordi; Boot-Handford, Raymond P.

doi:10.1242/jcs.03453

Cited by 700 publications

(607 citation statements)

References 29 publications

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“…In this tissue, the fibrils display a diameter at least five times larger in which the nanofibrils must be more constrained (for example, 50 to 200 nm in Ref. 27). This also explains why we were unable to record any 13 C signal through a cross-polarization MAS experiment and the very strong signal of the INEPT experiments for all carbons.…”

Section: Discussionmentioning

confidence: 99%

Solid-state NMR Study Reveals Collagen I Structural Modifications of Amino Acid Side Chains upon Fibrillogenesis

Peixoto¹,

Laurent²,

Azaı̈s³

et al. 2013

Journal of Biological Chemistry

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Background: Collagen fibrillogenesis is a fundamental process both in vivo and in vitro. Results: Fibrillogenesis increases the heterogeneity of conformations of side chain amino acids, impacting 40% of imino acids. Conclusion: A temperature-induced-attractive force component comes from significant amount of the collagen amino acids. Significance: This work brings new perspectives to studies of collagen assembly and interactions with other matrix molecules.

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Section: Discussionmentioning

confidence: 99%

Solid-state NMR Study Reveals Collagen I Structural Modifications of Amino Acid Side Chains upon Fibrillogenesis

Peixoto¹,

Laurent²,

Azaı̈s³

et al. 2013

Journal of Biological Chemistry

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“…The highest expression of tenascin is observed in unstable environments such as during cell migration, in active areas of epithelialmesenchymal interactions, and in neoplastic stroma [14,16,18,24]. Type I collagen is found throughout the connective tissue and is one of the most abundant components of the interstitial ECM [5,23,25], being highly resistant to proteases due to its unique supercoiled triple helix structure [26][27][28].…”

Section: Discussionmentioning

confidence: 99%

Expression of extracellular matrix proteins in ameloblastomas and adenomatoid odontogenic tumors

Medeiros

Nonaka

Galvão

et al. 2009

Eur Arch Otorhinolaryngol

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This study evaluated the expression of Wbronectin, tenascin and type I collagen in ameloblastomas and adenomatoid odontogenic tumors (AOTs) aiming to contribute with the comprehension of the diVerences in the biological behavior of these tumors. Immunohistochemical technique was performed in 20 cases of ameloblastoma (16 solid and 4 desmoplastic) and in 10 cases of AOT. All tumors presented moderate Wbronectin expression in the stroma. Solid ameloblastomas showed intense expression of Wbronectin at the epithelial-mesenchymal interface, whereas desmoplastic ameloblastomas revealed no immunoexpression of Wbronectin at this site. Ameloblastomas presented stronger immunoreactivity to tenascin than AOTs, especially at the epithelial-mesenchymal interface. AOTs and desmoplastic ameloblastomas showed intense labeling for type I collagen. The patterns of expression of the proteins studied agree with the locally more invasive behavior of ameloblastomas in comparison to AOTs. Our results might suggest a less invasive behavior of desmoplastic ameloblastoma in comparison to solid ameloblastoma.

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“…Collagen molecules represent the most abundant protein building block in the human body, where they provide mechanical stability, elasticity and strength to connective tissues such as tendons, ligaments and bone, as well as the extracellular matrix (ECM) [1]. Since pioneering experimental works by Fraser, Hulmes, Hess, Orgel, Fratzl and others it is known that virtually all collagen-based tissues are organized into hierarchical structures, where the lowest hierarchical level consists of triple helical collagen molecules (Fig.…”

Section: Introductionmentioning

confidence: 99%

Hierarchical Structure and Nanomechanics of Collagen Microfibrils from the Atomistic Scale Up

Gautieri

Vesentini²,

Redaelli³

et al. 2011

Nano Lett.

610

488

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Abstract:Collagen constitutes one third of the human proteome, providing mechanical stability, elasticity and strength to connective tissues. Collagen is also the dominating material in the extracellular matrix (ECM) and is thus crucial for cell differentiation, growth and pathology. However, fundamental questions remain with respect to the origin of the unique mechanical properties of collagenous tissues, and in particular its stiffness, extensibility and nonlinear mechanical response. By using x-ray diffraction data of a collagen fibril reported by Orgel et al.(Proceedings of the National Academy of Sciences USA, 2006) in combination with protein structure identification methods, here we present an experimentally validated model of the nanomechanics of a collagen microfibril that incorporates the full biochemical details of the amino acid sequence of the constituting molecules. We report the analysis of its mechanical properties under different levels of stress and solvent conditions, using a full-atomistic force field including explicit water solvent. Mechanical testing of hydrated collagen microfibrils yields a Young's modulus of ≈300 MPa at small and ≈1.2 GPa at larger deformation in excess of 10% strain, in excellent agreement with experimental data. Dehydrated, dry collagen microfibrils show a significantly increased Young's modulus of ≈1.8 to 2.25 GPa (or ≈6.75 times the modulus in the wet state) owing to a much tighter molecular packing, in good agreement with experimental measurements (where an increase of the modulus by ≈9 times was found). Our model demonstrates that the unique mechanical properties of collagen microfibrils can be explained based on their hierarchical structure, where deformation is mediated through mechanisms that operate at different hierarchical levels. Key mechanisms involve straightening of initially disordered and helically twisted molecules at small strains, followed by axial stretching of molecules, and eventual molecular uncoiling at extreme deformation. These mechanisms explain the striking difference of the modulus of collagen fibrils compared with single molecules, which is found in the range of 4.8±2 GPa or ≈10-20 times greater. These findings corroborate the notion that collagen tissue properties are highly scale dependent and nonlinear elastic, an issue that must be considered in the development of models that describe the interaction of cells with collagen in the extracellular matrix. A key impact the atomistic model of collagen microfibril mechanics reported here is that it enables the bottom-up elucidation of structure-property relationships in the broader class of collagen materials such as tendon or bone, including studies in the context of genetic disease where the incorporation of biochemical, genetic details in material models of connective tissue is essential.

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Collagens at a glance

Cited by 700 publications

References 29 publications

Solid-state NMR Study Reveals Collagen I Structural Modifications of Amino Acid Side Chains upon Fibrillogenesis

Solid-state NMR Study Reveals Collagen I Structural Modifications of Amino Acid Side Chains upon Fibrillogenesis

Expression of extracellular matrix proteins in ameloblastomas and adenomatoid odontogenic tumors

Hierarchical Structure and Nanomechanics of Collagen Microfibrils from the Atomistic Scale Up

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