Despite distinct mechanical functions, biological soft tissues have a common microstructure in which a ground matrix is reinforced by a collagen fibril network. The microstructural properties of the collagen network contribute to continuum mechanical tissue properties that are strongly anisotropic with tensile-compressive asymmetry. In this study, a novel approach based on a continuous distribution of collagen fibril volume fractions is developed to model fibril reinforced soft tissues as a nonlinearly elastic and anisotropic material. Compared with other approaches that use a normalized number of fibrils for the definition of the distribution function, this representation is based on a distribution parameter (i.e. volume fraction) that is commonly measured experimentally while also incorporating pre-stress of the collagen fibril network in a tissue natural configuration. After motivating the form of the collagen strain energy function, examples are provided for two volume fraction distribution functions. Consequently, collagen second-Piola Kirchhoff stress and elasticity tensors are derived, first in general form and then specifically for a model that may be used for immature bovine articular cartilage. It is shown that the proposed strain energy is a convex function of the deformation gradient tensor and, thus, is suitable for the formation of a polyconvex tissue strain energy function.
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http://dx.doi.org/10.1177/1081286510387866 | DOI Listing |
iScience
January 2025
Abteilung Paläontologie, Bonner Institut für Organismische Biologie, Universität Bonn, 53115 Bonn, Germany.
Bone is formed by specialized cells whose activity allows bone to grow, change shape, and repair itself. Its composite structure of collagen fibrils and bioapatite nanocrystals gives bone exceptional mechanical strength. Using scanning electron microscopy, we show in fossil ichthyosaurs, 150 to 200 million years old, from the Jurassic of France and the UK, abundant and direct evidence of cellular activity on the fossilized forming, resting, and resorbing surfaces of bone trabeculae, as well as bone fibrils, Sharpey fibers, and cartilage fibers.
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January 2025
Wellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, United Kingdom.
Collagen-I fibrillogenesis is crucial to health and development, where dysregulation is a hallmark of fibroproliferative diseases. Here, we show that collagen-I fibril assembly required a functional endocytic system that recycles collagen-I to assemble new fibrils. Endogenous collagen production was not required for fibrillogenesis if exogenous collagen was available, but the circadian-regulated vacuolar protein sorting (VPS) 33b and collagen-binding integrin α11 subunit were crucial to fibrillogenesis.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
Organoid Research Center, Institute of Translational Medicine, Shanghai University, Shanghai 200444, People's Republic of China.
Osteoporosis (OP) is a systemic skeletal disorder characterized by decreased bone mineral density and a heightened risk of fractures. Therapies for OP have primarily focused on balancing bone formation and bone resorption, but enhancing the remineralization of osteoporotic bone is also a key strategy for effective repair. Recent insights into biomineralization mechanisms have highlighted the essential role of mineral-containing extracellular vesicles (EVs) secreted by osteoblasts in promoting bone marrow mesenchymal stromal/stem cell (BMSC) differentiation and initiating matrix mineralization.
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January 2025
University of Amsterdam, Amsterdam, Netherlands.
Background: Achilles tendinopathy (AT) management can be difficult, given the paucity of effective treatment options and the degenerative nature of the condition. Innovative therapies for Achilles tendinopathy are therefore direly needed. New therapeutic developments predominantly begin with preclinical animal and in vitro studies to understand the effects at the molecular level and to evaluate toxicity.
View Article and Find Full Text PDFMatrix Biol
February 2025
Department of Physics, Simon Fraser University, Burnaby, BC, V5A 1S6, Canada. Electronic address:
Advanced Glycation End Products (AGEs) are the end result of the irreversible, non-enzymatic glycation of proteins by reducing sugars. These chemical modifications accumulate with age and have been associated with various age-related and diabetic complications. AGEs predominantly accumulate on proteins with slow turnover rates, of which collagen is a prime example.
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