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Unraveling the role of Calcium ions in the mechanical properties of individual collagen fibrils.

ABSTRACT: Collagen, the dominating material in the extracellular matrix, provides the strength, elasticity and mechanical stability to the organisms. The mechanical property of collagen is mainly dominated by its surrounding environments. However, the variation and origin of the mechanics of collagen fibril under different concentrations of calcium ions (χ_Ca) remains unknown. By using the atomic force microscopy based nanoindentation, the mechanics and structure of individual type II collagen fibril were first investigated under different χ_Ca in this study. The results demonstrate that both of the mechanical and structural properties of the collagen fibril show a prominent dependence on χ_Ca. The mechanism of χ_Ca-dependence of the collagen fibril was attributed to the chelation between collagen molecules and the calcium ions. Given the role of calcium in the pathology of osteoarthritis, the current study may cast new light on the understanding of osteoarthritis and other soft tissue hardening related diseases in the future.

SUBMITTER: Pang X

PROVIDER: S-EPMC5380965 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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Unraveling the role of Calcium ions in the mechanical properties of individual collagen fibrils.

Pang Xiangchao X Lin Lijun L Tang Bin B Tang Bin B

Scientific reports 20170405

Collagen, the dominating material in the extracellular matrix, provides the strength, elasticity and mechanical stability to the organisms. The mechanical property of collagen is mainly dominated by its surrounding environments. However, the variation and origin of the mechanics of collagen fibril under different concentrations of calcium ions (χ<sub>Ca</sub>) remains unknown. By using the atomic force microscopy based nanoindentation, the mechanics and structure of individual type II collagen f ...[more]

PMID: 28378770

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Project description:PurposeThe aim of this study was to identify the presence of collagen-binding integrin subunits in human scleral fibroblasts (HSFs) and investigate their actual functions in maintaining the mechanical creep properties of the HSFs-seeded collagen matrix.MethodsPrimary HSFs were cultured in vitro. Reverse- transcription PCR was used to detect mRNA expression of integrin α1, α2, and β1 subunits in HSFs. In addition, western blot analysis and immunofluorescence were used to detect their protein in HSFs. Monoclonal antibodies were applied directly against the extracellular domains of integrin subunits in HSFs cultured in the three-dimensional collagen gels to block the interaction between HSFs and the extracellular collagen matrix. The effects of anti-integrin antibodies on HSFs morphology in collagen gel were observed. The effects of the added antibodies on fibroblast-mediated collagen gels' contraction were evaluated. Furthermore, the changes in mechanical creep properties of collagen gel were measured by a biomechanics test instrument.ResultsThe mRNA and protein expressions of collagen-binding integrin α1, α2, and β1 subunits were present in HSFs. The elongated bipolar cells converted to spherical shapes after 6 h after the addition of integrin α1β1 and α2β1 antibody. The blocking of integrin α1β1 and α2β1 subunits noticeably decreased the contraction in the collagen gels. In addition, all samples were subjected to a constantly applied load of 0.03 N for 600 s. The blocking of integrin α1β1 and α2β1 subunits also induced increases in the values of final extension, creep extension, and creep rate, compared to those of the controls (p<0.01). Furthermore, the creep elements were significantly increased with the augmentation of the integrin antibody dose (p<0.01). The final extension of the integrin α2β1 antibody (1 μg/ml or 4 μg/ml) group was significantly higher compared to that of the integrin α1β1 antibody (1 μg/ml or 4 μg/ml) group (p<0.01). However, the creep extension and creep rate of the integrin α2β1 antibody (1 μg/ml or 4 μg/ml) group were not significantly different from those in the integrin α1β1 antibody (1 μg/ml or 4 μg/ml) group (p>0.05).ConclusionsOur findings suggested that HSF integrin α1β1 and α2β1 participated in maintaining the mechanical creep properties of the HSFs-seeded collagen matrix. Furthermore, integrin α2β1 might play a more crucial role in maintaining the mechanical creep properties of the collagen matrix than does integrin α1β1.

Project description:Amyloid fibrils are highly ordered protein aggregates that are associated with several pathological processes, including prion propagation and Alzheimer's disease. A key issue in amyloid science is the need to understand the mechanical properties of amyloid fibrils and fibers to quantify biomechanical interactions with surrounding tissues, and to identify mechanobiological mechanisms associated with changes of material properties as amyloid fibrils grow from nanoscale to microscale structures. Here we report a series of computational studies in which atomistic simulation, elastic network modeling, and finite element simulation are utilized to elucidate the mechanical properties of Alzheimer's Abeta(1-40) amyloid fibrils as a function of the length of the protein filament for both twofold and threefold symmetric amyloid fibrils. We calculate the elastic constants associated with torsional, bending, and tensile deformation as a function of the size of the amyloid fibril, covering fibril lengths ranging from nanometers to micrometers. The resulting Young's moduli are found to be consistent with available experimental measurements obtained from long amyloid fibrils, and predicted to be in the range of 20-31 GPa. Our results show that Abeta(1-40) amyloid fibrils feature a remarkable structural stability and mechanical rigidity for fibrils longer than approximately 100 nm. However, local instabilities that emerge at the ends of short fibrils (on the order of tens of nanometers) reduce their stability and contribute to their disassociation under extreme mechanical or chemical conditions, suggesting that longer amyloid fibrils are more stable. Moreover, we find that amyloids with lengths shorter than the periodicity of their helical pitch, typically between 90 and 130 nm, feature significant size effects of their bending stiffness due the anisotropy in the fibril's cross section. At even smaller lengths (50 nm), shear effects dominate lateral deformation of amyloid fibrils, suggesting that simple Euler-Bernoulli beam models fail to describe the mechanics of amyloid fibrils appropriately. Our studies reveal the importance of size effects in elucidating the mechanical properties of amyloid fibrils. This issue is of great importance for comparing experimental and simulation results, and gaining a general understanding of the biological mechanisms underlying the growth of ectopic amyloid materials.

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Unraveling the role of Calcium ions in the mechanical properties of individual collagen fibrils.

Publications

Unraveling the role of Calcium ions in the mechanical properties of individual collagen fibrils.

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