Search results for "Collagen fibril"

showing 6 items of 6 documents

Fracture Mechanics of Collagen Fibrils: Influence of Natural Cross-Links

2013

AbstractTendons are important load-bearing structures, which are frequently injured in both sports and work. Type I collagen fibrils are the primary components of tendons and carry most of the mechanical loads experienced by the tissue, however, knowledge of how load is transmitted between and within fibrils is limited. The presence of covalent enzymatic cross-links between collagen molecules is an important factor that has been shown to influence mechanical behavior of the tendons. To improve our understanding of how molecular bonds translate into tendon mechanics, we used an atomic force microscopy technique to measure the mechanical behavior of individual collagen fibrils loaded to failu…

AdultMaleTailMechanical PhenomenaBiophysicsModulusFibrilta3111Collagen fibrilPatellar LigamentTensile StrengthUltimate tensile strengthmedicineAnimalsHumansMolecular Machines Motors and Nanoscale Biophysicsta315Mechanical PhenomenaChemistryFracture mechanicsta3141AnatomyHydrogen-Ion ConcentrationMiddle Agedmusculoskeletal systemTendonBiomechanical PhenomenaRatsmedicine.anatomical_structureSolubilityBiophysicsCollagenType I collagenBiophysical Journal
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Mechanical Properties of Human Patellar Tendon at the Hierarchical levels of Tendon and Fibril

2012

Tendons are strong hierarchical structures, but how tensile forces are transmitted between different levels remains incompletely understood. Collagen fibrils are thought to be primary determinants of whole tendon properties, and therefore we hypothesized that the whole human patellar tendon and its distinct collagen fibrils would display similar mechanical properties. Human patellar tendons ( n = 5) were mechanically tested in vivo by ultrasonography. Biopsies were obtained from each tendon, and individual collagen fibrils were dissected and tested mechanically by atomic force microscopy. The Young's modulus was 2.0 ± 0.5 GPa, and the toe region reached 3.3 ± 1.9% strain in whole patellar …

AdultMalemusculoskeletal diseasesMaterials sciencePhysiologymacromolecular substancesFibrilMicroscopy Atomic ForceCollagen fibrilPatellar LigamentPhysiology (medical)Elastic ModulusUltimate tensile strengthMicroscopymedicineHumansAtomic force microscopyta1182ta3141Anatomymusculoskeletal systemPatellar tendonTendonBiomechanical Phenomenamedicine.anatomical_structureCollagenStress Mechanical
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Do More Highly Organized Collagen Fibrils Increase Bone Mechanical Strength in Loss of Mineral Density After One-Year Running Training?

1999

The aim of this study was to evaluate the effects of long-term running training on the structural properties of bone. Ten beagle dogs ran according to a strenuous progressive program (up to 40 km/day) for 1 year. At the end of the training program, there was a significant reduction in bone mineral density (up to 9.7%) in the vertebrae of the runner dogs as compared with 10 sedentary control dogs. Polarized light microscopy of the vertebral trabecular bone, however, displayed proportionally higher retardation values of the collagen network of the runner dogs than of the sedentary dogs, suggesting a reorganization in a more parallel manner in the collagen fibrils. The concentration and cross-…

Bone mineralTime FactorsEndocrinology Diabetes and Metabolismmedicine.medical_treatmentAnatomyBiologyBeagleBone and BonesBiomechanical PhenomenaRunningCollagen fibrilDogsMineral densityBone DensityPhysical Conditioning AnimalCollagen networkMechanical strengthCarnivoramedicineAnimalsFemaleOrthopedics and Sports MedicineCollagenhuman activitiesReduction (orthopedic surgery)Journal of Bone and Mineral Research
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X-ray investigations of the superstructure of collagen

2008

When compared with results from humid fibers, characteristic changes of the SAXS-pattern taken from dried collagen fibers have been observed. The average lateral width of the various reflexions increases with the order of reflexion whereby a fluctuation is superimposed, the type of which cannot easily be related to the reflexion order. Moreover, each of the reflexions is obviously laterally split into three components. An explanation of these characteristics can be given with the aid of a distinct model, assuming that the collagen fibrils have definitely varying diameters along their axis, whereby paracrystalline distortions appear, represented by nematic fluctuations. Additionally, there i…

Electron density distributionMaterials scienceCondensed matter physicsLiquid crystalX-rayParacrystallineSuperstructure (condensed matter)Collagen fibril
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In vitro testing the potential of a novel chimeric igg variant for inhibiting collagen fibrils formation in recurrent hereditary gingival fibromatosi…

2014

Gingival fibromatosis is a progressive enlargement of the gingiva. It may hinder oral cavity hygiene and result in underlying bone loss. The long-term benefits of surgery cannot be predicted. On the other hand, alternative, efficient and non-invasive methods are not available at present. The aim of this study was to test the inhibitory effects of a chimeric IgG variant on collagen fibril formation in the cell culture of gingival fibroblasts taken from a patient with hereditary gingival fibromatosis with a high propensity for recurrence. Gingival biopsies were collected from the mandibular gingiva and used for histological evaluation as well as to establish a fibroblast culture. A histologic…

hereditary gingival fibromatosisrecurrencecollagen fibrilschimeric antibodyJournal of Physiology and Pharmacology
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Interactions of α2β1 integrin and its ligands, type I collagen and echovirus 1

2015

integriinitreseptoritenterovirusintegrinspektroskopiakollageenitlipiditkollageenisäikeetsolukalvotenteroviruksetcollagen fibrilsRaman spectroscopylipid membranesECHO-viruksetsoluväliaineendosytoosimolecular interactions
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