scholarly journals Structure and formation of the twisted plywood pattern of collagen fibrils in rat lamellar bone

Microscopy ◽  
2012 ◽  
Vol 61 (2) ◽  
pp. 113-121 ◽  
Author(s):  
Tsuneyuki Yamamoto ◽  
Tomoka Hasegawa ◽  
Muneteru Sasaki ◽  
Hiromi Hongo ◽  
Chihiro Tabata ◽  
...  
Keyword(s):  
Collagen Fibrils ◽  
Lamellar Bone ◽  
Twisted Plywood

Investigation of the three-dimensional orientation of mineralized collagen fibrils in human lamellar bone using synchrotron X-ray phase nano-tomography

2013 ◽  
Vol 9 (9) ◽  
pp. 8118-8127 ◽  
Author(s):  
Peter Varga ◽  
Alexandra Pacureanu ◽  
Max Langer ◽  
Heikki Suhonen ◽  
Bernhard Hesse ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Collagen Fibrils ◽  
Lamellar Bone ◽  
X Ray ◽  
Mineralized Collagen

scholarly journals Homogenized stiffness matrices for mineralized collagen fibrils and lamellar bone using unit cell finite element models

2013 ◽  
Vol 13 (2) ◽  
pp. 437-449 ◽  
Author(s):  
Ana Vercher ◽  
Eugenio Giner ◽  
Camila Arango ◽  
José E. Tarancón ◽  
F. Javier Fuenmayor
Keyword(s):  
Finite Element ◽  
Unit Cell ◽  
Collagen Fibrils ◽  
Finite Element Models ◽  
Lamellar Bone ◽  
Stiffness Matrices ◽  
Mineralized Collagen

Twisted Plywood Pattern of Collagen Fibrils in Teleost Scales: An X-ray Diffraction Investigation

2001 ◽  
Vol 136 (2) ◽  
pp. 137-143 ◽  
Author(s):  
Adriana Bigi ◽  
Manfred Burghammer ◽  
Rosanna Falconi ◽  
Michel H.J Koch ◽  
Silvia Panzavolta ◽  
...  
Keyword(s):  
Collagen Fibrils ◽  
X Ray Diffraction ◽  
X Ray ◽  
Teleost Scales ◽  
Twisted Plywood

scholarly journals Interfibril hydrogen bonding improves the strain-rate response of natural armour

2019 ◽  
Vol 16 (150) ◽  
pp. 20180775 ◽  
Author(s):  
D. Arola ◽  
S. Ghods ◽  
C. Son ◽  
S. Murcia ◽  
E. A. Ossa
Keyword(s):  
Mineral Content ◽  
Loading Rate ◽  
Polar Solvent ◽  
The Body ◽  
Collagen Fibrils ◽  
Tail Region ◽  
Puncture Resistance ◽  
Content Scales ◽  
Intermolecular Bonding ◽  
Twisted Plywood

Fish scales are laminated composites that consist of plies of unidirectional collagen fibrils with twisted-plywood stacking arrangement. Owing to their composition, the toughness of scales is dependent on the intermolecular bonding within and between the collagen fibrils. Adjusting the extent of this bonding with an appropriate stimulus has implications for the design of next-generation bioinspired flexible armours. In this investigation, scales were exposed to environments of water or a polar solvent (i.e. ethanol) to influence the extent of intermolecular bonding, and their mechanical behaviour was evaluated in uniaxial tension and transverse puncture. Results showed that the resistance to failure of the scales increased with loading rate in both tension and puncture and that the polar solvent treatment increased both the strength and toughness through interpeptide bonding; the largest increase occurred in the puncture resistance of scales from the tail region (a factor of nearly 7×). The increase in strength and damage tolerance with stronger intermolecular bonding is uncommon for structural materials and is a unique characteristic of the low mineral content. Scales from regions of the body with higher mineral content underwent less strengthening, which is most likely the result of interference posed by the mineral crystals to intermolecular bonding. Overall, the results showed that flexible bioinspired composite materials for puncture resistance should enrol constituents and complementary processing that capitalize on interfibril bonds.

Effects of EDTA, Hyaluronidase and Collagenase on Epiphyseal Cartilage Matrix

1968 ◽  
Vol 26 ◽  
pp. 56-57
Author(s):  
H. Clarke Anderson ◽  
Priscilla R. Coulter
Keyword(s):  
Light And Electron Microscopy ◽  
Matrix Vesicles ◽  
Cartilage Matrix ◽  
Collagen Fibrils ◽  
Epiphyseal Cartilage ◽  
Dense Matrix ◽  
Type Iv ◽  
Bovine Testicular Hyaluronidase ◽  
The Matrix ◽  
Testicular Hyaluronidase

Epiphyseal cartilage matrix contains fibrils and particles of at least 5 different types: 1. Banded collagen fibrils, present throughout the matrix, but not seen in the lacunae. 2. Non-periodic fine fibrils <100Å in diameter (Fig. 1), which are most notable in the lacunae, and may represent immature collagen. 3. Electron dense matrix granules (Fig. 1) which are often attached to fine fibrils and collagen fibrils, and probably contain protein-polysaccharide although the possibility of a mineral content has not been excluded. 4. Matrix vesicles (Fig. 2) which show a selective distribution throughout the epiphysis, and may play a role in calcification. 5. Needle-like apatite crystals (Fig. 2).Blocks of formalin-fixed epiphysis from weanling mice were digested with the following agents in 0.1M phosphate buffer: a) 5% ethylenediaminetetraacetate (EDTA) at pH 8.3, b) 0.015% bovine testicular hyaluronidase (Sigma, type IV, 750 units/mg) at pH 5.5, and c) 0.1% collagenase (Worthington, chromatograhically pure, 200 units/mg) at pH 7.4. All digestions were carried out at 37°C overnight. Following digestion tissues were examined by light and electron microscopy to determine changes in the various fibrils and particles of the matrix.

Banded Structures in the Connective Tissue of Meningioma

1976 ◽  
Vol 34 ◽  
pp. 234-235
Author(s):  
C. N. Sun ◽  
H. J. White
Keyword(s):  
Connective Tissue ◽  
Osmium Tetroxide ◽  
Uranyl Acetate ◽  
Collagen Fibrils ◽  
Lead Citrate ◽  
Connective Tissues ◽  
Native Collagen ◽  
Routine Procedures

Previously, we have reported on extracellular cross-striated banded structures in human connective tissues of a variety of organs (1). Since then, more material has been examined and other techniques applied. Recently, we studied a fibrocytic meningioma of the falx. After the specimen was fixed in 4% buffered glutaraldehyde and post-fixed in 1% buffered osmium tetroxide, other routine procedures were followed for embedding in Epon 812. Sections were stained with uranyl acetate and lead citrate. There were numerous cross striated banded structures in aggregated bundle forms found in the connecfive tissue of the tumor. The banded material has a periodicity of about 450 Å and where it assumes a filamentous arrangement, appears to be about 800 Å in diameter. In comparison with the vicinal native collagen fibrils, the banded material Is sometimes about twice the diameter of native collagen.

Scanning electron microscopic study of collagen fibrillogenesis and extracellular compartmentalization in the chick embryo tendon

1986 ◽  
Vol 44 ◽  
pp. 208-209
Author(s):  
Grace C.H. Yang
Keyword(s):  
Chick Embryo ◽  
Extracellular Space ◽  
Fibroblast Cell ◽  
Collagen Fibrils ◽  
Electron Microscopic ◽  
Voltage Electron ◽  
Scanning Electron Microscopic Study ◽  
Microscopic Studies ◽  
And Function

The size and organization of collagen fibrils in the extracellular matrix is an important determinant of tissue structure and function. The synthesis and deposition of collagen involves multiple steps which begin within the cell and continue in the extracellular space. High-voltage electron microscopic studies of the chick embryo cornea and tendon suggested that the extracellular space is compartmentalized by the fibroblasts for the regulation of collagen fibril, bundle, and tissue specific macroaggregate formation. The purpose of this study is to gather direct evidence regarding the association of the fibroblast cell surface with newly formed collagen fibrils, and to define the role of the fibroblast in the control and the precise positioning of collagen fibrils, bundles, and macroaggregates during chick tendon development.

Platelet Adhesion to Native Collagens Involves Proteoglycans and May Be a Two-Step Process

1987 ◽  
Vol 58 (02) ◽  
pp. 786-789 ◽  
Author(s):  
O Behnke
Keyword(s):  
Electron Microscope ◽  
Platelet Adhesion ◽  
Close Contact ◽  
Blood Platelets ◽  
Collagen Fibrils ◽  
Platelet Membrane ◽  
Step Process ◽  
Rat Blood ◽  
Wide Gap ◽  
Rat Tail

SummaryAdhesion of rat blood platelets to native rat tail collagen fibrils was studied in the electron microscope under conditions that preserved collagen-associated proteoglycans (CAPG). The CAPG molecules were aligned in chain-like configurations that encircled the fibrils with a 65 nm period; they appeared to coat the fibrils completely and extended 60-100 nm away from the fibril. The initial platelet-fibril contact occurred between the platelet glycocalyx and the CAPG of the fibrils i.e. between two surfaces with net-negative charges. When close contact was established between the fibril surface proper and the platelet membrane, CAPG were not identified in the area of contact, and the collagen-platelet distance was reduced to a ~10-12 nm wide gap traversed by delicate links in register with fibril periodicities.

scholarly journals Molecular origin of viscoelasticity in mineralized collagen fibrils

2021 ◽  
Author(s):  
Mario Milazzo ◽  
Alessio David ◽  
Gang Seob Jung ◽  
Serena Danti ◽  
Markus J. Buehler
Keyword(s):  
Collagen Fibrils ◽  
Skeletal System ◽  
Mineralized Tissue ◽  
Molecular Origin ◽  
Mineralized Collagen

Bone is mineralized tissue constituting the skeletal system, supporting and protecting body organs and tissues. In addition to such fundamental mechanical functions, bone also plays a remarkable role in sound...

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