A note upon tensile stresses in the collagen fibers of articular cartilage

1965 ◽  
Vol 3 (4) ◽  
pp. 447-450 ◽  
Author(s):  
J. M. Zarek ◽  
J. Edwards
Keyword(s):  
Articular Cartilage ◽  
Collagen Fibers ◽  
Tensile Stresses

A Review of the Collagen Orientation in the Articular Cartilage

Cartilage ◽  
2021 ◽  
pp. 194760352098877
Author(s):  
Roy D. Bloebaum ◽  
Andrew S. Wilson ◽  
William N. Martin
Keyword(s):  
Surface Layer ◽  
Articular Cartilage ◽  
Fiber Orientation ◽  
Collagen Fiber ◽  
Articular Surface ◽  
Imaging Techniques ◽  
Collagen Fibers ◽  
Deep Zone ◽  
Collagen Fiber Orientation ◽  
Critical Point Drying

Objective There has been a debate as to the alignment of the collagen fibers. Using a hand lens, Sir William Hunter demonstrated that the collagen fibers ran perpendicular and later aspects were supported by Benninghoff. Despite these 2 historical studies, modern technology has conflicting data on the collagen alignment. Design Ten mature New Zealand rabbits were used to obtain 40 condyle specimens. The specimens were passed through ascending grades of alcohol, subjected to critical point drying (CPD), and viewed in the scanning electron microscope. Specimens revealed splits from the dehydration process. When observing the fibers exposed within the opening of the splits, parallel fibers were observed to run in a radial direction, normal to the surface of the articular cartilage, radiating from the deep zone and arcading as they approach the surface layer. After these observations, the same samples were mechanically fractured and damaged by scalpel. Results The splits in the articular surface created deep fissures, exposing parallel bundles of collagen fibers, radiating from the deep zone and arcading as they approach the surface layer. On higher magnification, individual fibers were observed to run parallel to one another, traversing radially toward the surface of the articular cartilage and arcading. Mechanical fracturing and scalpel damage induced on the same specimens with the splits showed randomly oriented fibers. Conclusion Collagen fiber orientation corroborates aspects of Hunter’s findings and compliments Benninghoff. Investigators must be aware of the limits of their processing and imaging techniques in order to interpret collagen fiber orientation in cartilage.

India Ink Pinprick Experiments on Surface Organization of Cricoarytenoid Joints

1986 ◽  
Vol 29 (4) ◽  
pp. 544-548 ◽  
Author(s):  
Joel C. Kahane ◽  
Alice R. Kahn
Keyword(s):  
Articular Cartilage ◽  
Collagen Fiber ◽  
Collagen Fibers ◽  
Articular Surfaces ◽  
India Ink ◽  
Age Related ◽  
Cricoarytenoid Joint ◽  
Mechanical Factors ◽  
Fiber Organization

Collagen fiber organization in the articular surfaces of the cricoarytenoid joint (CAJ) was studied using a pinpricking technique used in biomechanical research in orthopedics. Four male human formalin preserved specimens (3 months to 20 years) and 6 male freshly autopsied specimens (19 to 30 yrs) were studied. Specimens were dissected using the stereomicroscope. Distinctive patterns of articular cartilage slits reflect the orientation of collagen fibers in the cricoid and arytenoid articular surfaces. The orientation of the collagen fibers reinforces the articular surfaces along the principle path of CAJ motion. No age related differences were found. This suggests that the orientation of collagen fibers in the CAJ articular surfaces is prenatally determined rather than significantly influenced by postnatal mechanical factors.

On the Indentation Testing of Articular Cartilage: Determination of the Effective Poisson’s Ratio Using Two Different-Sized Punches

2008 ◽  
Author(s):  
Eugene T. Kepich ◽  
Roger C. Haut
Keyword(s):  
Articular Cartilage ◽  
Poisson’S Ratio ◽  
Direct Determination ◽  
Collagen Fibers ◽  
Poisson's Ratio ◽  
Compression Tests ◽  
Unconfined Compression ◽  
Collagen Network ◽  
Lateral Expansion

Effective Poisson’s ratio (EPR) of articular cartilage in compression is an important parameter, which is inversely correlated with stiffness of the collagen fibers [1]; and thus, if known, could provide valuable information about integrity of the collagen network in the tissue. Unfortunately, direct determination of the EPR by measuring lateral expansion during unconfined compression tests [2], while being effective, due to it’s destructive nature many times is not desired and/or hard to apply in practice. Optically-determined values of equilibrium EPR for bovine humeral articular cartilage using this method are reported to be in range 0.185±0.0065.

Electrostatic Contribution of the Proteoglycans to the In-Plane Shear and Compressive Stiffness of Corneal Stroma

2010 ◽  
Author(s):  
Hamed Hatami-Marbini ◽  
Peter M. Pinsky
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Electrostatic Interactions ◽  
Corneal Stroma ◽  
Collagen Fibers ◽  
Connective Tissues ◽  
Compressive Stiffness ◽  
Electrostatic Contribution ◽  
Repulsive Forces

The extracellular matrix (ECM) is a fibrous structure embedded in an aqueous gel. The mechanical and electrostatic interactions of the ECM constituents, i.e. collagen fibers and proteoglycans (PGs), define the structure and mechanical response of connective tissues (CTs) such as cornea and articular cartilage. Proteoglycans are complex macromolecules consisting of linear chains of repeating gylcosaminoglycans (GAGs) which are covalently attached to a core protein. PGs can be as simple as decorin with a single GAG side chain or as complex as aggrecan with many GAGs. Decorin is the simplest small leucine-rich PG and is the main PG inside the corneal stroma. It has an arch shape and links non-covalently at its concave surface to the collagen fibrils. It has been shown that while collagen fibers inside the extracellular matrix resist the tensile forces, the negatively charged glycosaminoglycans and their interaction with water give compressive stiffness to the tissue. The role of PGs in biomechanical properties of the connective tissues has mainly been studied in order to explore the behavior of articular cartilage [1], which is a CT with large and highly negatively charged PGs, aggrecans. In order to explain the role of PGs in this tissue, it is commonly assumed that their contribution to the CT elasticity is because of both the repulsive forces between negatively charged GAGs and GAG interactions with free mobile charges in the ionic bath. The electrostatic contribution to the shear and compressive stiffness of cartilage is modeled by approximating GAGs as charged rods [1]. The Poisson-Boltzmann equation is used to compute the change in electrical potential and mobile ion distributions which are caused by the macroscopic deformation.

THE ARCHITECTURE OF COLLAGENS IN OSTEOPHYTES: A STUDY BY IMMUNOHISTOCHEMISTRY

1999 ◽  
Vol 03 (03) ◽  
pp. 175-181
Author(s):  
T. O. Alonge ◽  
P. Rooney ◽  
O. O. A. Oni
Keyword(s):  
Articular Cartilage ◽  
Collagen Fibers ◽  
Precursor Cells ◽  
Type Ii ◽  
Intermediate Layers

The collagen architecture of osteophytes has been investigated by immunolocalization of types I, II, III and X collagens. Types I and III were observed in the superficial layers, type II in the superficial and middle layers and type X at the cartilage-bone junction. This pattern of distribution suggests a "maturation" pathway from precursor cells at the surface to cells transforming into bone at the base. The collagen fibers appear to be oriented horizontally in the superficial layers and vertically in the middle or intermediate layers, thus mimicking the architectural arrangement in normal articular cartilage.

The role of viscoelasticity of collagen fibers in articular cartilage: axial tension versus compression

2005 ◽  
Vol 27 (1) ◽  
pp. 51-57 ◽  
Author(s):  
L.P. Li ◽  
W. Herzog ◽  
R.K. Korhonen ◽  
J.S. Jurvelin
Keyword(s):  
Articular Cartilage ◽  
Collagen Fibers ◽  
Axial Tension

A hyperelastic biphasic fiber reinforced model for articular cartilage considering the distribution and orientation of collagen fibers

PAMM ◽  
2013 ◽  
Vol 13 (1) ◽  
pp. 55-56 ◽  
Author(s):  
Daniel Albrecht ◽  
Tim Ricken ◽  
David M. Pierce ◽  
Gerhard A. Holzapfel
Keyword(s):  
Articular Cartilage ◽  
Collagen Fibers ◽  
Fiber Reinforced
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