scholarly journals Deep vertical collagen fibrils play a significant role in mechanics of articular cartilage

2008 ◽  
Vol 26 (5) ◽  
pp. 608-615 ◽  
Author(s):  
R. Shirazi ◽  
A. Shirazi-Adl
Keyword(s):  
Articular Cartilage ◽  
Significant Role ◽  
Collagen Fibrils

scholarly journals Efficacy of Chemical Processes in Collagen Fibrils of Articular Cartilage is Osmolality Dependent

2017 ◽  
Vol 25 ◽  
pp. S275-S276
Author(s):  
B. Pouran ◽  
P. Rahnamay Moshtagh ◽  
V. Arbabi ◽  
J. Ruberti ◽  
A. Zadpoor ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Chemical Processes ◽  
Collagen Fibrils

Collagen fibrils are differently organized in weight-bearing and not-weight-bearing regions of pig articular cartilage

2000 ◽  
Vol 287 (5) ◽  
pp. 346-352 ◽  
Author(s):  
Santiago Gomez ◽  
Renato Toffanin ◽  
Sigrid Bernstorff ◽  
Milena Romanello ◽  
Heinz Amenitsch ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Weight Bearing ◽  
Collagen Fibrils

scholarly journals Susceptibility tensor imaging and tractography of collagen fibrils in the articular cartilage

2017 ◽  
Vol 78 (5) ◽  
pp. 1683-1690 ◽  
Author(s):  
Hongjiang Wei ◽  
Eric Gibbs ◽  
Peida Zhao ◽  
Nian Wang ◽  
Gary P. Cofer ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Collagen Fibrils ◽  
Susceptibility Tensor

A Fibril Reinforced Poroelastic Model of Articular Cartilage Including Depth Dependent Material Properties

1999 ◽  
Author(s):  
L. P. Li ◽  
M. D. Buschmann ◽  
A. Shirazi-Adl
Keyword(s):  
Articular Cartilage ◽  
Regional Differences ◽  
Articular Surface ◽  
Collagen Fibrils ◽  
Superficial Zone ◽  
Cartilage Surface ◽  
Poroelastic Model ◽  
Oriented Parallel ◽  
Strain Dependent ◽  
Very High

Abstract Articular cartilage is a highly nonhomogeneous, anisotropic and multiphase biomaterial consisting of mainly collagen fibrils, proteoglycans and water. Noncalcified cartilage is morphologically divided into three zones along the depth, i.e. superficial, transitional and radial zones. The thickness, density and alignment of collagen fibrils vary from the superficial zone, where fibrils are oriented parallel to the articular surface, to the radial zone where fibrils are perpendicular to the boundary between bone, and cartilage. The concentration of proteoglycans increases with the depth from the cartilage surface. These regional differences have significant implications to the mechanical function of joints, which is to be explored theoretically in the present work by considering inhomogeneity along the cartilage depth. A nonlinear fibril reinforced poroelastic model is employed as per Li et al. (1999) in which the collagen fibrils were modeled as a distinct constituent whose tensile stiffness was taken to be very high and be strain dependent but whose compressive stiffness was neglected.

The importance of superficial collagen fibrils for the function of articular cartilage

2013 ◽  
Vol 13 (1) ◽  
pp. 41-51 ◽  
Author(s):  
Sayyed Mohsen Hosseini ◽  
Yabin Wu ◽  
Keita Ito ◽  
Corrinus C. van Donkelaar
Keyword(s):  
Articular Cartilage ◽  
Collagen Fibrils

The ultrastructural organization of proteoglycans and collagen in human and rabbit scleral matrix

1985 ◽  
Vol 74 (1) ◽  
pp. 95-104
Author(s):  
R.D. Young
Keyword(s):  
Electron Microscopy ◽  
Articular Cartilage ◽  
Collagen Fibrils ◽  
Ultrastructural Organization ◽  
Connective Tissues ◽  
Collagen Organization ◽  
Band Position ◽  
Cuprolinic Blue ◽  
Relationship Of ◽  
Fibril Diameter

The distribution of proteoglycans and their association with collagen fibrils were studied in human and rabbit sclera following fixation of tissue in glutaraldehyde containing Cuprolinic Blue, a specific stain for proteoglycans when used in the presence of critical concentrations of electrolytes. Proteoglycans were visualized by electron microscopy as fine filaments, approximately 54 nm in length and 5 nm in diameter, associated with the d band in the gap zone of the periodic collagen banding pattern. Filaments were present in three orientations: (1) radiating from the d band to associate with corresponding sites on adjacent collagen fibrils; (2) encircling the collagen fibril at the d band position; and (3) lying along the fibril axis, often linking consecutive d bands. No difference was apparent between the proteoglycan-collagen organization in human and rabbit sclera. A similar arrangement of proteoglycan filaments in association with the d band was also evident throughout all levels of the sclera in spite of considerable variations in fibril diameter from inner to outer stroma. Furthermore, the specific relationship of proteoglycans with the collagen fibrils in sclera closely resembled that previously described in tendon and in articular cartilage, lending support to the view that the association of proteoglycans with collagen may be consistent in a majority of connective tissues, irrespective of their diverse functional specializations.

scholarly journals Submicroscopic structure of canine articular cartilage

2012 ◽  
Vol 49 (No. 6) ◽  
pp. 207-216 ◽  
Author(s):  
D. Horky ◽  
F. Tichy
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Articular Cartilage ◽  
Collagen Fibrils ◽  
Granular Endoplasmic Reticulum ◽  
Pericellular Matrix ◽  
Submicroscopic Structure ◽  
Intercellular Matrix ◽  
Cartilage Layer ◽  
Transport Vesicles

Canine articular cartilage was studied in male dogs at age 1, 4, 5 and 8 years. Samples collected from four hip joints and two humeral joints in each age category were processed by standard methods to be examined by scanning and transmission electron microscopy. The cartilage of both joints was similar in structure. In the superficial cartilage layer of one-year-old animals, individual spindle-shaped chondrocytes in the extracellular matrix were, together with associated collagen fibrils, located parallel to the surface. When viewed by scanning electron microscopy, they were distinctly prominent above the surrounding surface. Changes in the thickness and arrangement of both the chondrosynovial membrane and intercellular matrix were apparent in the 4-, 5- and 8-year-old animals, indicating the onset or progression of an osteoarthritic process. The middle cartilage layer in young animals showed elliptical chondrocytes occurring in pairs. The voluminous cytoplasm contained a great amount of granular endoplasmic reticulum, a large Golgi complex and numerous transport vesicles. The pericellular matrix, up to 1 µm thick, was composed of aperiodic fibrils. In the old animals the pericellular matrix was absent and was replaced by thick collagen fibrils with a marked periodicity. The deep cartilage layer in young dogs included groups of three to four chondrocytes situated in a common territory. The cytoplasm contained distinct bundles of intermediary filaments. The pericellular matrix occasionally formed septa between adjoining cells. The intracellular matrix included bundles of collagen fibrils arranged in a matted structure. In the old animals aggregation of chondrocytes into groups almost disappeared. The cytoplasm showed only short cisternae of granular endoplasmic reticulum, small numbers of mitochondria and transport vesicles, frequent lipid droplets and small glycogen deposits. The intercellular matrix consisted of only short collagen fibrils with no distinct periodicity.

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