TY - JOUR
T1 - Novel aspects to the structure of rabbit articular cartilage
AU - Wade, S.
AU - Richards, R. G.
AU - Ito, K.
AU - ap Gwynn, Iolo A.
N1 - ap Gwynn, I., Wade, S., Ito, K., Richards, R.G. (2002). Novel aspects to the structure of rabbit articular cartilage. European Cells and Materials, 4, 18-29.
Sponsorship: AO Research Fund (AORF)
PY - 2002
Y1 - 2002
N2 - Applying cryo and modified chemical preparation techniques,
mainly for scanning electron microscopy, revealed
entirely new aspects to the structure of the radial zone of
rabbit tibial plateau articular cartilage. The aggrecan component
of the extracellular matrix was contained radially
in columns, each with a diameter of 1-3μm, by a tightly
packed matrix of collagen fibrils. The collagen fibrils were
arranged radially, some straight and others in an opposed
spiral arrangement, with regularly repeating patterns. This
organization existed in the regions surrounding the columns
of chondrocytes, known as chondrons. The load
bearing property of the tissue was explained by the directed
flow and containment of the interstitial fluid, modulated
by the protein-carbohydrate complexes, along these
collagen bounded tubular structures. The reason why such
a structure has not been described previously may be that
it is not retained by aldehyde fixation followed by dehydration,
the method commonly used for tissue preparation
for electron microscopy.
AB - Applying cryo and modified chemical preparation techniques,
mainly for scanning electron microscopy, revealed
entirely new aspects to the structure of the radial zone of
rabbit tibial plateau articular cartilage. The aggrecan component
of the extracellular matrix was contained radially
in columns, each with a diameter of 1-3μm, by a tightly
packed matrix of collagen fibrils. The collagen fibrils were
arranged radially, some straight and others in an opposed
spiral arrangement, with regularly repeating patterns. This
organization existed in the regions surrounding the columns
of chondrocytes, known as chondrons. The load
bearing property of the tissue was explained by the directed
flow and containment of the interstitial fluid, modulated
by the protein-carbohydrate complexes, along these
collagen bounded tubular structures. The reason why such
a structure has not been described previously may be that
it is not retained by aldehyde fixation followed by dehydration,
the method commonly used for tissue preparation
for electron microscopy.
M3 - Article
VL - 4
SP - 18
EP - 29
JO - European Cells and Materials
JF - European Cells and Materials
ER -