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J. Cell Biol.,
Volume 142, Number 1, July 13, 1998 285-294
Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Waldeyerstrasse 15, D-48149 Münster,
Federal Republic of Germany
Cartilage fibrils contain collagen II as the
major constituent, but the presence of additional components, minor collagens, and noncollagenous glycoproteins is thought to be crucial for modulating several
fibril properties. We have examined the distribution of
two fibril constituents
decorin and collagen IXin
samples of fibril fragments obtained after bovine cartilage homogenization. Decorin was preferentially associated with a population of thicker fibril fragments
from adult articular cartilage, but was not present on
the thinnest fibrils. The binding was specific for the gap regions of the fibrils, and depended on the decorin core
protein. Collagen IX, by contrast, predominated in the
population with the thinnest fibrils, and was scarce on
wider fibrils. Double-labeling experiments demonstrated the coexistence of decorin and collagen IX in
some fibrils of intermediate diameter, although most
fibril fragments from adult cartilage were strongly positive for one component and lacked the other. Fibril
fragments from fetal epiphyseal cartilage showed a different pattern, with decorin and collagen IX frequently
colocalized on fragments of intermediate and large diameters. Hence, the presence of collagen IX was not
exclusive for fibrils of small diameter. These results establish that articular cartilage fibrils are biochemically
heterogeneous. Different populations of fibrils share
collagen II, but have distinct compositions with respect
to macromolecules defining their surface properties.
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