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J. Biol. Chem., Vol. 263, Issue 8, 3632-3638, Mar, 1988
TI Morales and VC Hascall
Proteoglycans exist in cartilage as complexes in which many proteoglycan
molecules are bound to a central filament of hyaluronic acid. Many studies
have investigated changes taking place in proteoglycan monomer structure
during cartilage catabolism usually under the assumption that hyaluronic
acid is a relatively inert metabolic component of the complex. In this
paper we present organ culture data supporting a new hypothesis that the
catabolism of proteoglycans and hyaluronic acid are coordinately regulated
by chondrocytes. The data indicates that: 1) newly synthesized hyaluronate
and proteoglycan maintain a nearly constant ratio, almost identical to that
existing for the total chemical amounts of these two components in
cartilage tissue; 2) these two components are catabolized with virtually
identical kinetics; and 3) this catabolic relationship in vitro reflects
the loss of hyaluronate and proteoglycans from native, undissociated
aggregates as isolated from the tissue. We conclude that hyaluronate
catabolism is an integral part of the overall mechanism of proteoglycan
resorption in cartilage and that further understanding of this process may
be key to the elucidation of the regulatory pathways for proteoglycan
resorption in health and disease.
Correlated metabolism of proteoglycans and hyaluronic acid in bovine cartilage organ cultures
Bone Research Branch, National Institute of Dental Research, Bethesda, Maryland 20892.
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