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Homogenates of 6 samples of human osteoarthritic cartilage were shown to degrade exogenous type XI collagen. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the cleavage products generated by each homogenate were similar, and they were identical to those obtained by cleavage of the substrate with purified gelatinase. Enzyme activity, which was inhibited by EDTA, was greater in extracts of fibrillated osteoarthritic cartilage than in extracts of grossly normal cartilage from the same joint or in extracts of cartilage from joints with osteonecrosis. Activation with APMA enhanced digestion, but breakdown was apparent in extracts of fibrillated osteoarthritic cartilage even without APMA. Enzymatic degradation of type XI collagen could play a significant role in the turnover of articular cartilage in health and disease states.
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
June 1999,
Annals of the rheumatic diseases,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
September 1994,
Osteoarthritis and cartilage,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
July 1982,
Clinical orthopaedics and related research,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
March 1999,
Osteoarthritis and cartilage,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
July 1992,
Arthritis and rheumatism,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
July 2008,
The American journal of pathology,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
November 1991,
Bone and mineral,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
April 1977,
The Journal of clinical investigation,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
October 1995,
Acta orthopaedica Scandinavica. Supplementum,
L P Yu, and
G N Smith, and
K D Brandt, and
W Capello
January 1992,
Connective tissue research,
