Induction of a novel gelatinolytic activity in synovial tissue of patients with rheumatoid arthritis.
Gelatinolytic activity induced by longtime incubation at 37 degrees C was found in extracts of rheumatoid synovial tissues. The enzyme activity was assessed by gelatin zymography and 3H-gelatin degradation assay. The observed enzyme had different characteristics from matrix metalloproteinases; it did not require metal ions for activity. However, metallocheltors blocked activation and addition of some metal ions restored the activation. The molecular size of the enzyme was changed time-dependently. The approximate molecular weight of the first enzyme produced by incubation was 65 kDa and it was converted to a broad size molecule with a molecular weight of 50 kDa after further incubation. Substrate specificity was detected for denatured collagen types I, II, III and IV.
Watanabe
Y
Y
Department of Pathophysiology and Biochemistry, Hokkaido College of Pharmacy, Otaru-shi, Japan. yasu-w@hokuyakudai.ac.jp
Yamaguchi
R
R
Iwaki-Egawa
S
S
Fujimoto
Y
Y
Matsuno
H
H
D001172:Arthritis, Rheumatoid / Q000201:enzymology*; D004790:Enzyme Induction; D005780:Gelatin / Q000378:metabolism*; D018093:Gelatinases / Q000096:biosynthesis / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D013583:Synovial Membrane / Q000201:enzymology*
D005780:Gelatin; D018093:Gelatinases