Gelatinase is the main matrix metalloproteinase involved in granuloma-induced cartilage degradation.
This study was performed to characterize the matrix metalloproteinases (MMPs) produced during the degradation of cotton-wrapped cartilage, implanted into the murine air pouch. One, two or three weeks following cartilage implantation, proteins were extracted from the granulation tissue and MMP activities were measured. Although collagenase-, gelatinase- and stromelysin-like activities were detected at each time point, gelatinase activity was by far the most prominent. These enzymes were inhibited by EDTA, but not by NEM or PMSF, indicating that these proteinases were metalloproteinases. Gelatin zymography revealed several lysis zones amongst which a major 92-kDa band shifted to 83- and 68-kDa species during the course of implantation. The emergence of these species coincided with enhanced gelatinolytic activity and collagen loss from the implanted cartilage.
Trancart
M M
MM
Centre de Recherche Jacques Logeais, Trappes, France.
Chalmeigne
N
N
Girardot
C
C
Zarpanelian
C
C
Prigent
D
D
D000818:Animals; D002357:Cartilage Diseases / Q000378:metabolism*; D002358:Cartilage, Articular / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D018093:Gelatinases; D006099:Granuloma / Q000378:metabolism*; D008297:Male; D008666:Metalloendopeptidases / Q000378:metabolism*; D051379:Mice; D010662:Phenylmercuric Acetate / Q000031:analogs & derivatives / Q000494:pharmacology; D051381:Rats; D017207:Rats, Sprague-Dawley
C010024:4-aminophenylmercuriacetate; D010450:Endopeptidases; D018093:Gelatinases; D008666:Metalloendopeptidases; D010662:Phenylmercuric Acetate