A synthetic peptide metalloproteinase inhibitor, but not TIMP, prevents the breakdown of proteoglycan within articular cartilage in vitro.
IL1-stimulated pig articular cartilage fragments were cultured in the and absence of various metalloproteinase inhibitors. Tissue inhibitor of metalloproteinases (TIMP) was unable to stop the release of proteoglycan from the cartilage. Incubation of cartilage with a potent synthetic metalloproteinase inhibitor inhibited the release of proteoglycan in a dose-dependent fashion. The results suggest that low-M(r) metalloproteinase inhibitors may have therapeutic potential in limiting connective tissue breakdown in conditions such as rheumatoid arthritis.
Andrews
H J
HJ
Rheumatology Research Unit, Addenbrooke's Hospital, Cambridge, UK.
Plumpton
T A
TA
Harper
G P
GP
Cawston
T E
TE
D000818:Animals; D002358:Cartilage, Articular / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D006023:Glycoproteins / Q000494:pharmacology*; D066298:In Vitro Techniques; D007375:Interleukin-1 / Q000494:pharmacology; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D011480:Protease Inhibitors / Q000494:pharmacology; D011509:Proteoglycans / Q000378:metabolism*; D013552:Swine; D019714:Tissue Inhibitor of Metalloproteinases
D006023:Glycoproteins; D007375:Interleukin-1; D011480:Protease Inhibitors; D011509:Proteoglycans; D019714:Tissue Inhibitor of Metalloproteinases; D008666:Metalloendopeptidases