Inhibition of lysosomal cysteine proteases by chrysotherapeutic compounds




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Details zur Publikation

Untertitel: a possible mechanism for the antiarthritic activity of Au(I)
Autorenliste: Chircorian A, Barrios AM
Verlag: Elsevier
Jahr der Veröffentlichung: 2004
Bandnummer: 14
Heftnummer: 20
Erste Seite: 5113
Letzte Seite: 5116
Seitenumfang: 4
ISSN: 0960-894X
Sprachen: Englisch-Vereinigtes Königreich (EN-GB)


Although Au(I) complexes have been used to treat rheumatoid arthritis for over 75 years, their mechanism of action is still poorly understood. A family of enzymes responsible for joint destruction in rheumatoid arthritis, the cathepsins, has been discussed as a possible biological target of Au(I). In this study, inhibition of the cathepsins by known Au(I) drugs and related compounds was investigated. The compounds tested inhibited cathepsin activity with IC50 values as low as 600 nM. More typical IC50 values were in the 50-200 muM range. Although the gold complexes are not extremely potent cathepsin inhibitors, it is likely that this inhibition is biologically relevant given the high concentrations of Au(I) in the serum and joints of patients undergoing chrysotherapy. While it is likely that there are multiple targets of Au(I) in vivo, inhibition of the cathepsins would provide protection against the joint destruction that is a hallmark of rheumatoid arthritis and is one possible mechanism for Au(I) antiarthritic activity. (C) 2004 Elsevier Ltd. All rights reserved.


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