Inhibition of lysosomal cysteine proteases by chrysotherapeutic compounds

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Subtitle: a possible mechanism for the antiarthritic activity of Au(I)
Author list: Chircorian A, Barrios AM
Publisher: Elsevier
Publication year: 2004
Volume number: 14
Issue number: 20
Start page: 5113
End page: 5116
Number of pages: 4
ISSN: 0960-894X
Languages: English-Great Britain (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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