MOL 45682 1 In vivo Inhibition of Serine Protease Processing Requires a High Fractional Inhibition of Cathepsin C
نویسندگان
چکیده
NM, JR, DE, DR, MP: Department of Biochemistry and Molecular Biology, Merck Frosst Centre for Therapeutic Research, Kirkland, Quebec, Canada. DG, CB, TR: Department of Medicinal Chemistry, Merck Frosst Centre for Therapeutic Research, Kirkland, Quebec, Canada KO, SW, DN: Department of Comparative Medicine, Merck Frosst Centre for Therapeutic Research, Kirkland, Quebec, Canada. Molecular Pharmacology Fast Forward. Published on March 6, 2008 as doi:10.1124/mol.108.045682
منابع مشابه
In vivo inhibition of serine protease processing requires a high fractional inhibition of cathepsin C.
Inhibition of cathepsin C, a dipeptidyl peptidase that activates many serine proteases, represents an attractive therapeutic strategy for inflammatory diseases with a high neutrophil burden. We recently showed the feasibility of blocking the activation of neutrophil elastase, cathepsin G, and proteinase-3 with a single cathepsin C selective inhibitor in cultured cells. Here we measured the frac...
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