Michael S. McQueney

TL;DR: It is shown that the activity of cathepsin K alone is sufficient to dissolve completely insoluble collagen of adult human cortical bone and is likely to be responsible for the key role of cat hepsIn K in bone resorption.

TL;DR: The in vitro activation of the recombinant purified human cathepsin K was an autocatalytic process and could be fully processed to mature enzyme by including one equivalent of wild-type procathepsIn K in the activation mixture.

TL;DR: Comparison with the crystal structure of the most closely related MMP, MMP2, indicates that the conformations of residues in the active-site cleft and in the cysteine-switch peptide of the prodomain are highly conserved and that design of MMP9-specific inhibitors will be challenging.

TL;DR: Initial kinetic studies suggest the possibility of irreversible and reversible active-site modification in cathepsin K, a cysteine protease unique to osteoclasts, and promising leads for therapeutic agents for the treatment of osteoporosis.

TL;DR: The structure of human cathepsin K, a potential target for treatment of osteoporosis, reveals active site differences with homologous cysteine proteinases that should enable the design of cathePSin K selective inhibitors.