Cathepsin B, a lysosomal protease, has been proposed to be involved in the progression and metastatic spread of breast cancer.  Associations have been made between high concentrations of cathepsin B and poor patient prognosis in primary breast cancer.  Active cathepsin B localized to the plasma membrane has been shown in invasive bladder tumor cells whereas non-invasive tumor cells have cathepsin B confined to the lysosomes.  This suggests that membrane associated cathepsins may participate in tumor invasion.  Specific proteinase inhibitors could lead to the development of theraputic agents for treatment of many types of carcinomas.  Described is the design and synthesis of inhibitors containing C-terminal argininal thiosemicarbazones.  Inhibition data for these cathepsin B inhibitors is reported using N-Carbobenzoxy-L-Phenylalanyl-Arginine-4-nitroanilide hydrochloride as the substrate. Supported by National Cancer Institute at NIH (Grant No. 3R15CA086933-04 and 3R15CA086933-04A2S1) and Western Illinois University.

New cathepsin B inhibitors containing argininal thiosemicarbazones

243rd National Meeting (2012)

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