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Jacqueline M. Lankelma Daniëlle M. Voorend Temo Barwari Joris Koetsveld Anne H. Van der Spek Alexander P.N.A. De Porto Geeske Van Rooijen Cornelis J.F. Van Noorden 《Life sciences》2010,86(7-8):225-233
Cathepsin L, a cysteine protease, is considered to be a potential therapeutic target in cancer treatment. Proteases are involved in the development and progression of cancer. Inhibition of activity of specific proteases may slow down cancer progression. In this review, we evaluate recent studies on the inhibition of cathepsin L in cancer. The effects of cathepsin L inhibition as a monotherapy on apoptosis and angiogenesis in cancer are ambiguous. Cathepsin L inhibition seems to reduce invasion and metastasis, but there is concern that selective cathepsin L inhibition induces compensatory activity by other cathepsins. The combination of cathepsin L inhibition with conventional chemotherapy seems to be more promising and has yielded more consistent results. Future research should be focused on the mechanisms and effects of this combination therapy. 相似文献
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Selenium supplementation sensitizes renca cells to tert-butylhydroperoxide induced loss of viability
Mouse renal carcinoma (renca) cells growing exponentially in foetal bovine serum (1%) supplemented with selenium (1 microM, sodium selenite) were exposed to oxidative insult. It was found that glutathione peroxidase activity increased (44%), while the activities of catalase, glutathione disulfide reductase, and level of total glutathione did not change due to selenium supplementation. Selenium supplementation made renca cells susceptible to tert-butylhydroperoxide induced cell death, while it did not affect the viability when the cells were exposed to hydrogen peroxide. It suggested that the contribution of glutathione peroxidase in antioxidant defense mechanism of renca cells was possibly not crucial and the function of catalase might be important especially against hydrogen peroxide. 相似文献
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Having been activated with glutaraldehyde, modified poly(ethylene terephthalate) grafted acrylamide fiber was used for the
immobilization of horseradish peroxidase (HRP). Both the free HRP and the immobilized HRP were characterized by determining
the activity profile as a function of pH, temperature, thermal stability, effect of organic solvent and storage stability.
The optimum pH values of the enzyme activity were found as 8 and 7 for the free HRP and the immobilized HRP respectively.
The temperature profile of the free HRP and the immobilized HRP revealed a similar behaviour, although the immobilized HRP
exhibited higher relative activity in the range from 50 to 60 °C. The immobilized HRP showed higher storage stability than
the free HRP. 相似文献
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