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Cathepsin L is a lysosomal cysteine protease expressed in most eukaryotic cells. Cathepsin L is known to hydrolyze a number of proteins, including the proform of urokinase-type plasminogen activator, which is activated by Cathepsin L cleavage. Cathepsin L has also been shown to proteolytically inactivate a1-antitrypsin and secretory leucoprotease inhibitor, two major protease inhibitors of the respiratory tract.
Cathepsin L has been implicated in several pathologic processes, including rheumatoid arthritis, muscular dystrophy, Alzheimers, cancer, myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria.
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- Joanna Szumska, Zaina Batool, Alaa Al-Hashimi, Vaishnavi Venugopalan, Vladislav Skripnik, Norbert Schaschke, Matthew Bogyo, Klaudia Brix. (2019). Treatment of Rat Thyrocytes in vitro With Cathepsin B and L Inhibitors Results in Disruption of Primary Cilia Leading to Redistribution of the Trace Amine Associated Receptor 1 to the Endoplasmic Reticulum. Biochimie. doi: 10.1016/j.biochi.2019.07.010
- Jonas Weber, Joseph McInnes, Cise Kizilirmak, Maren Rehders, Maria Qatato, Eva K. Wirth, Ulrich Schweizer, Francois Verrey, Heike Heuer, Klaudia Brix. (2017). Interdependence of thyroglobulin processing and thyroid hormone export in the mouse thyroid gland. European Journal of Cell Biology, doi: 10.1016/j.ejcb.2017.02.002
- Tripti Tamhanea, Brit K. Woltersa, Rukshala Illukkumburaa, Gunhild M. Maelandsmob, Mads H. Haugena, Klaudia Brixa. (2015). Construction of a plasmid coding for green fluorescent protein tagged cathepsin L and data on expression in colorectal carcinoma cells. Data in Brief, doi: 10.1016/j.dib.2015.09.022
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