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CTSL1

Official Full Name
cathepsin L1
Background
Cathepsin L is a lysosomal endopeptidase belonging to the papain cysteine protease superfamily. Macrophages and osteoclasts secrete the precursor of cathepsin L, procathepsin L, which is processed to some form of active enzyme by acid, surface activation, or proteolysis. It is then involved in connective tissue degradation and the turnover of extracellular matrix proteins. Procathepsin L is also secreted by many malignantly transformed cells, mRNA, and its protein expression levels, as well as the extent to which it is secreted are correlated to the malignant potential of these cells. As cathepsin L is capable of degrading protein constituents of the extracellular matrix, it may play a crucial role in tumor progression, metastasis, and other disorders involving the destruction of the extracellular matrix. Inhibition of the enzyme or the proenzyme by low molecular weight inhibitors or antibodies and in vivo lead to a suppression of the invasiveness of malignant cells or a decline in their ability to form tumors.
Synonyms
RP11-65B23.1; CATL; CTSL; MEP; cathepsin L; major excreted protein; CTSL1; cathepsin L1; cathepsin L , CTSL; FLJ31037;

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