Cathepsin

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[[Cathepsin]] (CTS) is a protease which becomes activated at low pH. It is found in lysosomes. Members of the CTS group are denoted as CTSA, CTSB etc and cleave proteins at different peptide bonds. The CTSs are expressed as an inactive precursor '''pro-CTS''' (PCTS) which becomes active when a long residue prosegment is cleaved off producing the mature CTS (MCTS).<ref>PMID:15751268</ref> For details on pro-CTS see [[Molecular Playground/Human PPCA]].
[[Cathepsin]] (CTS) is a protease which becomes activated at low pH. It is found in lysosomes. Members of the CTS group are denoted as CTSA, CTSB etc and cleave proteins at different peptide bonds. The CTSs are expressed as an inactive precursor '''pro-CTS''' (PCTS) which becomes active when a long residue prosegment is cleaved off producing the mature CTS (MCTS).<ref>PMID:15751268</ref> For details on pro-CTS see [[Molecular Playground/Human PPCA]].
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*'''CTS B, F, H, L, L1, L2''' are cysteine proteases.<br />
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*'''CTS B, F, H, L, L1, L2 or V''' are cysteine proteases.<br />
*'''CTS D, E''' are aspartyl proteases which degrade insulin.<br />
*'''CTS D, E''' are aspartyl proteases which degrade insulin.<br />
*'''CTS G''' is a serine protease with activity similar to chymotrypsin C.<br />
*'''CTS G''' is a serine protease with activity similar to chymotrypsin C.<br />

Current revision

human cathepsin B complex with inhibitor 3ai8

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References

  1. Nomura T, Katunuma N. Involvement of cathepsins in the invasion, metastasis and proliferation of cancer cells. J Med Invest. 2005 Feb;52(1-2):1-9. PMID:15751268
  2. Mirkovic B, Renko M, Turk S, Sosic I, Jevnikar Z, Obermajer N, Turk D, Gobec S, Kos J. Novel Mechanism of Cathepsin B Inhibition by Antibiotic Nitroxoline and Related Compounds. ChemMedChem. 2011 May 20. doi: 10.1002/cmdc.201100098. PMID:21598397 doi:10.1002/cmdc.201100098

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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