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Cathepsin L (EC3.4.22.15, Aldrichina grahami cysteine proteinase) is an important lysosomal endopeptidase enzyme which is involved in the initiation of protein degradation.[1][2][3][4] It is a member of the Peptidase C1 family, which play an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis. [5] Cathepsin L has been reported in many organisms including fish,[6] birds and mammals. [7]
^Kirschke, H., Wikstrom, P. and Shaw, E. (1988). "Active center differences between cathepsins L and B: the S1 binding region". FEBS Lett. 228 (1): 128–130. doi:10.1016/0014-5793(88)80600-8. PMID3342870.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^Dickinson DP. Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease, CROBM 2002 13: 238.
^Venkatesh K, Prasanth B, Rajesh P, Annie J.G, Mukesh P, Jesu A (2014). "A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity". Biologia. 39: 395–406. doi:10.2478/s11756-013-0326-8.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^Sevenich L, Pennacchio LA, Peters C, Reinheckel T.Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biol Chem. 2006 Jul;387(7):885-91.
