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benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pro-neuropeptide Y + H2O
neuropeptide Y + ?
cathepsin L cleaves pro-neuropeptide Y (1-70) to generate neuropeptide Y-Gly (1-38) and the COOH-terminal peptide fragment (39-70)
-
-
?
BAM-22P + H2O
(Met)enkephalin + ?
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Cholecystokinin + H2O
?
-
-
-
-
?
chromogranin A + H2O
catestatin
-
-
-
-
?
Disrupted in renal carcinoma 2 + H2O
?
-
the substrate is proteolytically processed into a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment, respectively. The cleavage site is between amino acid residues 214 and 261
-
-
?
Gelatin + H2O
?
-
-
-
-
?
histone H3 + H2O
?
-
during embryonic stem cell differentiation, histone H3 is proteolytically cleaved at its N-terminus. H3 cleavage may be regulated by covalent modifications present on the histone tail itself
-
-
?
Insulin B-chain + H2O
?
-
preferential cleavage at: Glu13-Ala14, Leu17-Val18, and Tyr26-Thr27
-
-
?
Nipah virus fusion protein + H2O
?
-
cathepsin L specifically converts Nipah virus fusion protein to a mature and fusogenic form
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
pro-dynorphin + H2O
?
-
-
-
-
?
pro-enkephalin + H2O
enkephalin + ?
-
-
-
-
?
Pro-opiomelanocortin + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
additional information
?
-
additional information
?
-
upon interferon-gamma activation of peritoneal macrophages, enzymatic activityof cathepsin L is specifically inhibited, such that cathepsin S mediates Ii degradation and regulates MHC class II maturation
-
?
additional information
?
-
-
p4165aa, a 65 amino acid segment of the p41 splice variant of major histocompatibility complex class II-associated invariant chain, stabilizes cathepsin L in the extracellular environment and induces a local decrease in the concentration of matrix-degrading enzymes during inflammation. Through its interaction with cathepsin L, complex class II-associated invariant chain Ii may control the migratory response of antigen-presenting cells and/or the recruitment of effectors of the inflammatory response
-
?
additional information
?
-
-
cathepsin L elevates alpha-secretase activity, thereby suppressing amyloid precursor protein Abeta42 level. Cathepsin L reduces the formation of Abeta42 peptides by cleaving amyloid precursor protein within the Abeta peptide sequence. In addition, both cathepsins B and L degrade Abeta42 into less toxic Abeta peptides
-
-
?
additional information
?
-
-
cathepsin L expression levels regulate cell responsiveness to IGF-type I, function for cathepsin L in the control of the tumorigenic/metastatic phenotype
-
-
?
additional information
?
-
-
cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
-
-
?
additional information
?
-
cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
-
-
?
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malfunction
-
ablation of cathepsin L in a cystatin M/E-deficient background (Cst6-/-Ctsl-/-double-knockout mice) restores viability and results in normalization of stratum corneum morphology
malfunction
-
cathepsin L knockout mouse brains show extensive decreases in dynorphin A, dynorphin B, and alpha-neoendorphin that are reduced by 75%, 83%, and 90%, respectively
malfunction
-
deficiency for cathepsin L promotes enhanced tumor progression and metastasis in mouse epidermis, Ctsl deficiency potentiates neoplastic progression in K14-HPV16 transgenic mice but does not alter immune cell infiltration or angiogenesis during neoplastic progression in HPV16 mice
malfunction
-
in cathepsin L knockout mice, cholecystokinin 8 levels are substantially reduced in brain cortex by an average of 75%
malfunction
-
inhibition of cathepsin L by specific inhibitors results in a significant decrease of intraocular neovascularization, a similar decrease of neovascularization is found in cathepsin L-deficient mice
malfunction
-
in cathepsin L knockou mice, brain levels of (Met)enkephalin are reduced to 44%, brain levels of neuropeptide Y are reduced to 22%, brain levels of cholecystokinin are reduced to 75%, brain levels of dynorphin A are reduced to 25% , brain levels of dynorphin B are reduced to 17%, brain levels of alpha-neoendorphin are reduced to 10%, brain levels of adrenocorticotropin hormone are reduced to 23%, brain levels of beta-endorphin are reduced to 18%, and brain levels of alpha-MSH are reduced to 7% of the wild type level
physiological function
-
cathepsin L functions as a major protease responsible for cholecystokinin 8 production in mouse brain cortex, and participates with prohormone convertase 1/3 for cholecystokinin 8 production in pituitary cells
physiological function
-
cathepsin L is required for ecotropic murine leukemia virus infection in NIH-3T3 cells
physiological function
-
cathepsin L plays a critical role in intraocular angiogenesis
physiological function
-
cathepsin L plays a prominent role, jointly with PC1/3 and PC2, for production of dynorphins in brain
physiological function
-
Ctsl is critical for the termination of growth factor signaling in the endosomal/lysosomal compartment of keratinocytes and, therefore, functions as an anti-tumor protease
physiological function
-
granule-bound cathepsins are essential for processing perforin to its active form, and CatL is an important, but not exclusive, participant in this process
physiological function
-
the cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea. Activation of cathepsin D and transglutaminase-1 are downstream events, dependent of cathepsin L activity
physiological function
-
cathepsin L in secretory vesicles functions as a key protease for proteolytic processing of proneuropeptides (including enkephalin, neuropeptide Y, dynorphins, cholecystokinin, and others) and prohormones into active neuropeptides that are released to mediate cell-cell communication in the nervous system for neurotransmission. Cathepsin L is a key protease responsible for cholecystokinin 8 production in brain
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Troen, B.R.; Gal, S.; Gottesman, M.M.
Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin
Biochem. J.
246
731-735
1987
Mus musculus
brenda
Gal, S.; Gottesman, M.M.
The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificity
Biochem. Biophys. Res. Commun.
139
156-162
1986
Mus musculus
brenda
Fiebiger, E.; Maehr, R.; Villadangos, J.; Weber, E.; Erickson, A.; Bikoff, E.; Ploegh, H.L.; Lennon-Dumenil, A.M.
Invariant chain controls the activity of extracellular cathepsin L
J. Exp. Med.
196
1263-1269
2002
Mus musculus
brenda
Beers, C.; Honey, K.; Fink, S.; Forbush, K.; Rudensky, A.
Differential regulation of cathepsin S and cathepsin L in interferon gamma-treated macrophages
J. Exp. Med.
197
169-179
2003
Mus musculus (P06797)
brenda
Mallen-St Clair, J.; Shi, G.P.; Sutherland, R.E.; Chapman, H.A.; Caughey, G.H.; Wolters, P.J.
Cathepsins L and S are not required for activation of dipeptidyl peptidase I (cathepsin C) in mice
Biol. Chem.
387
1143-1146
2006
Mus musculus
brenda
Khalikova, T.A.; Zhanaeva, S.Y.; Korolenko, T.A.; Kaledin, V.I.; Kogan, G.
Regulation of activity of cathepsins B, L, and D in murine lymphosarcoma model at a combined treatment with cyclophosphamide and yeast polysaccharide
Cancer Lett.
223
77-83
2005
Mus musculus
brenda
Nepal, R.M.; Mampe, S.; Shaffer, B.; Erickson, A.H.; Bryant, P.
Cathepsin L maturation and activity is impaired in macrophages harboring M. avium and M. tuberculosis
Int. Immunol.
18
931-939
2006
Mus musculus
brenda
Urbich, C.; Heeschen, C.; Aicher, A.; Sasaki, K.; Bruhl, T.; Farhadi, MR.; Vajkoczy, P.; Hofmann, W.K.; Peters, C.; Pennacchio, L.A.; Abolmaali, N.D.; Chavakis, E.; Reinheckel, T.; Zeiher, A.M.; Dimmeler, S.
Cathepsin L is required for endothelial progenitor cell-induced neovascularization
Nat. Med.
11
206-213
2005
Homo sapiens, Mus musculus
brenda
Spira, D.; Stypmann, J.; Tobin, D.J.; Petermann, I.; Mayer, C.; Hagemann, S.; Vasiljeva, O.; Guenther, T.; Schuele, R.; Peters, C.; Reinheckel, T.
Cell type-specific functions of the lysosomal protease cathepsin L in the heart
J. Biol. Chem.
282
37045-37052
2007
Homo sapiens, Mus musculus
brenda
Funkelstein, L.; Toneff, T.; Hwang, S.R.; Reinheckel, T.; Peters, C.; Hook, V.
Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expression
J. Neurochem.
106
384-391
2008
Mus musculus, Mus musculus (P06797)
brenda
Bulynko, Y.A.; Hsing, L.C.; Mason, R.W.; Tremethick, D.J.; Grigoryev, S.A.
Cathepsin L stabilizes the histone modification landscape on the Y chromosome and pericentromeric heterochromatin
Mol. Cell. Biol.
26
4172-4184
2006
Mus musculus
brenda
Pager, C.T.; Craft, W.W.; Patch, J.; Dutch, R.E.
A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L
Virology
346
251-257
2006
Mus musculus
brenda
Duncan, E.M.; Muratore-Schroeder, T.L.; Cook, R.G.; Garcia, B.A.; Shabanowitz, J.; Hunt, D.F.; Allis, C.D.
Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation
Cell
135
284-294
2008
Mus musculus
brenda
Mihelic, M.; Dobersek, A.; Guncar, G.; Turk, D.
Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation
J. Biol. Chem.
283
14453-14460
2008
Homo sapiens, Homo sapiens (P07711), Mus musculus, Mus musculus (P06797)
brenda
Nepal, R.M.; Vesosky, B.; Turner, J.; Bryant, P.
DM, but not cathepsin L, is required to control an aerosol infection with Mycobacterium tuberculosis
J. Leukoc. Biol.
84
1011-1018
2008
Mus musculus
brenda
Klein, D.M.; Felsenstein, K.M.; Brenneman, D.E.
Cathepsins B and L differentially regulate amyloid precursor protein processing
J. Pharmacol. Exp. Ther.
328
813-821
2009
Mus musculus
brenda
Navab, R.; Pedraza, C.; Fallavollita, L.; Wang, N.; Chevet, E.; Auguste, P.; Jenna, S.; You, Z.; Bikfalvi, A.; Hu, J.; OConnor, R.; Erickson, A.; Mort, J.S.; Brodt, P.
Loss of responsiveness to IGF-I in cells with reduced cathepsin L expression levels
Oncogene
27
4973-4985
2008
Mus musculus
brenda
Biswas, G.; Srinivasan, S.; Anandatheerthavarada, H.K.; Avadhani, N.G.
Dioxin-mediated tumor progression through activation of mitochondria-to-nucleus stress signaling
Proc. Natl. Acad. Sci. USA
105
186-191
2008
Mus musculus
brenda
Shimada, N.; Ohno-Matsui, K.; Iseki, S.; Koike, M.; Uchiyama, Y.; Wang, J.; Yoshida, T.; Sato, T.; Peters, C.; Mochizuki, M.; Morita, I.
Cathepsin L in bone marrow-derived cells is required for retinal and choroidal neovascularization
Am. J. Pathol.
176
2571-2580
2010
Mus musculus
brenda
Yamazaki, Y.; Kamei, Y.; Sugita, S.; Akaike, F.; Kanai, S.; Miura, S.; Hirata, Y.; Troen, B.R.; Kitamura, T.; Nishino, I.; Suganami, T.; Ezaki, O.; Ogawa, Y.
The cathepsin L gene is a direct target of FOXO1 in skeletal muscle
Biochem. J.
427
171-178
2010
Mus musculus
brenda
Zeeuwen, P.L.; van Vlijmen-Willems, I.M.; Cheng, T.; Rodijk-Olthuis, D.; Hitomi, K.; Hara-Nishimura, I.; John, S.; Smyth, N.; Reinheckel, T.; Hendriks, W.J.; Schalkwijk, J.
The cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea
FASEB J.
24
3744-3755
2010
Mus musculus
brenda
Konjar, S.; Sutton, V.R.; Hoves, S.; Repnik, U.; Yagita, H.; Reinheckel, T.; Peters, C.; Turk, V.; Turk, B.; Trapani, J.A.; Kopitar-Jerala, N.
Human and mouse perforin are processed in part through cleavage by the lysosomal cysteine proteinase cathepsin L
Immunology
131
257-267
2010
Homo sapiens, Mus musculus
brenda
Minokadeh, A.; Funkelstein, L.; Toneff, T.; Hwang, S.R.; Beinfeld, M.; Reinheckel, T.; Peters, C.; Zadina, J.; Hook, V.
Cathepsin L participates in dynorphin production in brain cortex, illustrated by protease gene knockout and expression
Mol. Cell. Neurosci.
43
98-107
2010
Mus musculus
brenda
Dennemaerker, J.; Lohmueller, T.; Mayerle, J.; Tacke, M.; Lerch, M.M.; Coussens, L.M.; Peters, C.; Reinheckel, T.
Deficiency for the cysteine protease cathepsin L promotes tumor progression in mouse epidermis
Oncogene
29
1611-1621
2010
Mus musculus
brenda
Beinfeld, M.C.; Funkelstein, L.; Foulon, T.; Cadel, S.; Kitagawa, K.; Toneff, T.; Reinheckel, T.; Peters, C.; Hook, V.
Cathepsin L plays a major role in cholecystokinin production in mouse brain cortex and in pituitary AtT-20 cells: protease gene knockout and inhibitor studies
Peptides
30
1882-1891
2009
Mus musculus
brenda
Yoshii, H.; Kamiyama, H.; Minematsu, K.; Goto, K.; Mizota, T.; Oishi, K.; Katunuma, N.; Yamamoto, N.; Kubo, Y.
Cathepsin L is required for ecotropic murine leukemia virus infection in NIH3T3 cells
Virology
394
227-234
2009
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Savalas, L.R.; Gasnier, B.; Damme, M.; Luebke, T.; Wrocklage, C.; Debacker, C.; Jezegou, A.; Reinheckel, T.; Hasilik, A.; Saftig, P.; Schroeder, B.
Disrupted in renal carcinoma 2 (DIRC2), a novel transporter of the lysosomal membrane, is proteolytically processed by cathepsin L
Biochem. J.
439
113-128
2011
Mus musculus
brenda
Hook, V.; Funkelstein, L.; Wegrzyn, J.; Bark, S.; Kindy, M.; Hook, G.
Cysteine cathepsins in the secretory vesicle produce active peptides: Cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimers disease
Biochim. Biophys. Acta
1824
89-104
2012
Mus musculus
brenda