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Information on EC 3.4.22.43 - cathepsin V
for references in articles please use BRENDA:EC3.4.22.43
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.22 Cysteine endopeptidases
3.4.22.43 cathepsin V
IUBMB Comments
Cathepsin V is a human lysosomal cysteine endopeptidase of family C1 (papain family) that is maximally active at pH 5.7 and unstable at neutral pH. Compound E-64, leupeptin and chicken cystatin are inhibitors. Human cathepsin V shows expression restricted to thymus, testis, corneal epithelium and some colon and breast carcinomas. Human gene locus: 9q22.2
The enzyme appears in viruses and cellular organisms
- 3.4.22.43
- cathepsins
-
papain-like
- elastases
-
elastolytic
- legumain
-
l-like
- medicine
- diagnostics
Reaction Schemes
showThe recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)
Synonyms
cathepsin v, ctsl2, stratum corneum thiol protease, cathepsin v/l2, cathepsin-v, cathepsin l2/v, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cathepsin L2
cathepsin U
CatV
CTSL2
CTSV
cathepsin L2
-
-
-
-
cathepsin U
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)
The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)
endopeptidase
-
-
-
The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)
Cathepsin V is a human lysosomal cysteine endopeptidase of family C1, papain family that is maximally active at pH 5.7 and unstable at neutral pH. Compound E-64, leupeptin and chicken cystatin are inhibitors. Human cathepsin V shows expression restricted to thymus, testis, corneal epithelium and some colon and breast carcinomas. Human gene locus: 9q22.2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
223670-00-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
Substrates: best substrate
Products: -
Products: -
?
2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLR + SIKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: best substrate
Products: -
Products: -
?
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KLRSXKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLR + SXKQ-N-(2,4-dinitrophenyl)ethylenediamine
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Substrates: X is varied with diverse amino acids, highest activity with Ile, kinetics, detailed overview
Products: -
Products: -
?
2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KLRXSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLR + XSKQ-N-(2,4-dinitrophenyl)ethylenediamine
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Substrates: X is varied with diverse amino acids, highest activity with Val, kinetics, detailed overview
Products: -
Products: -
?
2-aminobenzoyl-KLXSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLX + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
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Substrates: X is varied with diverse amino acids, highest activity with Arg, kinetics, detailed overview
Products: -
Products: -
?
2-aminobenzoyl-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-KPPVV + LLPDQ-N-[2,4-dinitrophenyl]ethylenediamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-KPVS + TEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KXRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
Substrates: X is varied with diverse amino acids, highest activity with Leu, kinetics, detailed overview
Products: -
Products: -
?
2-aminobenzoyl-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-LF + EKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-VLF + EKKQ-N-[2,4-dinitrophenyl]ethylenediamine
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Substrates: selective substrate for cathepsin V when compared with cathepsins B, L, and S
Products: -
Products: -
?
2-aminobenzoyl-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-VLF + EKKVY + LQ-N-[2,4-dinitrophenyl]ethylenediamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-VLF + EKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-XLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
Substrates: X is varied with diverse amino acids, highest activity with Ala, kinetics, detailed overview
Products: -
Products: -
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Lys + Arg-7-amido-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Lys-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Lys + Arg-7-amido-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Tyr-Lys-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Tyr-Lys + Arg-7-amido-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Boc-Gly-Lys-Arg-7-amido-4-methylcoumarin + H2O
Boc-Gly-Lys-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
kininogen fragments + H2O
?
-
Substrates: kininogenase activity with high and low molecular weight kininogens
Products: Lys-bradykinin is the major product
Products: Lys-bradykinin is the major product
?
N-benzyloxycarbonyl-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Arg + 7-amino-4-methylcoumarin
-
Substrates: very low activity
Products: -
Products: -
?
N-benzyloxycarbonyl-L-Arg-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
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Substrates: very low activity
Products: -
Products: -
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
Type I collagen + H2O
?
-
Substrates: cleavage of telopeptide region
Products: -
Products: -
?
Z-Arg-Arg-4-methoxy-2-nitroanilide + H2O
Z-Arg-Arg + 4-methoxy-2-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Z-Leu-Arg-7-amido-4-methylcoumarin + H2O
Z-Leu-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Z-Phe-Arg-4-methylcoumarin-7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Elastin + H2O
?
-
Substrates: elastin degradation activity leading to loss of elasticity in atherosclerosis
Products: -
Products: -
?
Elastin + H2O
?
-
Substrates: the enzyme exhibits high elastolytic cysteine protease activity
Products: -
Products: -
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
Substrates: Cbz-Phe-Arg-AMC, 25 microM used for protease inhibition assay, inhibitory conditions of cathepsin V propeptide analyzed
Products: -
Products: -
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
Substrates: mechanisms of interaction between serpins, human cathepsin V and DNA analyzed, kinetic constants for substrate cleavage in the presence and absence of cofactors determined, final concentrations of cathepsin V and ds65mer DNA at 0.1 and 10 nM, final substrate concentrations ranging from 5 to 200 microM in cathepsin V buffer
Products: -
Products: -
?
plasminogen + H2O
?
Substrates: capability of recombinant human cathepsin V to hydrolyze plasminogen analyzed, physiological role for cathepsin V related to the control of neovascularization in cornea suggested
Products: -
Products: -
?
plasminogen + H2O
?
Substrates: 4.5 microM human plasminogen and 30 nM of recombinant human cathepsins V used for plasminogen digestion assay, three major products of 60, 50 and 40 kDa obtained, SDS-PAGE
Products: -
Products: -
?
plasminogen + H2O
?
-
Substrates: cathepsin V hydrolyzes plasminogen at Phe94-Glu95, Ser358-Thr359, and Val468-Leu469 generating angiostatin-related fragments
Products: -
Products: -
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
Substrates: role of cathepsis V and the endogenous inhibitor cystatin C in adverse extracellular matrix remodeling of stenotic aortic valves analyzed
Products: -
Products: -
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the corneal enzyme stays within cells and is not secreted, suggesting that components of the corneal epithelium are likely substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the predominant expression in thymus suggests a role in the immune system, the expression in testes suggests a role in fertilization processes, the expression in cancer cells together with its absence in normal cells suggests a role in tumor processes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme can stimulate H2O2 production, enzyme expression is increased in keratoconus corneas compared to healthy ones, oxidative stress might be involved in the disorder
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme and inhibitor cystatin M/E are involved in regulation of epidermal differentiation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers hydrophobic residues in its S2-binding pocket, the substrate specificity is similar to cathepsin L, no cleavage of the triple-helical region of native collagen
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate and cleavage site specificity of activated recombinant enzyme, comparison to cathepsin L, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the human transglutaminase zymogen is no substrate for the enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: direct interaction of cathepsin V with TLR4 and its adaptor protein MyD88
Products: -
Products: -
?
additional information
?
-
-
Substrates: direct interaction of cathepsin V with TLR4 and its adaptor protein MyD88
Products: -
Products: -
?
additional information
?
-
Substrates: cathepsin L and cathepsin V cleave at the N-terminal side and between the dibasic residues (e.g., -K-R, -R-K, and K-K), with a preference for hydrophobic residues at the P2 position of the cleavage site. Cathepsin V shows a preference for Lys at the P1 position and some preference for Arg at the P1 position. Cathepsin L specific activity is 10fold greater than cathepsin V
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Elastin + H2O
?
-
Substrates: elastin degradation activity leading to loss of elasticity in atherosclerosis
Products: -
Products: -
?
plasminogen + H2O
?
Substrates: capability of recombinant human cathepsin V to hydrolyze plasminogen analyzed, physiological role for cathepsin V related to the control of neovascularization in cornea suggested
Products: -
Products: -
?
plasminogen + H2O
?
-
Substrates: cathepsin V hydrolyzes plasminogen at Phe94-Glu95, Ser358-Thr359, and Val468-Leu469 generating angiostatin-related fragments
Products: -
Products: -
?
additional information
?
-
-
Substrates: the corneal enzyme stays within cells and is not secreted, suggesting that components of the corneal epithelium are likely substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the predominant expression in thymus suggests a role in the immune system, the expression in testes suggests a role in fertilization processes, the expression in cancer cells together with its absence in normal cells suggests a role in tumor processes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme can stimulate H2O2 production, enzyme expression is increased in keratoconus corneas compared to healthy ones, oxidative stress might be involved in the disorder
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme and inhibitor cystatin M/E are involved in regulation of epidermal differentiation
Products: -
Products: -
?
additional information
?
-
Substrates: direct interaction of cathepsin V with TLR4 and its adaptor protein MyD88
Products: -
Products: -
?
additional information
?
-
-
Substrates: direct interaction of cathepsin V with TLR4 and its adaptor protein MyD88
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R)-1-{2-[butyl(dichloro)-l4-tellanyl]phenyl}ethyl methyl ether
-
less than 10% residual activity at 0.001 mM
(1R)-1-{2-[dibromo(butyl)-l4-tellanyl]phenyl}ethyl methyl ether
-
less than 10% residual activity at 0.001 mM
(1S)-1-{2-[butyl(dichloro)-l4-tellanyl]phenyl}ethyl methyl ether
-
less than 10% residual activity at 0.001 mM
(1S)-1-{2-[dibromo(butyl)-l4-tellanyl]phenyl}ethyl methyl ether
-
less than 10% residual activity at 0.001 mM
(2-(benzyloxy)phenyl)(3-(2-phenylthiazol-4-yl)oxiran-2-yl)methanone
-
uncompetitive and reversible
(3-(benzofuran-2-yl)oxiran-2-yl)(2-(benzyloxy)-4,5-dimethylphenyl)methanone
-
noncomeptitive and tight-binding or irreversible, decreases elastin degradation in cells
1,3,5-trihydroxy-4-methoxy-10-methyl-2,8-bis(3-methylbut-2-enyl)acridin-9(10H)-one
-
-
2,3-dihydro-4,9-dihydroxy-2-(2-hydroxy-propan-2-yl)-11-methoxy-10-methylfuro[3,2-b]acridin-5(10H)-one
-
-
2-[butyl(dichloro)-l4-tellanyl]benzyl methyl ether
-
about 10% residual activity at 0.001 mM
2-[dibromo(butyl)-l4-tellanyl]benzyl methyl ether
-
less than 10% residual activity at 0.001 mM
3,4-dihydro-3,5,8-trihydroxy-6-methoxy-2,2,7-trimethyl-2H-pyrano[2,3-a]acridin-12(7H)-one
-
-
4-fluoro-N-prop-2-yn-1-yl-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
4-methylpiperazine-1-carboxylic acid [1-[(3-benzenesulfonyl-1-phenethylallyl)carbamoyl]-2-phenylethyl]amide
-
i.e. APC-3316
chondroitin 4-sulfate
-
specific inhibition of elastolytic activity, formation of specific complexes with the enzyme, no inhibition of the activity with Z-Phe-Arg-4-methyl-7-coumaryl amide
cystatin C
endogenous inhibitor of cathepsin V analyzed, expression of cystatin C increased in stenotic valves, cystatin C protein particularly found in areas with infiltrates of inflammatory cells
-
fragment p41 of major histocompatibility complex class II-associated invariant chain
-
inhibitory to human cathepsin V, cathepsin L, cathepsin K, cathepsin F with Ki values in the low nanomolar range. Ki values are sufficiently low to ensure complex formation at physiological concentrations. Regulation of the proteolytic activity of most of the cysteine cathepsins by the p41 fragment is an important and widespread control mechanism of antigen presentation
-
methyl ((2S,3S)-3-(propylcarbamoyl)oxirane-2-carbonyl)-L-isoleucyl-D-prolinate
-
competitive and irreversible, completely blocks cathepsin V after 2 h of incubation and decreases elastin degradation
N-(3-acetylphenyl)-5-oxo-5H-thiazolo[3,2-a]pyrimidine-6-carboxamide
-
competitive
N-(3-bromoprop-2-yn-1-yl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-(cyanomethyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-but-3-yn-2-yl-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-[(1,1-dimethylethoxy)carbonyl]-L-tryptophan-2-[[[2-[(2-ethylphenyl)amino]-2-oxoethyl]thio]carbonyl]hydrazide
phenyl 4-((3-(naphthalen-1-ylmethyl)ureido)methyl)piperidine-1-carboxylate
-
competitive and reversible, selective inhibitor of cathepsin V, exerted significant effects on cell proliferation, elastin degradation, and immune cell cytotoxicity
phenyl 4-((3-benzhydrylureido)methyl)piperidine-1-carboxylate
-
noncompetitive and reversible
saquinavir
SQV, the HIV protease inhibitor Inhibits the interaction between cathepsin V and the TLR4-MyD88 receptor complex, also blocks disulfide HMGB1-induced TLR4 activation
serpin
cofactors fine tuning serpin activity in the extracellular milieu analyzed, DNA accelerate the rate at which the model serpin MENT inhibit cathepsin V up to 50-fold, primarily effected via the protease and secondarily by the recruitment of the DNA as a template onto which cathepsin V and MENT are bound, altered substrate turnover and conformational change within the protease observed, enzyme concentration constant at 0.1 nM, serpin concentration varying between 0.5 and 60 nM with a maximum of 5 nM serpin in the presence of DNA
-
STO33438
334, a mammalian protease inhibitor, inhibits cathepsin V, also blocks disulfide HMGB1-induced TLR4 activation
cystatin
cystatin inhibition relies on occlusion of the active site rather than the substrate-like behavior of serpins, unaltered by addition of DNA
-
cystatin M/E
-
cystatin M/E wild-type and mutant N64A show high affinity for cathepsin V, but not cystatin M/E mutant W135A
-
cystatin M/E
-
regulatory role, two distinct binding sites for cysteine proteases of the C1 peptidase family, the endogenous inhibitor is co-localized with the enzyme in lamellar granules and corneodesmosomes
-
cystatin M/E
-
the antiprotease activity of cystatin M/E inhibits the activity of cathepsin V
-
cystatin M/E
-
high-affinity inhibitor of cathepsin V, directly controls the activity of cathepsin V
-
N-[(1,1-dimethylethoxy)carbonyl]-L-tryptophan-2-[[[2-[(2-ethylphenyl)amino]-2-oxoethyl]thio]carbonyl]hydrazide
SID, suppresses the activity of cathepsin V and reverses the upregulation of inflammatory cytokines (IL-6, IL-8 and TNF-alpha), adhesion and chemotaxis of leukocytes and vascular inflammation induced by L-homocysteine (L-Hcy) in vivo and in vitro. SID also inhibits the monocyte-endothelial adhesion and neutrophil chemotaxis induced by L-Hcy. SID reverses this increased phosphorylation of ERK1/2 and STAT1, which is similar to the results obtained in vitro
N-[(1,1-dimethylethoxy)carbonyl]-L-tryptophan-2-[[[2-[(2-ethylphenyl)amino]-2-oxoethyl]thio]carbonyl]hydrazide
SID, inhibits the enzyme and also blocks HMGB1-induced TNF-alpha production
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the recombinant proenzyme is autocatalytically activated in vitro by incubation at pH 4.0 and 30°C
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alopecia
Evaluation of the CTSL2 Gene as a Candidate Gene For Alopecia X in Pomeranians and Keeshonden.
Arthritis
Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.
Arthritis, Juvenile
Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.
Arthritis, Rheumatoid
Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.
Atherosclerosis
Solution phase synthesis of a combinatorial library of chalcones and flavones as potent cathepsin V inhibitors.
Autoimmune Diseases
Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.
Breast Neoplasms
An exploratory study of host polymorphisms in genes that clinically characterize breast cancer tumors and pretreatment cognitive performance in breast cancer survivors.
Breast Neoplasms
Cathepsin V suppresses GATA3 protein expression in luminal A breast cancer.
Carcinoma
Significance of nuclear cathepsin V in normal thyroid epithelial and carcinoma cells.
Carcinoma, Ductal
Prognostic significance of cathepsin V (CTSV/CTSL2) in breast ductal carcinoma in situ.
Carcinoma, Hepatocellular
Elevated CTSL2 expression is associated with an adverse prognosis in hepatocellular carcinoma.
Carcinoma, Intraductal, Noninfiltrating
Prognostic significance of cathepsin V (CTSV/CTSL2) in breast ductal carcinoma in situ.
Colorectal Neoplasms
Cathepsin V Mediates the Tazarotene-induced Gene 1-induced Reduction in Invasion in Colorectal Cancer Cells.
Dermatitis, Atopic
The cystatin M / E-controlled pathway of skin barrier formation: expression of its key components in psoriasis and atopic dermatitis.
Endometrial Neoplasms
Expression of cysteine protease cathepsin L is increased in endometrial cancer and correlates with expression of growth regulatory genes.
Goiter
Significance of nuclear cathepsin V in normal thyroid epithelial and carcinoma cells.
Hyperhomocysteinemia
HMGB1 mediates homocysteine-induced endothelial cells pyroptosis via cathepsin V-dependent pathway.
Keratoconus
Increased levels of catalase and cathepsin V/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays a role in this disorder.
Lung Neoplasms
Manipulating substrate and pH in zymography protocols selectively distinguishes cathepsins K, L, S, and V activity in cells and tissues.
Mucopolysaccharidoses
The abnormal accumulation of heparan sulfate in patients with mucopolysaccharidosis prevents the elastolytic activity of cathepsin V.
Myasthenia Gravis
Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis.
Neoplasm Metastasis
Cathepsin V suppresses GATA3 protein expression in luminal A breast cancer.
Neoplasm Metastasis
Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
Neoplasms
An exploratory study of host polymorphisms in genes that clinically characterize breast cancer tumors and pretreatment cognitive performance in breast cancer survivors.
Neoplasms
CTSL2 is a pro-apoptotic target of E2F1 and a modulator of histone deacetylase inhibitor and DNA damage-induced apoptosis.
Neoplasms
Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
Neoplasms
Elevated CTSL2 expression is associated with an adverse prognosis in hepatocellular carcinoma.
Neoplasms
Expression of cysteine protease cathepsin L is increased in endometrial cancer and correlates with expression of growth regulatory genes.
Neoplasms
Manipulating substrate and pH in zymography protocols selectively distinguishes cathepsins K, L, S, and V activity in cells and tissues.
Neuroblastoma
Human cathepsin V protease participates in the production of enkephalin and NPY neurotransmitters.
Placenta Accreta
Possible Association between Cathepsin V and the Development of Placenta Accreta Spectrum Disorders.
Psoriasis
The cystatin M / E-controlled pathway of skin barrier formation: expression of its key components in psoriasis and atopic dermatitis.
Sarcoidosis, Pulmonary
Endostatin and cathepsin-V in bronchoalveolar lavage fluid of patients with pulmonary sarcoidosis.
Scleroderma, Systemic
Decreased cathepsin V expression due to Fli1 deficiency contributes to the development of dermal fibrosis and proliferative vasculopathy in systemic sclerosis.
Thyroid Cancer, Papillary
Significance of nuclear cathepsin V in normal thyroid epithelial and carcinoma cells.
Vascular Diseases
l-Homocysteine-induced cathepsin V mediates the vascular endothelial inflammation in hyperhomocysteinaemia.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
2-aminobenzoyl-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0017
2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.002
2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0008
2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0006
2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0012
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0006
2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0024
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
0.0044
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
0.0045
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of chondroitin 4-sulfate
0.0048
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of dermatan sulfate
0.0057
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of heparin
0.0057
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of heparan sulfate
0.0069
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of chondroitin 6-sulfate
0.0041
Z-Phe-Arg-4-methyl-7-coumaryl amide
-
recombinant enzyme, pH 5.5, 25°C, in presence of 0.3 M NaCl
additional information
additional information
presence of ds65-mer DNA causes a nonsignificant decrease in the Km value for the interaction between cathepsin V and the substrate, values from about 33.1 microM to 27.5 microM measured
-
additional information
additional information
-
presence of ds65-mer DNA causes a nonsignificant decrease in the Km value for the interaction between cathepsin V and the substrate, values from about 33.1 microM to 27.5 microM measured
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4
2-aminobenzoyl-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
1.3
2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.6
2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
1.7
2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
1.5
2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
1.3
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.9
2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
19
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
1.3
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of dermatan sulfate
1.4
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of heparan sulfate
5.3
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of heparin
5.4
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of chondroitin 4-sulfate
8.2
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of chondroitin 6-sulfate
156
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
3.7
Z-Phe-Arg-4-methyl-7-coumaryl amide
-
recombinant enzyme, pH 5.5, 25°C, in presence of 0.3 M NaCl
additional information
additional information
presence of DNA reduces the turnover rate up to 50% indicating that the binding of DNA changes the active site of cathepsin V such that the enzyme interacts with peptide substrates differently
-
additional information
additional information
-
presence of DNA reduces the turnover rate up to 50% indicating that the binding of DNA changes the active site of cathepsin V such that the enzyme interacts with peptide substrates differently
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
496
2-aminobenzoyl-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
903
2-aminobenzoyl-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
4528
2-aminobenzoyl-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
3055
2-aminobenzoyl-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
6833
2-aminobenzoyl-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, pH 5.5
4277
2-aminobenzoyl-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
7900
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
240
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of heparan sulfate
270
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of dermatan sulfate
900
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of heparin
1180
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of chondroitin 6-sulfate
1200
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
pH 5.5, 37°C, presence of chondroitin 4-sulfate
35000
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0212
(2-(benzyloxy)phenyl)(3-(2-phenylthiazol-4-yl)oxiran-2-yl)methanone
-
pH 5.5, 37°C
0.0683
(3-(benzofuran-2-yl)oxiran-2-yl)(2-(benzyloxy)-4,5-dimethylphenyl)methanone
-
pH 5.5, 37°C
0.0012
1,3,5-trihydroxy-2,8-bis(3-methylbut-2-enyl)-10-methyl-9-acridone
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0005
1,3,5-trihydroxy-4-methoxy-10-methyl-2,8-bis(3-methylbut-2-enyl)acridin-9(10H)-one
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0044
2,3-dihydro-4,9-dihydroxy-2-(2-hydroxy-propan-2-yl)-11-methoxy-10-methylfuro[3,2-b]acridin-5(10H)-one
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0017
3,4-dihydro-3,5,8-trihydroxy-6-methoxy-2,2,7-trimethyl-2H-pyrano[2,3-a]acridin-12(7H)-one
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0002
citibrasine
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.001
citrusinine-I
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0042
citrusinine-II
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.00000008
clitocypin
pH and temperature not specified in the publication
-
0.0000000072
fragment p41 of major histocompatibility complex class II-associated invariant chain
-
pH 6.0, 25°C
-
0.01
glycocitrine-I
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0011
glycocitrine-IV
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.00000069
macrocypin-1
pH and temperature not specified in the publication
-
0.008
methyl ((2S,3S)-3-(propylcarbamoyl)oxirane-2-carbonyl)-L-isoleucyl-D-prolinate
-
pH 5.5, 37°C
0.0887
phenyl 4-((3-(naphthalen-1-ylmethyl)ureido)methyl)piperidine-1-carboxylate
-
pH 5.5, 37°C
0.1558
phenyl 4-((3-benzhydrylureido)methyl)piperidine-1-carboxylate
-
pH 5.5, 37°C
0.00000025
VBY-825
-
apparent value, in 50 mM MES pH 6.5, 2.5 mM DTT, 2.5 mM EDTA, 100 mM NaCl, 0.01% (w/v) bovine serum albumin, and 10% (v/v) DMSO, at 25°C
0.0843
N-(3-acetylphenyl)-5-oxo-5H-thiazolo[3,2-a]pyrimidine-6-carboxamide
-
pH 5.5, 37°C
0.3522
N-(3-acetylphenyl)-5-oxo-5H-thiazolo[3,2-a]pyrimidine-6-carboxamide
-
pH 5.5, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0039
1,3,5-trihydroxy-2,8-bis(3-methylbut-2-enyl)-10-methyl-9-acridone
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0025
1,3,5-trihydroxy-4-methoxy-10-methyl-2,8-bis(3-methylbut-2-enyl)acridin-9(10H)-one
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0052
2,3-dihydro-4,9-dihydroxy-2-(2-hydroxy-propan-2-yl)-11-methoxy-10-methylfuro[3,2-b]acridin-5(10H)-one
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0028
3,4-dihydro-3,5,8-trihydroxy-6-methoxy-2,2,7-trimethyl-2H-pyrano[2,3-a]acridin-12(7H)-one
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.024
4-fluoro-N-prop-2-yn-1-yl-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.048
5-hydroxynoracronycine
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0012
citibrasine
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0022
citrusinine-I
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.01
citrusinine-II
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.025
glycocitrine-I
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0022
glycocitrine-IV
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.000016
N-(3-bromoprop-2-yn-1-yl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.00091
N-(cyanomethyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.046
N-but-3-yn-2-yl-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.0006
odanacatib
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.044
pyranofoline
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
inhibition properties of cathepsin V propeptide by fluorimetric assay determined, purification and expression of cathepsin V propeptide described, recombinant cathepsin V used for inhibition studies
additional information
plasminogen digestion by cathepsin V determined by SDS-PAGE and by subsequent plasmin activity tests, sequences EKKVYL, TEQLAP and LLPNVE obtained by N-terminal sequencing compatible with cleavage sites at plasminogen F94-E95, S358-T359 and V468-L469 peptide bonds, in vitro angiogenesis Matrigel assay described, angiogenesis inhibition activity caused by plasminogen processing by cathepsin V determined
additional information
-
plasminogen digestion by cathepsin V determined by SDS-PAGE and by subsequent plasmin activity tests, sequences EKKVYL, TEQLAP and LLPNVE obtained by N-terminal sequencing compatible with cleavage sites at plasminogen F94-E95, S358-T359 and V468-L469 peptide bonds, in vitro angiogenesis Matrigel assay described, angiogenesis inhibition activity caused by plasminogen processing by cathepsin V determined
additional information
interaction between cathepsin V with the model serpins MENT and SCCA-1 and with cystatin A analyzed, association rate constant (ka) for cathepsin V interaction in the presence and absence of cofactors determined, stoichiometry of inhibition (SI) in the absence and presence of cofactors determined, kinetic parameters of MENT and cystatin A in the presence of various DNA constructs ranging between 18mers and 65mers measured, binding of serpins and cathepsin V to DNA indicated by gel mobility shift analysis, electrostatic potential of human cathepsins V and effect of dsDNA on cathepsin V fluorescence indicated
additional information
-
interaction between cathepsin V with the model serpins MENT and SCCA-1 and with cystatin A analyzed, association rate constant (ka) for cathepsin V interaction in the presence and absence of cofactors determined, stoichiometry of inhibition (SI) in the absence and presence of cofactors determined, kinetic parameters of MENT and cystatin A in the presence of various DNA constructs ranging between 18mers and 65mers measured, binding of serpins and cathepsin V to DNA indicated by gel mobility shift analysis, electrostatic potential of human cathepsins V and effect of dsDNA on cathepsin V fluorescence indicated
additional information
expression of cathepsin V studied by RT-PCR and immunohistochemistry, cathepsin activity in aortic valves quantified by fluorometric microassay, increased mRNA expression and high activity of cathepsin V in stenotic valves observed, association of cathepsin V and the inhibitor cystatin C with calcific aortic valve disease determined, participation in adverse extracellular matrix remodelling of stenotic aortic valves suggested
additional information
expression of cathepsin V studied by RT-PCR and immunohistochemistry, cathepsin activity quantified by fluorometric microassay, intense association of cathepsin V with neovessels of the stenotic aortic valves reveals a role in neovascularization of the valves
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression in aorta valve, control valves and stenotic valves analyzed
brenda
cathepsin V localized to endothelial cells in areas rich of neovascularization
brenda
from healthy subjects and Besnier-Boeck-Schaumann (BBS) disease patients, the latter show decreased cathepsin V concentrations, while contents of endostatin, an inhibitor of lung epithelial cells, are increased
brenda
recombinant human cathepsin V for inhibition studies, N-terminal propeptide domains as inhibitors of cathepsin V
brenda
-
in the human thymic cortex, CTSV is the predominately expressed protease
brenda
additional information
CatV colocalizes with heparan sulfate in bronchial epithelial cells of mucopolysaccharidosis patients
brenda
-
normal and keratoconus corneas, the latter show a 1.5fold increased cathepsin V expression level, expression pattern, overview
brenda
-
localization of the enzyme in the root sheets of the hair follicle
brenda
plasminogen processing by cathepsin V, angiogenesis inhibition activity determined in
brenda
CatV colocalizes with heparan sulfate in bronchial epithelial cells of mucopolysaccharidosis patients
brenda
-
in plaque areas of diseased blood vessels, cathepsin expression levels during differentiation, overview
brenda
CTSV is highly expressed across the entire epidermis in normal skin. But CTSV expression levels are lower in the basal layer than those in the stratum corneum side in the hyperpigmented region
brenda
-
in extracellular space associated to corneodesmosomes, co-localization of the enzyme and inhibitor cystatin M/E
brenda
-
co-localization of the enzyme and inhibitor cystatin M/E, which are separately transported within lamellar granules
brenda
additional information
-
no expression in colon, lung, trachea, ureter, testis, heart, muscle, aorta, spleen, and mammary gland
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the corneal enzyme stays within cells and is not secreted
brenda
-
predominant localization in cells of cold nodules, follicular and papillary thyroid carcinoma tissue, less often in cells of hot nodules and goiter tissue. Cathepsin V is the predominant cysteine cathepsin in the nuclei of thyroid cell lines in steady state
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
RNAi-mediated depletion of the enzyme effectively abrogates ectopic E2F1-induced apoptosis, coupled with reduced lysosomal membrane permeabilization and mitochondrial membrane depolarization. Enzyme knockdown also inhibits apoptosis mediated by the endogenous E2F1 activated by DNA damage. Enzyme depletion in cancer cells results in inhibition of histone deacetylase inhibitor-induced apoptosis
malfunction
melanosome degradation is suppressed in CTSV knockdown cells. Inhibition of CTSV expression increases melanosome accumulation in HaCaT keratinocytes. The rate of melanosome degradation is reduced in CTSV knockdown keratinocytes
malfunction
increased cathepsin V promoted the degradation of DUSP6 and DUSP7, phosphorylation and subsequent nuclear translocation of ERK1/2, phosphorylation of STAT1 and expression of interleukin (IL)-6, IL-8 and TNF-alpha
malfunction
lack of cathepsins prevent the development of lung granulomas in a mouse model of Besnier-Boeck-Schaumann (BBS) disease, sarcoidosis. Cathepsin V (Cath V) in bronchoalveolar lavage fluid (BALF) in humans
metabolism
cathepsin V participates in the production of enkephalin and neuropeptide Y neurotransmitters in secretory vesicles
metabolism
effects of cathepsin V on the dual-specificity protein phosphatases (DUSPs) and MAPK pathways
metabolism
cathepsin V and endostatin may represent an index of pulmonary sarcoidosis activity
physiological function
-
expression of CTSV rescues the reduced frequency of CD4+ T cells in cysteine protease cathepsin L-deficient mice with H-2b haplotype
physiological function
-
CTSV is involved in the breakdown of corneodesmosomal proteins
physiological function
cathepsin like 2 is required for E2F1-induced apoptosis by engaging lysosomal membrane permeabilization. Its level also modulates the cellular sensitivity to histone deacetylase inhibitor
physiological function
enzyme cathepsin V (CTSV) is involved in melanosome degradation in the keratinocytes derived from lightcolored skin. It is one of the factors regulating pigmentation
physiological function
L-homocysteine-induced cathepsin V mediates the vascular endothelial inflammation in hyperhomocysteinaemia. Cathepsin V, specifically expressed in humans, is involved in vascular diseases through its elastolytic and collagenolytic activities. Cathepsin V mediates the L-homocysteine-induced upregulation of inflammatory cytokines
physiological function
exogenous cathepsin V protein protects human cardiomyocytes from angiotensin II-induced hypertrophy, human cardiomyocytes hypertrophic cardiomyopathy (HCM) as a cell model to investigate the effects of exogenous CTSV on Ang II-induced cardiac cell hypertrophy, overview. Analysis of the mechanism of CTSV cardioprotection, overview. Exogenous CTSV inhibits Ang II-induced hypertrophy in HCM cells by inhibiting PI3K/Akt/mTOR
physiological function
HIV protease inhibitor saquinavir targets the interaction of cathepsin V with TLR4/MyD88
physiological function
tazarotene-induced gene TIG1 interacts with cathepsin V (CTSV), which reduces CTSV stability and affects the production of activated urokinase-type plasminogen activator. Ectopic expression of CTSV increases the expression of activated urokinase-type plasminogen activator and the number of migrated and invaded cells
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CATL2_BOVIN
334
0
37393
Swiss-Prot
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23999
-
2 * 23999, amino acid sequence calculation of the mature enzyme, 2 * 31000, recombinant mature enzyme from insect cells and Pichia pastoris, 2 * 38000-45000, recombinant proenzyme from Pichi pastoris
24000
31000
-
2 * 23999, amino acid sequence calculation of the mature enzyme, 2 * 31000, recombinant mature enzyme from insect cells and Pichia pastoris, 2 * 38000-45000, recombinant proenzyme from Pichi pastoris
35000
37000
37330
preproprotein, containing a 17 amino acid signal peptide, a 96 amino acid propeptide and a 221 amino acid mature region, calculation from sequence of cDNA
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 23999, amino acid sequence calculation of the mature enzyme, 2 * 31000, recombinant mature enzyme from insect cells and Pichia pastoris, 2 * 38000-45000, recombinant proenzyme from Pichi pastoris
additional information
-
three-dimensional two-domain structure analysis at 1.6 A resolution, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
recombinant enzyme is partially and heterogenously glycosylated
proteolytic modification
-
autoactivation of the inactive extracellular zymogen at pH 4.0 and 37°C to the active mature protein
proteolytic modification
-
the recombinant enzyme is activated by pepsin treatment and further purified by gel filtration
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cathepsin V in complex with clitocypin, vapor diffusion method, using 0.4 M Li2SO4, 12% (w/v) polyethylene glycol 800, 20% (v/v) glycerol
molecular modeling of complex with fragment p41 of major histocompatibility complex class II-associated invariant chain
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme can complement cathepsin L-deficient mice by expression of cathepsin V in epidermis and hair follicles, the mutant mice suffer from a complex skin phenotype consisting of hair loss and epidermal hyperplasia with hyperproliferation of basal epidermal keratinocytes, acanthosis, and hyperkeratosis, overview
additional information
siRNA knockdown of CTSV in keratinocytes. Inhibition of CTSV expression increases melanosome accumulation in HaCaT keratinocytes. The rate of melanosome degradation is reduced in CTSV knockdown keratinocytes
additional information
cathepsin V enzyme knockout by siRNA transfection of THP-1 cells
additional information
-
cathepsin V enzyme knockout by siRNA transfection of THP-1 cells
additional information
-
an N-terminally truncated cathepsin V-eGFP is more abundant in the nuclei during S phase. N-terminally truncated cathepsin V-eGFP expressing cells are more proliferative than those expressing full-length cathepsin V-eGFP or wild type controls
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Pichia pastoris to homogeneity, activated mature native enzyme by hyrophobic interaction chromatography, recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography
-
recombinant enzyme from Pichia pastoris, further purified by gel filtration after activation by pepsin treatment
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expression in Pichia pastoris
from cDNA libraries, the gene maps to chromosome 9q21, DNA and amino acid sequence determination and analysis, genomic organization, expression in insect cells using the baculovirus system, in Pichia pastoris, and as GST-tagged enzyme with low activity in Escherichia coli
-
recombinant human cathepsin V produced using the Pichia pastoris expression system
recombinant procathepsin V is expressed in soluble form in the cytoplasm of Escherichia coli Rosetta-gami B (DE3) pLysS cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CTSL2 transcript levels are strongly elevated in endometrial cancer, particularly in G3 tumors
CTSV expression is inversely correlated with GATA3 in ER-positive breast cancer
L-homocysteine induces cathepsin V expression, L-homocysteine promoted cathepsin V expression in HUVECs. Methylation of the promoter region of cathepsin V is decreased following L-Hcy stimulation
mRNA expression of CTSV is significantly higher in colorectal cancer tissue samples than that in normal colon tissue samples
siRNA-cathepsin V inhibits the up-regulation of cathepsin V-induced by L-homocysteine
there is decreased expression of cathepsin V in lesional atopic dermatitis and psoriasis epidermis at the mRNA level as well as the protein level
-
tissue necrosis factor alpha increases cathepsin V expression and activity by 2fold. Tissue necrosis factor alpha and co-culturing with THP-1 monocytes stimulates a 460% increase in cathepsin V active enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
the enzyme is a potential marker for certain colon tumors and breast cancer
medicine
medicine
studies on the role of cathepsin V and cystatin C in the pathophysiology aortic stenosis
medicine
mammalian protease cathepsin V is a therapeutic target to inhibit TLR4-mediated inflammation induced by extracellular high-mobility group box 1 (HMGB1) (disulfide form). HMGB1 (disulfide form), via activation of toll-like receptor 4 (TLR4)-dependent signaling, is a strong driver of pathologic inflammation in both acute and chronic conditions. The mechanism of action involves a direct interaction between cathepsin V with TLR4 and its adaptor protein MyD88
medicine
-
an N-terminally truncated cathepsin V-eGFP is more abundant in the nuclei during S phase. N-terminally truncated cathepsin V-eGFP expressing cells are more proliferative than those expressing full-length cathepsin V-eGFP or wild type controls
medicine
-
hyperhomocysteinemia induces an increase in plasma IL-1beta levels in patients and mice models, while inhibition of cathepsin V reduces the plasma IL-1beta levels. High mobility group box-1 protein HMGB1 increases gasdermin N-terminal expression, and lysosomal cysteine protease cathepsin V mediates HMGB1-induced activation of caspase-1 and gasdermin. Silencing cathepsin V reverses HMGB1-induced pyroptosis
medicine
CatV colocalizes with heparan sulfate in bronchial epithelial cells of mucopolysaccharidosis patients. The heparan sulfate level correlates positively with the severity of respiratory symptoms and negatively to the overall endopeptidase activity of cysteine cathepsins. Heparan sulfate binds tightly to CatV and impairs its activity. Withdrawal of heparan sulfate preserves exogenous CatV activity
medicine
mRNA expression of CTSV is significantly higher in colorectal cancer tissue samples than that in normal colon tissue samples. Tazarotene-induced gene TIG1 interacts with cathepsin V (CTSV), which reduces CTSV stability and affects the production of activated urokinase-type plasminogen activator. Ectopic expression of CTSV increases the expression of activated urokinase-type plasminogen activator and the number of migrated and invaded cells
medicine
cathepsin V expression is associated with reduced survival in estrogen receptor-positive (ER-positive) breast cancers. Cathepsin V regulates the expression of GATA3 in ER-positive breast cancers, through promoting its degradation via the proteasome. Depletion of cathepsin V results in elevated pAkt-1 and reduced GSK-3beta expression, which rescues GATA3 from proteasomal degradation
medicine
high levels of CTSV expression correlate with an unfavorable prognosis in various cancers. High CTSV expression closely correlates with decreased expression of metabolic genes and increased expression of cell cycle genes. CTSV expression correlates with macrophages and CD4+ T cells and with macrophage infiltration in liver cancer tissues. Knockdown of CTSV inhibits liver cancer cells proliferation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brmme, D.; Li, Z.; Barnes, M.; Mehler, E.
Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
Biochemistry
38
2377-2385
1999
Homo sapiens (O60911), Homo sapiens
brenda
Adachi, W.; Kawamoto, S.; Ohno, I.; Nishida, K.; Kinoshita, S.; Matsubara, K.; Okubo, K.
Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium
Invest. Ophthalmol. Vis. Sci.
39
1789-1796
1998
Homo sapiens
brenda
Santamaria, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; Lopez-Otin, C.
Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas
Cancer Res.
58
1624-1630
1998
Homo sapiens
brenda
Somoza, J.R.; Zhan, H.; Bowman, K.K.; Yu, L.; Mortara, K.D.; Palmer, J.T.; Clark, J.M.; McGrath, M.E.
Crystal structure of human cathepsin V
Biochemistry
39
12543-12551
2000
Homo sapiens
brenda
Puzer, L.; Cotrin, S.S.; Alves, M.F.; Egborge, T.; Araujo, M.S.; Juliano, M.A.; Juliano, L.; Broemme, D.; Carmona, A.K.
Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L
Arch. Biochem. Biophys.
430
274-283
2004
Homo sapiens
brenda
Hagemann, S.; Guenther, T.; Dennemaerker, J.; Lohmueller, T.; Broemme, D.; Schuele, R.; Peters, C.; Reinheckel, T.
The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles
Eur. J. Cell Biol.
83
775-780
2004
Homo sapiens
brenda
Broemme, D.
Cathepsin V
Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D., Woessner, J.F., eds)
2nd Ed.
1107-1109
2004
Homo sapiens
-
brenda
Kenney, M.C.; Chwa, M.; Atilano, S.R.; Tran, A.; Carballo, M.; Saghizadeh, M.; Vasiliou, V.; Adachi, W.; Brown, D.J.
Increased levels of catalase and cathepsin V/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays a role in this disorder
Invest. Ophthalmol. Vis. Sci.
46
823-832
2005
Homo sapiens
brenda
Yasuda, Y.; Li, Z.; Greenbaum, D.; Bogyo, M.; Weber, E.; Broemme, D.
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
J. Biol. Chem.
279
36761-36770
2004
Homo sapiens
brenda
Cheng, T.; Hitomi, K.; van Vlijmen-Willems, I.M.; de Jongh, G.J.; Yamamoto, K.; Nishi, K.; Watts, C.; Reinheckel, T.; Schalkwijk, J.; Zeeuwen, P.L.
Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification
J. Biol. Chem.
281
15893-15899
2006
Homo sapiens
brenda
Zeeuwen, P.L.; Ishida-Yamamoto, A.; van Vlijmen-Willems, I.M.; Cheng, T.; Bergers, M.; Iizuka, H.; Schalkwijk, J.
Colocalization of cystatin M/E and cathepsin V in lamellar granules and corneodesmosomes suggests a functional role in epidermal differentiation
J. Invest. Dermatol.
127
120-128
2006
Homo sapiens
brenda
Helske, S.; Syvaeranta, S.; Lindstedt, K.A.; Lappalainen, J.; Oeoerni, K.; Maeyraenpaeae, M.I.; Lommi, J.; Turto, H.; Werkkala, K.; Kupari, M.; Kovanen, P.T.
Increased Expression of Elastolytic Cathepsins S, K, and V and Their Inhibitor Cystatin C in Stenotic Aortic Valves
Arterioscler. Thromb. Vasc. Biol.
26
1791-1798
2006
Homo sapiens (O60911)
brenda
Burden, R.E.; Snoddy, P.; Jefferies, C.A.; Walker, B.; Scott, C.J.
Inhibition of cathepsin L-like proteases by cathepsin V propeptide
Biol. Chem.
388
541-545
2007
Homo sapiens (O60911)
brenda
Puzer, L.; Barros, N.M.; Paschoalin, T.; Hirata, I.Y.; Tanaka, A.S.; Oliveira, M.C.; Broemme, D.; Carmona, A.K.
Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen
Biol. Chem.
389
195-200
2008
Homo sapiens (O60911), Homo sapiens
brenda
Ong, P.C.; McGowan, S.; Pearce, M.C.; Irving, J.A.; Kan, W.T.; Grigoryev, S.A.; Turk, B.; Silverman, G.A.; Brix, K.; Bottomley, S.P.; Whisstock, J.C.; Pike, R.N.
DNA accelerates the inhibition of human cathepsin V by serpins
J. Biol. Chem.
282
36980-36986
2007
Homo sapiens (O60911), Homo sapiens
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
brenda
Elie, B.T.; Gocheva, V.; Shree, T.; Dalrymple, S.A.; Holsinger, L.J.; Joyce, J.A.
Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model
Biochimie
92
1618-1624
2010
Homo sapiens
brenda
Sevenich, L.; Hagemann, S.; Stoeckle, C.; Tolosa, E.; Peters, C.; Reinheckel, T.
Expression of human cathepsin L or human cathepsin V in mouse thymus mediates positive selection of T helper cells in cathepsin L knock-out mice
Biochimie
92
1674-1680
2010
Homo sapiens
brenda
Coppini, L.P.; Barros, N.M.; Oliveira, M.; Hirata, I.Y.; Alves, M.F.; Paschoalin, T.; Assis, D.M.; Juliano, M.A.; Puzer, L.; Broemme, D.; Carmona, A.K.
Plasminogen hydrolysis by cathepsin S and identification of derived peptides as selective substrate for cathepsin V and cathepsin L inhibitor
Biol. Chem.
391
561-570
2010
Homo sapiens
brenda
Cheng, T.; Tjabringa, G.S.; van Vlijmen-Willems, I.M.; Hitomi, K.; van Erp, P.E.; Schalkwijk, J.; Zeeuwen, P.L.
The cystatin M/E-controlled pathway of skin barrier formation: expression of its key components in psoriasis and atopic dermatitis
Br. J. Dermatol.
161
253-264
2009
Homo sapiens
brenda
Renko, M.; Sabotic, J.; Mihelic, M.; Brzin, J.; Kos, J.; Turk, D.
Versatile loops in mycocypins inhibit three protease families
J. Biol. Chem.
285
308-316
2010
Homo sapiens (O60911)
brenda
Zeeuwen, P.L.; Cheng, T.; Schalkwijk, J.
The biology of cystatin M/E and its cognate target proteases
J. Invest. Dermatol.
129
1327-1338
2009
Homo sapiens
brenda
Wilder, C.L.; Park, K.Y.; Keegan, P.M.; Platt, M.O.
Manipulating substrate and pH in zymography protocols selectively distinguishes cathepsins K, L, S, and V activity in cells and tissues
Arch. Biochem. Biophys.
516
52-57
2011
Homo sapiens
brenda
Severino, R.P.; Guido, R.V.; Marques, E.F.; Broemme, D.; da Silva, M.F.; Fernandes, J.B.; Andricopulo, A.D.; Vieira, P.C.
Acridone alkaloids as potent inhibitors of cathepsin V
Bioorg. Med. Chem.
19
1477-1481
2011
Homo sapiens
brenda
Piovan, L.; Alves, M.F.; Juliano, L.; Broemme, D.; Cunha, R.L.; Andrade, L.H.
Structure-activity relationships of hypervalent organochalcogenanes as inhibitors of cysteine cathepsins V and S
Bioorg. Med. Chem.
19
2009-2014
2011
Homo sapiens
brenda
McCarthy, E.; Cunningham, E.; Copley, L.; Jackson, D.; Johnston, D.; Dalton, J.; Mulcahy, G.
Cathepsin L proteases of the parasitic copepod, Lepeophtheirus salmonis
Aquaculture
356-357
264-271
2012
Lepeophtheirus salmonis (A7TZ36)
-
brenda
Skrzypczak, M.; Springwald, A.; Lattrich, C.; Haering, J.; Schueler, S.; Ortmann, O.; Treeck, O.
Expression of cysteine protease cathepsin L is increased in endometrial cancer and correlates with expression of growth regulatory genes
Cancer Invest.
30
398-403
2012
Homo sapiens (O60911), Homo sapiens
brenda
Funkelstein, L.; Lu, W.D.; Koch, B.; Mosier, C.; Toneff, T.; Taupenot, L.; O'Connor, D.T.; Reinheckel, T.; Peters, C.; Hook, V.
Human cathepsin V protease participates in production of enkephalin and NPY neuropeptide neurotransmitters
J. Biol. Chem.
287
15232-15241
2012
Homo sapiens (O60911), Homo sapiens
brenda
Keegan, P.M.; Wilder, C.L.; Platt, M.O.
Tumor necrosis factor alpha stimulates cathepsin K and V activity via juxtacrine monocyte-endothelial cell signaling and JNK activation
Mol. Cell. Biochem.
367
65-72
2012
Homo sapiens (O60911), Homo sapiens
brenda
Wong, C.H.; Wu, Z.; Yu, Q.
CTSL2 is a pro-apoptotic target of E2F1 and a modulator of histone deacetylase inhibitor and DNA damage-induced apoptosis
Oncogene
33
1249-1257
2014
Homo sapiens (O60911), Homo sapiens
brenda
Novinec, M.; Pavsic, M.; Lenarcic, B.
A simple and efficient protocol for the production of recombinant cathepsin V and other cysteine cathepsins in soluble form in Escherichia coli
Protein Expr. Purif.
82
1-5
2012
Homo sapiens (O60911)
brenda
Naumnik, W.; Ossolinska, M.; Plonska, I.; Chyczewska, E.; Niklinski, J.
Endostatin and cathepsin-V in bronchoalveolar lavage fluid of patients with pulmonary sarcoidosis
Adv. Exp. Med. Biol.
833
55-61
2015
Homo sapiens (O60911), Homo sapiens
brenda
Homma, T.; Kageyama, S.; Nishikawa, A.; Nagata, K.
Melanosome degradation in epidermal keratinocytes related to lysosomal protease cathepsin V
Biochem. Biophys. Res. Commun.
500
339-343
2018
Homo sapiens (O60911)
brenda
Leng, Y.P.; Ma, Y.S.; Li, X.G.; Chen, R.F.; Zeng, P.Y.; Li, X.H.; Qiu, C.F.; Li, Y.P.; Zhang, Z.; Chen, A.F.
L-Homocysteine-induced cathepsin V mediates the vascular endothelial inflammation in hyperhomocysteinaemia
Br. J. Pharmacol.
175
1157-1172
2018
Homo sapiens (O60911), Homo sapiens
brenda
Huang, K.; Gao, L.; Yang, M.; Wang, J.; Wang, Z.; Wang, L.; Wang, G.; Li, H.
Exogenous cathepsin V protein protects human cardiomyocytes HCM from angiotensin II-induced hypertrophy
Int. J. Biochem. Cell Biol.
89
6-15
2017
Homo sapiens (O60911), Homo sapiens
brenda
Mons, E.; Jansen, I.D.C.; Loboda, J.; van Doodewaerd, B.R.; Hermans, J.; Verdoes, M.; van Boeckel, C.A.A.; van Veelen, P.A.; Turk, B.; Turk, D.; Ovaa, H.
The Alkyne moiety as a latent electrophile in irreversible covalent small molecule inhibitors of cathepsin K
J. Am. Chem. Soc.
141
3507-3514
2019
Homo sapiens (P07711)
brenda
Pribis, J.P.; Al-Abed, Y.; Yang, H.; Gero, D.; Xu, H.; Montenegro, M.F.; Bauer, E.M.; Kim, S.; Chavan, S.S.; Cai, C.; Li, T.; Szoleczky, P.; Szabo, C.; Tracey, K.J.; Billiar, T.R.
The HIV protease inhibitor saquinavir inhibits HMGB1-driven inflammation by targeting the interaction of cathepsin V with TLR4/MyD88
Mol. Med.
21
749-757
2015
Homo sapiens (O60911), Homo sapiens
brenda
Yoon, M.C.; Ames, J.; Mosier, C.; Jiang, Z.; Podvin, S.; ODonoghue, A.J.; Hook, V.
Distinct dibasic cleavage specificities of neuropeptide-producing cathepsin L and cathepsin V cysteine proteases compared to PC1/3 and PC2 serine proteases
ACS Chem. Neurosci.
13
245-256
2022
Homo sapiens (O60911)
brenda
Leng, Y.; Chen, R.; Chen, R.; He, S.; Shi, X.; Zhou, X.; Zhang, Z.; Chen, A.F.
HMGB1 mediates homocysteine-induced endothelial cells pyroptosis via cathepsin V-dependent pathway
Biochem. Biophys. Res. Commun.
532
640-646
2020
Homo sapiens
brenda
Al-Hashimi, A.; Venugopalan, V.; Sereesongsaeng, N.; Tedelind, S.; Pinzaru, A.M.; Hein, Z.; Springer, S.; Weber, E.; Fuehrer, D.; Scott, C.J.; Burden, R.E.; Brix, K.
Significance of nuclear cathepsin V in normal thyroid epithelial and carcinoma cells
Biochim. Biophys. Acta Mol. Cell Res.
1867
118846
2020
Homo sapiens
brenda
Sereesongsaeng, N.; McDowell, S.H.; Burrows, J.F.; Scott, C.J.; Burden, R.E.
Cathepsin V suppresses GATA3 protein expression in luminal A breast cancer
Breast Cancer Res.
22
139
2020
Homo sapiens (O60911)
brenda
Chazeirat, T.; Denamur, S.; Bojarski, K.K.; Andrault, P.M.; Sizaret, D.; Zhang, F.; Saidi, A.; Tardieu, M.; Linhardt, R.J.; Labarthe, F.; Broemme, D.; Samsonov, S.A.; Lalmanach, G.; Lecaille, F.
The abnormal accumulation of heparan sulfate in patients with mucopolysaccharidosis prevents the elastolytic activity of cathepsin V
Carbohydr. Polym.
253
117261
2021
Homo sapiens (O60911)
brenda
Wang, C.H.; Wang, L.K.; Wu, C.C.; Chen, M.L.; Kuo, C.Y.; Shyu, R.Y.; Tsai, F.M.
Cathepsin V mediates the tazarotene-induced gene 1-induced reduction in invasion in colorectal cancer cells
Cell Biochem. Biophys.
78
483-494
2020
Homo sapiens (O60911)
brenda
Mitrovic, A.; Senjor, E.; Jukic, M.; Bolcina, L.; Prunk, M.; Proj, M.; Nanut, M.P.; Gobec, S.; Kos, J.
New inhibitors of cathepsin V impair tumor cell proliferation and elastin degradation and increase immune cell cytotoxicity
Comput. Struct. Biotechnol. J.
20
4667-4687
2022
Homo sapiens
brenda
Liu, J.; Zhang, W.; Wang, Z.; Wang, Y.; Li, T.; Wang, Y.; Ding, J.; Ning, B.
Cathepsin V is correlated with the prognosis and tumor microenvironment in liver cancer
Mol. Carcinog.
63
400-416
2024
Homo sapiens (O60911)
brenda
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Release 2026.1 (March 2026)
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