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Information on EC 3.4.22.16 - cathepsin H and Organism(s) Homo sapiens and UniProt Accession P09668
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3.4.22.16 cathepsin HSpecify your search results
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
Synonyms
cathepsin h, aleurain, catb3, cat h, procathepsin h, cathepsin b3, cathepsin h-like cysteine proteinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aleurain
-
-
-
-
cathepsin B3
-
-
-
-
cathepsin Ba
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
same catalytic mechanism as in papain and actinidin
-
CAS REGISTRY NUMBER
COMMENTARY
60748-73-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
?
Arg-7-amido-4-trifluoromethylcoumarin + H2O
Arg + 7-amino-4-trifluoromethylcoumarin
fluorogenic cathepsin H substrate
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
alpha-N-benzoyl-DL-arginine-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + beta-naphthylamine
-
-
-
-
?
alpha-neoendorphin + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
bradykinin + H2O
?
-
no aminopeptidase activity, endopeptidase activity after prolonged incubation
-
?
demorphin + H2O
?
-
no aminopeptidase activity, endopeptidase activity after prolonged incubation
-
?
dynorphin(1-13) + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
dynorphin(1-6) + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-enkephalin + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
Lys-bradykinin + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
neurotensin + H2O
?
-
no aminopeptidase activity, endopeptidase activity after prolonged incubation
-
?
pro-surfactant protein B-EGFP fusion protein + H2O
?
-
cleavage 13 amino acids upstream of the NH2-terminus of mature surfactant protein B, and at the boundary between surfactant protein and C-terminal peptide
-
-
?
talin + H2O
?
-
cathepsin H cleaves the N-terminus of the talin F0 head domain
-
-
?
VALSLKISIGNVVKTMQFEPST + H2O
?
-
the peptide mimicks the N-terminus of the talin F0 head domain
-
-
?
Z-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
?
-
no substrate for wild type enzyme, endopeptidase activity of mutant T11_E18del-cathepsin H
-
?
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
conventional test substrate
-
ir
Arg-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
-
assay at pH 5.5, 37°C
-
-
?
benzoyl-DL-Arg-2-naphthylamide + H2O
benzoyl-DL-Arg + 2-naphthylamine
-
-
-
ir
benzoyl-DL-Arg-2-naphthylamide + H2O
benzoyl-DL-Arg + 2-naphthylamine
-
-
-
ir
Proteins + H2O
?
-
involved in human glioma, anaplastic astrocytoma, and glioblastoma progression and invasion
-
-
?
additional information
?
-
procathepsin H is not capable of autocleavage at pH 4.5-6.5
-
-
?
additional information
?
-
-
procathepsin H is not capable of autocleavage at pH 4.5-6.5
-
-
?
additional information
?
-
-
activity as endopeptidase and aminopeptidase on synthetic substrates
-
-
?
additional information
?
-
-
enzyme is involved in maturation of the biologically active surfactant protein B
-
-
?
additional information
?
-
-
does not cleave benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin, benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin, and benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is involved in maturation of the biologically active surfactant protein B
-
-
?
Proteins + H2O
?
-
involved in human glioma, anaplastic astrocytoma, and glioblastoma progression and invasion
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CNWAAGYNCGGGS-NH2
-
cyclic peptide with intramolecular disulfide bond, comparison of inhibitory effect with cathepsin K, cathepsin L, cathepsin B and papain
CNWTLGGYKCGGGS-NH2
-
cyclic peptide with intramolecular disulfide bond, comparison of inhibitory effect with cathepsin K, cathepsin L, cathepsin B and papain
CWEWGGWHCGGSS-OH
-
cyclic peptide with intramolecular disulfide bond, comparison of inhibitory effect with cathepsin K, cathepsin L, cathepsin B and papain
CWSMMGFQCGGGS-NH2
-
cyclic peptide with intramolecular disulfide bond, comparison of inhibitory effect with cathepsin K, cathepsin L, cathepsin B and papain
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
-
E-64-d, inhibits processing of proenzyme to synthetic analogs
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
Thiol proteinase inhibitor
-
from human serum, human lung, molecular weights: 13000 and 80000, the latter including haptoglobin, 4-7% inhibition
-
Thiol proteinase inhibitor
-
proteinase inhibitor from rat, man, hog, Tetrahymena, tuna, chicken, toad, purified rat lung inhibitors have molecular weight of 14000, purified hog kidney inhibitors have molecular weight of 11000, also high molecular weight inhibitors in human and rat serum, tissue distributions in humans and rat: inhibitors widely distributed, probaly regulatory function
-
additional information
no significant inhibitory effect of enzyme propeptide fragments, detailed analysis using several different peptides. Recombinant enzyme lacking the mini-chain shows inhibitory interaction
-
additional information
molecular basis for the inhibition of the mature enzyme by the prodomain. The prodomain of procathepsin H has an N-terminal helical subdomain (Ala1P-Ser75P) and an extended portion (Glu76P-Pro93P) that links the helical subdomain to Tyr1 of the mature domain
-
additional information
-
molecular basis for the inhibition of the mature enzyme by the prodomain. The prodomain of procathepsin H has an N-terminal helical subdomain (Ala1P-Ser75P) and an extended portion (Glu76P-Pro93P) that links the helical subdomain to Tyr1 of the mature domain
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
procathepsin H is not capable of autoactivation and requires other proteases such as cathepsin L for its activation
-
additional information
-
procathepsin H is not capable of autoactivation and requires other proteases such as cathepsin L for its activation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.092
Z-L-Phe-L-Arg-NH-4-methylcoumaryl-7-amide
-
mutant T11_E18del-cathepsin H, pH 6.8, 30°C
3.6
H-L-Arg-NH-4-methylcoumaryl-7-amide
-
mutant T11_E18del-cathepsin H, pH 6.8, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00014
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
0.0014
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
0.000000095
chicken egg white cystatin
-
mutant T11_E18del-cathepsin H, pH 6.8, 30°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
cathepsin H is a member of the papain superfamily of lysosomal cysteine proteases
malfunction
loss of CTSH inhibits filaggrin processing, but not expression, and impairs epidermal barrier function, evidence for compensation in CTSH knockout
metabolism
phosphoinositide 3-kinase signaling through AKT1 is required for the proteolytic processing of filaggrin during late epidermal terminal differentiation
physiological function
malfunction
-
specific inhibition of cathepsin H increases the activation of alphabeta3-integrin on PC-3 cells
physiological function
-
cathepsin H mediates the processing of talin and regulates migration of prostate cancer cells
additional information
physiological function
profilaggrin to filaggrin processing is complex, requiring dephosphorylation and numerous proteolytic events, several proteases have been identified that cleave profilaggrin at specific sites, releasing the filaggrin monomers and both the N- and C-termini, including cathepsin H. CTSH is a differentiation-dependent protease coexpressed with filaggrin
physiological function
the mature enzyme is inhibited by its own prodomain after maturation cleavage. Upon activation, cathepsin H displays a distinct proteolytic activity among the papain superfamily, functioning predominantly as an aminopeptidase that cleaves a single N-terminal residue from a polypeptide chain. Cathepsin H has also been shown to act as an endopeptidase, although with much lower efficiency
additional information
the catalytic triad residues Cys26, His166 and Asn186 of procathepsin H reside in the active site cleft
additional information
-
the catalytic triad residues Cys26, His166 and Asn186 of procathepsin H reside in the active site cleft
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). CATH_HUMAN
335
0
37394
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
230 residues, 8 of which belong to SS-linked minichain, high sequnece homologies to cathepsin B and other cysteine proteinases of the papain superfamily
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the enzyme harbors two glycosylation sites, Asn79P on the mini-chain of the prodomain and Asn115 on the mature domain. No glycan is built for Asn79P in cathepsin H due to poor electron density, although it is glycosylated
proteolytic modification
proteolytic modification
proteolytic modification
propeptide-binding region of enzyme is structurally rearranged during maturation processing and mini-chain formation, which impairs the effective recognition of mature enzyme by its propeptide
proteolytic modification
the enzyme is synthesized as an inactive proenzyme, the N-terminal prodomain (Ala1P-Pro93P) is cleaved off for maturation, a C-terminal mature domain (Tyr1-Val220) with a disulfide bridge between Cys212 and the mini-chain Cys80P remains. Procathepsin H is not autoactivated but can be transactivated by cathepsin L. The prodomain of procathepsin H has an N-terminal helical subdomain (Ala1P-Ser75P) and an extended portion (Glu76P-Pro93P) that links the helical subdomain to Tyr1 of the mature domain
proteolytic modification
-
mutant lacking the mini chain, autocatalytic processing at pH 5.0, 37°C, processing is accelerated in presence of 0.025 mg/ml of dextran, prolonged activation results in both cases in decrease of enzyme acivtiy
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified wild-type and C26S mutant procathepsin H, sitting drop vapor diffusion method, 5.7 mg/ml protein, crystal growth from 0.1 M Na2HPO4/citric acid, pH 4.2, and 2.0 M (NH4)2SO4, 1 week, 20°C, method optimization, X-ray diffraction structure determination and analysis at 2.0 A and 1.66 A resolution, respectively, molecular replacement and modeling
comparison of structure and primary sequences of 5 papain, actinidin, cathepsins B and H and stem bromelain yields high degree of similarity
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C26S
site-directed mutagenesis, catalytically inactive active site mutant
C80S
site-directed mutagenesis, the mutation removes the disulfide between the mini-chain and the mature domain and completely abolishes the protease activity
H166A
site-directed mutagenesis, catalytically inactive active site mutant
N186A
site-directed mutagenesis, catalytically inactive active site mutant
T83A
site-directed mutagenesis, mutation of the Thr83 of the mini-chain has only mild effects on the enzyme activity
additional information
additional information
-
mutant lacking the mini chain, loss of aminopeptidase activity, increase in endopeptidase activity
additional information
-
mutant lacking the mini-chain, T11_E18del-cathepsin H, minimal aminopeptidase activity against good wild type substrates, endopeptidase activity against Z-L-Phe-L-Arg-NH-4-methylcoumaryl-7-amide, which is not cleaved by wild type
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
analysis of stability of the mini-chain in cathepsin H and procathepsin H, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.02 M sodium acetate buffer, pH 5.2, 1 mM EDTA, several months without loss of activity
-
4°C or -20°C, 50 mM Na-acetate buffer, pH 5.0, 0.2 M NaCl, 0. 5 mM HgCl2, 1 mM EDTA
-
4°C or -20°C, 50-100 mM Na-acetate buffer, pH 5.5, 1 mM Na2-EDTA, 0.1% Brij 35, 5 mM Na-tetrathionate, 1 month, 0-10% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Spodoptera frugiperda Sf9 cells or HEK-23T cells, respectively, by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CTSH, real-time PCR enzyme expression analysis in skin and keratinocyte culture
procathepsin H (Ala1P-Val220) construct is cloned with an N-terminal gp64 secretion signal peptide and an uncleavable C-terminal His6-tag, recombinant expression of wild-type enzyme in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system, recombinant expression of His-tagged mutant enzymes in HEK-293T cells using the lentiviral viral vector CD731B
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
tumor specific increase in cathepsin H antigen may be useful marker of tumor progression in central nervous system neoplasms
medicine
-
enzyme activity, immunoreactivity, and mRNA in most basal cell carcinomas are higher than in normal skin. Reactive cells are located between and around tumor nodules, but not in tumor nests. Enzyme in peritumoral cells may either promote invasion of the tumor cells by degradation of the extracellular matrix or may reflect an elevated activity of the surrounding immunological cells
medicine
-
enzyme from meningogioma shows a 3.5fold increased vmax-value compared to normal tissue, and a 1.3fold decrease in KM-value. Molecular weight of tumor enzyme is decreased
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lenney, J.F.; Liao, J.R.; Sugg, S.L.; Gopalakrishnan, V.; Wong, H.C.H.; Ouye, K.H.; Chan, P.W.H.
Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF
Biochem. Biophys. Res. Commun.
108
1581-1587
1982
Homo sapiens
Barrett, A.J.; Kirschke, H.
Cathepsin B, Cathepsin H, and cathepsin L
Methods Enzymol.
80
535-561
1981
Homo sapiens, Rattus norvegicus
Lenney, J.F.; Tolan, J.R.; Sugai, W.J.; Lee, A.G.
Thermostable endogenous inhibitors of cathepsins B and H
Eur. J. Biochem.
101
153-161
1979
Homo sapiens, Paramecium caudatum, Rattus norvegicus, Sus scrofa, Tetrahymena pyriformis
Fuchs, R.; Machleidt, W.; Gassen, H.G.
Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H
Biol. Chem. Hoppe-Seyler
369
469-475
1988
Homo sapiens
Popovic, T.; Brzin, J.; Kos, J.; Lenarcic, B.; Machleidt, W.; Ritonja, A.; Hanada, K.; Turk, V.
A new purification procedure of human kidney cathepsin H, its properties ans kinetic data
Biol. Chem. Hoppe-Seyler
369
175-183
1988
Homo sapiens
-
Ritonja, A.; Popovic, T.; Kotnik, M.; Machleidt, W.; Turk, V.
Amino acid sequences of the human kidney cathepsins H and L
FEBS Lett.
228
341-345
1988
Homo sapiens
Bergmeyer, H.U.ed
Cathepsin B, cathepsin H, and cathepsin L
Methods Enzym. Anal. (3rd. ed. )
5
195-210
1984
Homo sapiens, Rattus norvegicus
-
Schwartz, W.N.; Barrett, A.J.
Human cathepsin H
Biochem. J.
191
487-497
1980
Homo sapiens, Rattus norvegicus
Sivaparvathi, M.; Sawaya, R.; Gokaslan, Z.L.; Chintala, K.S.; Rao, J.S.
Expression and the role of cathepsin H in human glioma progression and invasion
Cancer Lett.
104
121-126
1996
Homo sapiens, Rattus norvegicus
Guncar, G.; Podobnik, M.; Pungercar, J.; Strukelj, B.; Turk, V.; Turk, D.
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
Structure
6
51-61
1998
Homo sapiens, Sus scrofa
Kamphuis, I.G.; Drenth, J.; Baker, E.N.
Thiol proteases: comparative studies on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain
J. Mol. Biol.
182
317-329
1985
Homo sapiens
Vasiljeva, O.; Dolinar, M.; Turk, V.; Turk, B.
Recombinant human cathepsin H lacking the mini chain is an endopeptidase
Biochemistry
42
13522-13528
2003
Homo sapiens, Sus scrofa
Dodt, J.; Reichwein, J.
Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase
Biol. Chem.
384
1327-1332
2003
Homo sapiens
Brguljan, P.M.; Turk, V.; Nina, C.; Brzin, J.; Krizaj, I.; Popovic, T.
Human brain cathepsin H as a neuropeptide and bradykinin metabolizing enzyme
Peptides
24
1977-1984
2003
Homo sapiens
Froehlich, E.; Moehrle, M.; Klessen, C.
Cathepsins in basal cell carcinomas: activity, immunoreactivity and mRNA staining of cathepsins B, D, H and L. [Erratum to document cited in CA141:021292]
Arch. Dermatol. Res.
296
94
2004
Homo sapiens
-
Bratkovic, T.; Lunder, M.; Popovic, T.; Kreft, S.; Turk, B.; Strukelj, B.; Urleb, U.
Affinity selection to papain yields potent peptide inhibitors of cathepsins L, B, H, and K
Biochem. Biophys. Res. Commun.
332
897-903
2005
Homo sapiens
Horn, M.; Doleckova-Maresova, L.; Rulisek, L.; Masa, M.; Vasiljeva, O.; Turk, B.; Gan-Erdene, T.; Baudys, M.; Mares, M.
Activation processing of cathepsin H impairs recognition by its propeptide
Biol. Chem.
386
941-947
2005
Homo sapiens (P09668)
Chornaya, V.; Lyannaya, O.
Some physicochemical properties of cathepsin H from human meningioma
Exp. Oncol.
26
278-281
2004
Homo sapiens
Ueno, T.; Linder, S.; Na, C.L.; Rice, W.R.; Johansson, J.; Weaver, T.E.
Processing of pulmonary surfactant protein B by napsin and cathepsin H
J. Biol. Chem.
279
16178-16184
2004
Homo sapiens
Serveau-Avesque, C.; Ferrer-Di Martino, M.; Herve-Grepinet, V.; Hazouard, E.; Gauthier, F.; Diot, E.; Lalmanach, G.
Active cathepsins B, H, K, L and S in human inflammatory bronchoalveolar lavage fluids
Biol. Cell.
98
15-22
2006
Homo sapiens
Torikai, H.; Akatsuka, Y.; Miyazaki, M.; Tsujimura, A.; Yatabe, Y.; Kawase, T.; Nakao, Y.; Tsujimura, K.; Motoyoshi, K.; Morishima, Y.; Kodera, Y.; Kuzushima, K.; Takahashi, T.
The human cathepsin H gene encodes two novel minor histocompatibility antigen epitopes restricted by HLA-A*3101 and -A*3303
Br. J. Haematol.
134
406-416
2006
Homo sapiens (P09668), Homo sapiens
Woischnik, M.; Bauer, A.; Aboutaam, R.; Pamir, A.; Stanzel, F.; de Blic, J.; Griese, M.
Cathepsin H and napsin A are active in the alveoli and increased in alveolar proteinosis
Eur. Respir. J.
31
1197-1204
2008
Homo sapiens (P09668), Homo sapiens
Li, J.; Petrassi, H.; Tumanut, C.; Masick, B.; Trussell, C.; Harris, J.
Substrate optimization for monitoring cathepsin C activity in live cells
Bioorg. Med. Chem.
17
1064-1070
2009
Homo sapiens
Jevnikar, Z.; Rojnik, M.; Jamnik, P.; Doljak, B.; Fonovic, U.P.; Kos, J.
Cathepsin H mediates the processing of talin and regulates migration of prostate cancer cells
J. Biol. Chem.
288
2201-2209
2013
Homo sapiens
Naeem, A.S.; Tommasi, C.; Cole, C.; Brown, S.J.; Zhu, Y.; Way, B.; Willis Owen, S.A.; Moffatt, M.; Cookson, W.O.; Harper, J.I.; Di, W.L.; Brown, S.J.; Reinheckel, T.; O'Shaughnessy, R.F.
A mechanistic target of rapamycin complex 1/2 (mTORC1)/V-Akt murine thymoma viral oncogene homolog 1 (AKT1)/cathepsin H axis controls filaggrin expression and processing in skin, a novel mechanism for skin barrier disruption in patients with atopic dermatitis
J. Allergy Clin. Immunol.
139
1228-1241
2017
Homo sapiens (P09668), Homo sapiens, Mus musculus (P49935), Mus musculus, Mus musculus C57BL/6J (P49935), Rattus norvegicus (P00786)
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