3.4.22.1: cathepsin B
This is an abbreviated version!
For detailed information about cathepsin B, go to the full flat file.
Word Map on EC 3.4.22.1
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3.4.22.1
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cathepsins
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lysosomal
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proteinases
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papain
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collagen
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metastasis
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pancreatic
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cystatins
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procathepsin
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upa
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exopeptidase
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food industry
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myofibrillar
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mansoni
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schistosoma
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lc3-ii
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calpains
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permeabilization
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zymogen
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intralysosomal
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leupeptin
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peptidase
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hyperamylasemia
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pharmacology
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papain-like
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diagnostics
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biotechnology
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collagenase
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antibody-drug
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autophagy-lysosome
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pepstatin
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acinar
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ficin
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plasminogen
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caspase-1
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proenzyme
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legumain
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autophagosomes
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elastase
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caerulein
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caerulein-induced
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molecular biology
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dipeptidyl
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fluorogenic
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inflammasome
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endosomes
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pro-il-1
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supramaximal
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l-like
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b-mediated
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fasciola
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mu-calpain
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medicine
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trypsinogen
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hepatica
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drug development
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collagenolytic
- 3.4.22.1
- cathepsins
- lysosomal
- proteinases
- papain
- collagen
- metastasis
- pancreatic
- cystatins
-
procathepsin
- upa
-
exopeptidase
- food industry
- myofibrillar
- mansoni
- schistosoma
-
lc3-ii
- calpains
-
permeabilization
- zymogen
-
intralysosomal
- leupeptin
- peptidase
-
hyperamylasemia
- pharmacology
-
papain-like
- diagnostics
- biotechnology
- collagenase
-
antibody-drug
-
autophagy-lysosome
- pepstatin
-
acinar
- ficin
- plasminogen
- caspase-1
- proenzyme
- legumain
-
autophagosomes
- elastase
- caerulein
-
caerulein-induced
- molecular biology
-
dipeptidyl
-
fluorogenic
- inflammasome
- endosomes
-
pro-il-1
-
supramaximal
-
l-like
-
b-mediated
- fasciola
- mu-calpain
- medicine
- trypsinogen
- hepatica
- drug development
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collagenolytic
Reaction
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides =
Synonyms
AC-5, AC-cathB-1, AC-cathB-2, APP secretase, cat B, CatB, CatB1, Cath B, Cath-B, CathB, cathepsin B, cathepsin B proteinase, cathepsin B-like AC-5, cathepsin B-like counter-defence protein, cathepsin B-like cysteine protease, cathepsin B-like cysteine protease 1, cathepsin B-type cysteine protease, cathepsin B1, cathepsin B2, cathepsin B5, cathepsin Ba, cathepsin II, cathepsin-B, CmCatB1, CmCatB2, CP-2, CPB, CpCathB, CPR-4, CsCB1, CsCB2, CsCB3, CsCB4, CTB, CTSB, cysteine cathepsin, DEVDase, LycCatB, MmeCB, More, Na-CP-2, Na-CP-3, Na-CP-4, Na-CP-5, NbCathB, nfcpb, nfcpb-L, PcCTSB, rFgCatB2, Sm31, SmCatB, SmCB1, toxopain-1, TrCB1.1, TrCB1.2, TrCB1.3, TrCB1.4, TrCB1.5, TrCB1.6, TsCPB2
ECTree
3.4.22.1 cathepsin BAdvanced search results
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results (Localization
Localization on EC 3.4.22.1 - cathepsin B
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LOCALIZATION 
ORGANISM
UNIPROT
COMMENTARY 
GeneOntology No.
LITERATURE
SOURCE
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cathepsin B is synthesised as a pre-pro-enzyme and the primary pathways for its normal trafficking to the lysosome utilise mannose-6-phosphate receptors. Inactive pro-cathepsin-B is processed to active single and double chain forms of cathepsin-B in the late endosomes and lysosomes, respectively
cathepsin B activity is detected in exosomes isolated from hydrogen peroxide treated cells
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additional information
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of the lysosomal fraction, co-localization of active cathepsin B and its cell surface binding partners, S100A/p11 of the annexin II heterotetramer, to caveolae of human umbilical vein endothelial cells and colorectal carcinoma cells
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phagocytosis of crystalline silica induces lysosomal destabilization and subsequent release of cathepsin B into the cytoplasm, leading to NALP3 activation
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in oxidative stress cathepsin B may be released from lysosomes into cytoplasm with lowered pH and cleave cytoplasmic proteins, including caspase-3 substrates
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cathepsin B is secreted as an inactive precursor form, up-regulation of cathepsin B expression and enhanced secretion in mitochondrial DNA-depleted osteosarcoma cells resulting, at least in part, from the activation of the transcription factor NF-kappaB
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under certain conditions cathepsin-B may be secreted extracellularly as a pro-enzyme that requires proteolytic activation
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release from intestine mucosa after mechanical injury and during initial post-traumatic stages
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the enzyme is released by activated microglia accumulating in the granule cell layer of the lingual and central lobe
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36634, 678699, 680996, 695447, 696631, 698029, 699130, 699208, 699337, 707625, 707967, 707971, 708035, 708258, 708264, 708275, 708277, 708376, 708482, 708641, 709347, 709771, 709916, 710205, 710254
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cathepsin B is synthesised as a pre-pro-enzyme and the primary pathways for its normal trafficking to the lysosome utilise mannose-6-phosphate receptors. Inactive pro-cathepsin-B is processed to active single and double chain forms of cathepsin-B in the late endosomes and lysosomes, respectively
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phagocytosis of crystalline silica induces lysosomal destabilization and subsequent release of cathepsin B into the cytoplasm, leading to NALP3 activation
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cathepsin B is expressed ubiquitously and represents the major portion of lysosomal enzymes
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in oxidative stress cathepsin B may be released from lysosomes into cytoplasm with lowered pH and cleave cytoplasmic proteins, including caspase-3 substrates
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of sea urchin eggs, in lysosomal cytoplasmic organelles
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of sea urchin eggs, in lysosomal cytoplasmic organelles
additional information
Alexa Fluor 488 labeled intracellular cathepsin B is localized in vesicle-like structures in the perinuclear region of HUVECs
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additional information
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Alexa Fluor 488 labeled intracellular cathepsin B is localized in vesicle-like structures in the perinuclear region of HUVECs
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additional information
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the enzyme is secreted to blood or body fluids in patients with cancers such as leptomeningeal metastasis or hepatocellular carcinoma
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additional information
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imatinib mediates redistribution of cathepsin B, Iiatinib or BCR-ABL knockdown induces lysosomal membrane permeabilization that culminates in activation and redistribution of cathepsin B into the cytoplasm of chronic myelogenous leukemia cells
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additional information
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release of specific proteases such as cathepsin B seems to be causally related to inflammasome activation
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additional information
enzymatic activity increases significantly in the injury epicenter at 5 and 7 days post-injury
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