3.4.22.1 amyloid beta peptide + H2O cathepsin B is involved in degradation of amyloid beta peptides, its inhibition can lead to amyloid beta accumulation, an early trigger of Alzheimer's disease, cystatin C regulates the enzyme negatively, CysC ablation ameliorates amyloid beta-associated neuronal and synaptic deficits in hippocampal circuits, neuroprotective effects of CysC ablation depend on CatB, overview 3.4.22.1 amyloid beta precursor protein + H2O cathepsin B selectively cleaves the wild-type beta-secretase site but not the rare Swedish mutant beta-secretase site 3.4.22.1 amyloid-beta + H2O - 3.4.22.1 caspase 1 precursor + H2O - 3.4.22.1 Collagen + H2O - 3.4.22.1 Collagen IV + H2O - 3.4.22.1 Collagen IV + H2O collagen IV of the basement membrane damaged by cathepsin B, that is released after mechanical injury, during initial post-traumatic stages, overview 3.4.22.1 Gelatin + H2O - 3.4.22.1 Laminin + H2O laminin of the basement membrane damaged by cathepsin B, that is released after mechanical injury, during initial post-traumatic stages, overview 3.4.22.1 additional information enzyme is involved in myoblast-myoblast fusion 3.4.22.1 additional information CmCatB2 may be an inactive protease isoform resulting from splicing errors 3.4.22.1 additional information absence of Ctsb significantly impairs development of high-grade invasive ductal carcinomas and reduces the metastatic burden in the lungs, and cancer cells lacking Ctsb exhibit significantly higher resistance to apoptosis induction by the lysosomotropic agent Leu-Leu-OMe 3.4.22.1 additional information autocatalytic activation of the inactive proenzyme 3.4.22.1 additional information cathepsin B belongs to the lysosomal cysteine cathepsins, a third major class of matrix-degrading enzymes involved in tumor invasion and tissue remodeling. Cathepsin B is involved in matrix degradation at podosomes, cysteine protease inhibitors reduce matrix degradation and invasion in vitro 3.4.22.1 additional information cathepsin B is a lysosomal cysteine protease of the papain-like enzyme family with multiple biological functions 3.4.22.1 additional information cathepsin B is a target of Hedgehog signaling in pancreatic cancer, downregulation of CATB by Hedgehog, cyclopamine reduces CATB protein and mRNA levels. CATB might influence pancreatic cancer cell invasiveness 3.4.22.1 additional information cathepsin B is an intracellular lysosomal cysteine proteinase that can degrade extracellular components including collagen and protein turnover in the lysosomal system. Cathepsin B plays an important role in the resolution of organic matrix, a final step in bone resorption. It is also known to play an important role in the initiation and perpetuation of inflammatory processes 3.4.22.1 additional information cathepsin B is expressed in cerebral aneurysms and promotes the progression of cerebral aneurysms, which include degradation of extracellular matrix in arterial walls in strong subarachnoid hemorrhage, overview 3.4.22.1 additional information cathepsin B is expressed in induced cerebral aneurysms and promotes the progression of cerebral aneurysms, which include degradation of extracellular matrix in arterial walls in strong subarachnoid hemorrhage, overview 3.4.22.1 additional information cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages 3.4.22.1 additional information cathepsin B plays a key role in parasite infection, overview 3.4.22.1 additional information cathepsin B plays an essential role in the pathogenesis of fulminant hepatic failure, and the cathepsin B inhibitor CA-074me can attenuate apoptosis and liver injury, overview 3.4.22.1 additional information cathepsin B secreted by activated microglia is closely associated with the MeHg-induced severe pyknotic changes of the cerebellar granule cells, overview. Cathepsin B is involved in apoptotic processes 3.4.22.1 additional information cathepsin B, together with cathepsin L, urokinase-type plasminogen activator and its inhibitor PAI-1, plays an important role in colorectal cancer invasion. Correlation analysis of proteolytic enzymes in colorectal cancer, overview 3.4.22.1 additional information cathepsin-B is a lysosomal cysteine proteasewith broad substrate specificity, which belongs to a family of 11 cysteine proteases. The enzyme is involved in tumor progression, e.g. of endometrial carcinomas 3.4.22.1 additional information cysteine cathepsins play a critical role in the biologic activity of tumor-shed vesicles at acidic pH, but not at physiological pH, endothelial cell invasiveness is increased by tumor-shed vesicles exposed to acidic pH, overview 3.4.22.1 additional information differential regulation of snail cathepsin B transcript pre- and postparasite exposure, overview 3.4.22.1 additional information disturbances in the regulation of the intracellular activities and uncontrolled release of cathepsins from lysosomes have been implicated in many disease states, such as osteoporosis, inflammatory diseases, and tumor progression 3.4.22.1 additional information effective inhibition of cathepsin B can decrease the severity of joint inflammation and to reduce the destruction of particular tissues in the rat model of antigen adjuvant-induced arthritis 3.4.22.1 additional information increased cathepsin B levels in acute and chronic lung diseases resulting from high levels of extracellular neutrophil elastase, expression of the protease can be inhibited by alpha1-antitrypsin augmentation therapy 3.4.22.1 additional information inhibitors of cathepsin B improve memory and reduce beta-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, beta-secretase site of the amyloid precursor protein 3.4.22.1 additional information NF-kappaB induced up-regulation of cathepsin B expression contributes to the invasive property of the 143B cells lacking mtDNA, overview. Extracellularly released cathepsin B can act alone or in concert with some matrix metalloproteinases 3.4.22.1 additional information participation of cathepsin B in emodin-induced apoptosis in HK-2 cells, enzyme inhibition by Ca-074 causes significant attenuation the ratio of hypodiploid and apoptotic cells, partially blockage of caspase 3 activation and inhibition of reduction of cell viability induced by emodin, overview 3.4.22.1 additional information Porphyromonas gingivalis strain 381 or its lipopolysaccharides increases the expression of cathepsin B in oral epithelial cells 3.4.22.1 additional information regulation of cathepsin B in gingival fibroblasts involves interleukin-6 and its receptor along with the Cav-1-JNK-AP-1 pathway, overview 3.4.22.1 additional information the enzyme has a principle function in gross protein degradation of internalized proteins within endo-lysosomes, but cathepsins are also involved in the processing of precursor proteins to biologically active peptides in endosomes of entero-endocrine cells. Cathepsin B, released form intestinal mucosa due to mechanical injury, plays an important role in extracellular matrix damage and the onset of postoperative ileus, an inevitable consequence of abdominal surgery, in that it contributes to disintegration of the basement membrane of the gastrointestinal tract in early post-traumatic phases. Cathepsin B is best known for its critical contribution to enhanced tumor cell invasion and metastasis, including colorectal carcinomas, by degradation of extracellular matrix components 3.4.22.1 additional information the enzyme is involved in degradation of extracellular matrix and of basement membrane components leading to tumor invasion in the intestine. Expression of matrix metalloproteinase-9 and cathepsin B is correlated with lymph node metastasis in advanced gastric carcinoma, but not with patients' postoperative survival, overview. Correlation between the synthesis of cysteine and serine proteases and the potential tumor invasion 3.4.22.1 additional information the enzyme is involved in extracellular matrix degradation in caveolae of endothelial cells during tube formation, overview. Cathepsin B regulates both pro- and anti-angiogenic factors and may be a contributor to the angiogenic switch of endothelial cells 3.4.22.1 additional information the enzyme is involved in inflammatory processes 3.4.22.1 additional information the enzyme plays an important role in cancer invasion and metastasis, the enzyme content is positively correlated with tumors in different tissue types 3.4.22.1 additional information under certain conditions, e.g. in hypoxia, cathepsin B participates in cleavage of caspase-3 substrates in brain cells 3.4.22.1 additional information autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region and can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins 3.4.22.1 myristoylated alanine-rich C kinase substrate + H2O i.e. MARCKS 3.4.22.1 ovalbumin + H2O - 3.4.22.1 Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O albumin-binding prodrug of doxorubicin, which incorporates a maleimide moiety and a 4-aminobenzyloxycarbonyl spacer coupled to the dipeptide Phe-Lys, is cleaved by cathepsin B and in tumor homogenates of MDA-MB 435 tumor cells from in vitro culture transplanted subcutaneously into the left flank region of mice, overview 3.4.22.1 Proteins + H2O - 3.4.22.1 Proteins + H2O degradation of tissue proteins within lysosomes 3.4.22.1 Proteins + H2O turnover of intracellular proteins 3.4.22.1 Proteins + H2O muscle proteins 3.4.22.1 Proteins + H2O plays a role in cancer invasion and metastasis 3.4.22.1 Proteins + H2O enzyme activation and conversion of precursor proteins to their active form 3.4.22.1 TNF-alpha + H2O cathepsin B is required for optimal posttranslational processing of TNF-alpha 3.4.22.1 TNF-alpha + H2O cathepsin B is required for optimal posttranslational processing of TNF-alpha in response to the bacterial cell wall component lipopolysacchrides