Disease relevance of Ctsb

• The induction of Ctsb messenger RNA in the infected middle ear mucosa suggests a role in early tissue injury; thus, Ctsb may represent a potential target for molecular diagnostics and/or rational intervention during the development of acute otitis media [1].
• Cathepsin B mRNA and protein expression following contusion spinal cord injury in rats [2].
• We provide the first data that cathepsin B (Cath B), a lysosomal cysteine protease, is up-regulated following contusion-spinal cord injury (SCI) [2].
• Cathepsin B (Cath B), a potent lysosomal protease, has also been implicated in the pathology of CNS diseases including brain tumors, Alzheimer's disease, amyotrophic lateral sclerosis and stroke [3].
• Immunofluorescence studies showed MMP-9, calpain, and cathepsin B activation colocalized to both neurons and the neurovascular endothelial cells after ischemia, which was reduced by E64d [4].

High impact information on Ctsb

• Mucosal presence and activity of cysteine PI and cathepsin B have also been investigated in the pathogenesis of chemically induced HML [5].
• We extracted and partially isolated acid and thermostable inhibitors of cathepsin B in the gastric mucosa, and found rapid inactivation of PI and activation of cathepsin B in the early phase of E- or A-induced HML [5].
• Ubiquitin mRNA in muscle returned to control levels within 24 h after cessation of acidosis. mRNA for subunits of the proteasome (C2 and C3) in muscle were also increased 4-fold and 2.5-fold, respectively, with acidosis; mRNA for cathepsin B did not change [6].
• In vitro cathepsin B redistribution also occurs when rat pancreatic fragments are incubated with plasma obtained from opossums with hemorrhagic necrotizing pancreatitis caused by bile/pancreatic duct ligation [7].
• As a result, lysosomal hydrolases such as cathepsin B are redistributed to the subcellular zymogen granule-rich fraction and lysosomal hydrolases as well as digestive enzyme zymogens are colocalized within large cytoplasmic vacuoles [7].

Chemical compound and disease context of Ctsb

• Inhibitors of prostaglandin synthesis or cathepsin B prevent muscle wasting due to sepsis in the rat [8].
• Luepeptin, a cathepsin B inhibitor, and indomethacin, a prostaglandin synthesis inhibitor, prevented muscle atrophy and impaired contractility [8].
• This study aimed, firstly, to determine the effect of ethanol on the content and messenger RNA levels of pancreatic digestive enzymes and on the messenger RNA level of the lysosomal enzyme cathepsin B, and secondly, to examine the influence of concomitant protein deficiency (a known association of alcoholism and pancreatic injury) on these effects [9].
• Cathepsin B and L in nephron segments of rats with puromycin aminonucleoside nephrosis [10].
• Peptidyl fluoromethyl ketones as inhibitors of cathepsin B. Implication for treatment of rheumatoid arthritis [11].

Biological context of Ctsb

• The changes in Ctsb and Ctsk gene expression were sustained at 48 hours [1].
• The rate of hydrolysis of three cysteine-type proteinase substrates, N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-coumarylamide (AMC) (cathepsin B), Arg-AMC (cathepsin H), and N-benzyloxycarbonyl-Phe-Arg-AMC (cathepsin L), were determined in rat lung throughout the time course of the induction of Pneumocystis carinii infection by immunosuppression [12].
• Using in situ hybridization, we have established that RSG-2 mRNA is expressed in the luminal epithelial cells of the prostate and mammary gland that are known to undergo active cell death, suggesting that it may be a general marker for secretory epithelial cell death [13].
• The kinetics of the response to cathepsin B and cathepsin L after infection of sheep and rats confirm the temporal expression of these proteins during the life cycle of the parasite [14].
• These results indicate a specific increase in VYS cathepsin B and L activities late in gestation [15].

Anatomical context of Ctsb

• Specifically, at 12 hours, Ctsk and Ctsl messenger RNA that was abundantly expressed in the normal middle ear mucosa was decreased, whereas Ctsb transcript was induced [1].
• Trafficking of lysosomal cathepsin B-green fluorescent protein to the surface of thyroid epithelial cells involves the endosomal/lysosomal compartment [16].
• In in situ hybridization, cathepsin B mRNA localized to the mononuclear cell infiltrate in injured muscle, and only background levels of hybridization were observed either over muscle cells in injured tissue or in uninjured muscle [17].
• Cathepsin B, a cysteine protease implicated in metastatic progression, is also expressed during regression of the rat prostate and mammary glands [13].
• These results suggest that RSG-2, or cathepsin B, is required for the local degradation of the basement membrane, which is one of the earliest morphologically recognizable events of active cell death [13].

Associations of Ctsb with chemical compounds

• The lysosomal cysteine proteinase cathepsin B (EC 3.4.22.1) plays an important role in protein catabolism and has also been implicated in various disease states [18].
• The two forms of cathepsin B which degraded Z-Phe-Arg-NMec, Z-Arg-Arg-NNap and BANA were very sensitive to p-CMB and leupeptin [19].
• Analysis of the distribution of the cathepsin B protein by immunofluorescence microscopy demonstrates that there is diffuse, but punctate, expression of the protein in all of the luminal epithelial cells of the normal prostate and mammary gland [13].
• The specific substrates for cathepsin B (Z-Arg-Arg-NHMec) and cathepsin H (Arg-NHMec) were not hydrolysed by trypanopain-Tc under the conditions tested [20].
• In addition, by using CM-cellulose column chromatography, cathepsin B and L were separated and the level of cathepsin L activity increased significantly [21].

Regulatory relationships of Ctsb

• Our results indicate that cathepsin B redistribution occurs when rat pancreatic fragments are incubated with a supramaximally stimulating concentration of the cholecystokinin analogue caerulein along with plasma from an animal subjected to in vivo supramaximal caerulein stimulation [7].
• Conditioned medium from activated microglia or cathepsin B alone induced neuronal apoptosis and caspase 3 activation [22].
• These results demonstrate (1) that cathepsin B expression in the thyroid is regulated in parallel with that of thyroglobulin and actin, and (2) that cyclic AMP- and Ca2+-dependent processes stimulate gene expression, while phorbol ester treatment inhibits gene expression in FRTL5 cells [23].
• The neutral proteinase and cathepsin B-like activity were inhibited by leupeptin and not by pepstatin while the converse obtained for cathepsin D activity [24].
• Moreover, 4-hour pre-infusion of ethanol caused a significant increase in pancreatic cathepsin B output stimulated by caerulein (0.2 microgram/kg.hr) and secretin (0.2 CU/kg.hr) compared with the control rats [25].

Other interactions of Ctsb

• The 252-residue sequence of cathepsin B and the 220-residue sequence of cathepsin H were determined largely by automated Edman degradation of their intact polypeptide chains and of the two chains of each enzyme generated by limited proteolysis [26].
• Cathepsin B-like and cathepsin L-like activities fell below control values initially, but from week 8 of the immunosuppressive treatment significant increases above the control were noted [12].
• Cathepsin B, a lysosomal cysteine proteinase, is involved in limited proteolysis of thyroglobulin with thyroxine liberation at the apical surface of thyroid epithelial cells [16].
• BACKGROUND AND PURPOSE: Matrix metalloproteinases (MMPs) and cysteine proteases (calpain and cathepsin B) play an important role in cell death and are upregulated after focal cerebral ischemia [4].
• The carbohydrate of cathepsin B consisted of a single residue of glucosamine and trace mannose [27].

Analytical, diagnostic and therapeutic context of Ctsb

• Immunogold/electron microscopy showed specific staining for cathepsin B only in lysosome-like structures in cells of the mononuclear cell infiltrate in injured muscle [17].
• In the regressing prostate, RSG-2 mRNA levels peak at 3-4 days after castration, at the time that tissue regression is maximal [13].
• METHODS: Cathepsin B was identified in rat ocular tissues by Western blotting and immunohistochemistry [28].
• Cathepsin B, L and H were also detected by using an immunoblotting procedure in which their bands were expressed after differentiation was induced by the increasing calcium concentration [21].
• Hepatic collagenase activity was similar to the control; however, hepatic cathepsin B and cathepsin L activity and the intracellular degradation of newly synthesized collagen were markedly decreased 3, 5, and 7 days after partial hepatectomy compared with the controls [29].

References