Gene interactions and pathways from curated databases and text-mining

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CASP3 — CTSB

Text-mined interactions from Literome

Knoblach et al., J Cereb Blood Flow Metab 2004 (Brain Injuries...) : Neither the 120 kD caspase mediated alpha-spectrin cleavage product nor cathepsin B were expressed after maitotoxin injury
Guicciardi et al., Gastroenterology 2005 : These data suggest that tumor necrosis factor alpha triggers Bid dependent lysosomal permeabilization, followed by release of cathepsin B into the cytosol and activation of caspase 2
Ben-Ari et al., Apoptosis 2005 (Reperfusion Injury) : Recently, it was demonstrated that the release of cathepsin B , a cysteine protease, from the cytosol in liver injury induces mitochondrial release of cytochrome c and the activation of caspase-3 and -9, thereby leading to apoptosis
Yeung et al., J Biol Chem 2006 (Pancreatic Neoplasms) : PS-341 induced caspase-2 activation was attenuated by a selective pharmacological inhibitor of cathepsin B ( R-3032 ), suggesting that cathepsin B release occurs upstream of caspase-2
Paris et al., Apoptosis 2007 : A cathepsin B/L inhibitor partially suppresses caspase activation and apoptosis induction, indicating signaling between lysosomes and mitochondria
Huang et al., J Pharmacol Exp Ther 2009 : Taken together, we show that GSK-3beta exhibits a mechanism of ER stress induced lysosomal apoptosis in leukemia involving caspase-2 induced LMP and cathepsin B relocation, which result in caspase-8 and -3 activation
Zheng et al., PloS one 2012 (Necrosis...) : IL-1ß secretion was reduced in the presence of cathepsin B inhibitors, suggesting that activation of caspase-1 requires cathepsin B activity
Sun et al., J Neurosci 2012 (Chronic Pain...) : There is increasing evidence that cathepsin B (CatB) , a typical lysosomal cysteine protease, is involved in the pro-caspase-1 activation and the subsequent maturation of IL-1ß and IL-18
Morchang et al., Biochem Biophys Res Commun 2013 : Treatment with cathepsin B inhibitor also reduced the activity of caspase 9, suggesting that cathepsin B activates both caspase-9 and caspase-3
Jones et al., Am J Physiol 1998 (Liver Neoplasms, Experimental) : Our data demonstrate that 1 ) bile salt induced apoptosis can be inhibited by the cystatin A transgene and 2 ) caspase and cathepsin B activation are linked mechanistically with cathepsin B downstream of caspases
Schotte et al., Biochem Biophys Res Commun 1998 (Inflammation) : Cathepsin B-mediated activation of the proinflammatory caspase-11
Vancompernolle et al., FEBS Lett 1998 : All newly described activities of cathepsin B , namely processing of caspase zymogens and induction of nuclear apoptosis, are inhibited by the synthetic peptide caspase inhibitors z-VAD.fmk, z-DEVD.fmk and to a lesser extent by Ac-YVAD.cmk
Schotte et al., FEBS Lett 1999 : In addition, the caspase inhibitors z-VAD.fmk, z-DEVD.fmk and Ac-YVAD.cmk also efficiently inhibited cathepsin B activity in vitro and in tissue culture cells at concentrations that are generally used to demonstrate the involvement of caspases