IndraLab

Statements

Chloroquine inhibits CTSB. 14 / 14
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"Inhibition of serine and cysteine proteases, including cathepsins, with leupeptin increases tau secretion (Mohamed et al., 2014), while chloroquine treatment, which inhibits CTSB, CTSD, and CTSL, increases tau accumulation (Hamano et al., 2008), providing additional evidence that cathepsins play an important role in the degradation and clearance of tau."
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"In addition, chloroquine has been shown to inhibit specifically cathepsin B1 (10), a lysosomal protease capable of degrading collagen (18)."
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"At high concentrations, chloroquine also directly inhibits the proteolytic activity of the cysteine endoprotease cathepsin B (Wibo and Poole, 1974)."
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"It is known that addition of chloroquine to lysosomes in vitro causes inhibition of lysosomal cathepsin B [15] and release of the enzyme (s) into the medium [16]."
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"Chloroquine inhibited cathepsin B and diamine oxidase enzyme activities and inhibited protein synthesis[ 11 , 14 ] 4."
| PMC
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"The chloroquine treatment of cells reduced cathepsin B activity of cell lysates prepared from the treated cells (Fig. 9D left panel)."
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"Assessment of the effect of protease inhibitors on the capacity of MCF-7 cells to incorporate [3 H] E 2 confirmed our enzyme immunological data : four lysosomal inhibitors (i.e. chloroquine, NH 4 Cl, [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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ctd
No evidence text available
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"The weak base chloroquine accumulates within acidic intracellular compartments, raises their pH, and can inhibit proteolysis as well as cathepsin B."
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"CQ, monodesthyl chloroquine (mdCQ), amodiaquine (AQ), mdAQ, MF, and quinacrine inhibited cathepsin B in vitro."
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eidos
"Chloroquine inhibited cathepsin B and diamine oxidase enzyme activities and inhibited protein synthesis [ 11 , 14 ] 4 ."
| PMC
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"Chloroquine, at concentrations attained inside the lysosomes, inhibited cathepsin B 1 but not cathepsin D."
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"These include chloroquine [6], which in addition to its weak-base lysosomotropism also inhibits cathepsin B directly [12]; the microtubule poisons vinblastine and colchicine [13], which presumably blo[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As the NLRP3 inflammasome can be activated due to lysosomal damage and release of cathepsin B, ammonium chloride (NH 4 Cl) and chloroquine diphosphate (CQ), which inhibit endosomal-lysosomal system acidification, and CA-074-Me, which acts as a cell-permeable inhibitor of thiol proteases, were used to block lysosomal acidification and cathepsin B activity, respectively."
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