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Last update 08 May 2025

CTSB x cysteine protease

Last update 08 May 2025

Basic Info

Related Targets

CTSBcysteine protease

Drugs associated with CTSB x cysteine protease

Aloxistatin

Target

CTSB x cysteine protease

Mechanism

CTSB inhibitors [+1]

Active Org.

Sunnybrook Health Sciences Centre [+3]

Originator Org.

Sunnybrook Health Sciences Centre

Active Indication

Anti-Glomerular Basement Membrane Disease [+2]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with CTSB x cysteine protease

DRKS00028033

/ CompletedPhase 1

CoViD-19 treatment by Aloxistatin-Inhalation – a phase I trial to evaluate the safety of inhalable aloxistatin (E64d) - COALITION-I

Start Date05 Jun 2023

Sponsor / Collaborator-

100 Clinical Results associated with CTSB x cysteine protease

100 Translational Medicine associated with CTSB x cysteine protease

0 Patents (Medical) associated with CTSB x cysteine protease

671

Literatures (Medical) associated with CTSB x cysteine protease

01 Jul 2025·Journal of Invertebrate Pathology

Infection of two cestode larvae, Nybelinia enterika sp. nov. and Phoreiobothrium sp. in oval squid Sepioteuthis lessoniana species complex

Article

Author: Zifcakova, Lucia ; Nakamura, Shinichi ; Zoral, Mehmet Arif ; Miller, Jonathan ; Lajbner, Zdenek

Recently, oval squid of Sepioteuthis lessoniana species complex has gained importance in aquaculture due to its successful breeding in semi-intensive and intensive aquaculture systems. However, there is a lack of information regarding pathogens and diseases that can affect this species, prompting the need for further research. Two cestode species, Nybelinia enterika sp. nov. and Phoreiobothrium sp., were identified as members of the Trypanorhyncha and Onchoproteocephalidea orders, respectively, using both morphological and molecular diagnostic markers in wild-caught oval squids (Sepioteuthis lessoniana sp.1, S. lessoniana sp.2, S. lessoniana sp.3). These cestode species were found to use the oval squids as intermediate hosts. In histopathology samples, the infected squid with N. enterika was surrounded by numerous hemocytes in the infected area. In the genomes of both cestode species, we identified multiple genes for enzymes involved in cephalopod tissue degradation, such as cysteine proteases including cathepsin-L, cathepsin-D, cathepsin-A, cathepsin-B, cathepsin-K, and cathepsin-S. These enzymes potentially help the parasites manipulate the squid immune system and neutralize squid hemocytes. The detection of these parasites in wild squid populations, with 100% prevalence in Okinawa, is concerning as the effect of these parasites on human consumers' health remains unknown. However, our research demonstrated that fully cultured squid remain completely cestode parasite-free, indicating they are more likely to meet the highest standards for food safety and quality.

01 Jun 2025·Biochemical Pharmacology

The SGLT2 inhibitor dapagliflozin suppresses endothelial cell pyroptosis mediated by the NF-κB/NLRP3 pathway through downregulation of CTSB

Article

Author: Liu, Danan ; Zhao, Quanwei ; Liao, Fujun ; Li, Hui ; Chen, Long ; Gong, Caiwei ; Zhou, Bo

Atherosclerosis (AS) is a chronic inflammatory disease, and pyroptosis-a recently discovered pro-inflammatory programmed cell death process-can exacerbate these inflammatory responses. Vascular endothelial cell pyroptosis contributes to AS progression. Cathepsin B (CTSB) is a crucial member of the cysteine protease family found in lysosomes. However, its exact role in vascular endothelial cell pyroptosis remains unclear. Dapagliflozin (DAPA), a sodium-glucose cotransporter-2 (SGLT2) inhibitor, inhibits pyroptosis and alleviates AS independent of its hypoglycemic effect. This study utilized oxidized low-density lipoprotein (ox-LDL) to induce pyroptosis in human umbilical vein endothelial cells (HUVECs) and investigated the effect of this process. The study revealed that ox-LDL induced HUVEC pyroptosis in a concentration-dependent manner, resulting in Na⁺ and Ca²⁺ overload, lysosomal damage, and increased CTSB release into the cytosol. Lentiviral vectors were used to overexpress or silence CTSB; subsequent analysis revealed that CTSB promotes NLRP3-mediated pyroptosis through nuclear factor κB (NF-κB) activation. Finally, we found that DAPA attenuated HUVEC pyroptosis by inhibiting the NF-κB/NLRP3 pathway and decreasing the expression of CTSB. This effect may be attributed to its ability to alleviate lysosomal damage caused by Na⁺-Ca²⁺ overload, thereby reducing CTSB release into the cytosol.

02 Apr 2025·ACS Chemical Neuroscience

Activation of Cytosolic Cathepsin B Activity in the Brain by Traumatic Brain Injury and Inhibition by the Neutral pH Selective Inhibitor Probe Z-Arg-Lys-AOMK

Article

Author: Rissman, Robert A. ; Podvin, Sonia ; Spencer, Brian ; Florio, Jazmin ; O’Donoghue, Anthony J. ; Yoon, Michael C. ; Guzman, Estefani ; Hook, Vivian ; Mosier, Charles ; Gerwick, William H. ; Mante, Michael ; Phan, Von V. ; Almaliti, Jehad ; Arias, Carlos

Cathepsin B has been shown to contribute to deficits in traumatic brain injury (TBI), an important risk factor for Alzheimer's disease (AD). Cathepsin B is elevated in TBI and AD patients, as well as in animal models of these conditions. Knockout of the cathepsin B gene results in amelioration of TBI-induced motor dysfunction and improvement of AD memory deficit in mice. The mechanism of cathepsin B pathogenesis in these brain disorders has been hypothesized to involve its translocation to the cytosol from its normal lysosomal location. This study, therefore, evaluated brain cytosolic cathepsin B activity in the controlled cortical impact (CCI) mouse model of TBI. CCI-TBI resulted in motor deficits demonstrated by the rotarod assay, brain tissue lesions, and disorganization of the hippocampus. Significantly, CCI-TBI increased cytosolic cathepsin B activity in the brain cortex in the ipsilateral brain hemisphere that received the CCI-TBI injury, with a concomitant decrease in the lysosomal fraction. Cathepsin B activity was monitored using the substrate Z-Nle-Lys-Arg-AMC which specifically detects cathepsin B activity but not other cysteine proteases. The normal lysosomal distribution of cathepsin B was observed by its discrete localization in brain cortical cells. CCI-TBI resulted in a more diffuse cellular distribution of cathepsin B consistent with translocation to the cytosol. Further studies utilized the novel neutral pH-selective inhibitor, Z-Arg-Lys-AOMK, that specifically inhibits cathepsin B at neutral pH 7.2 of the cytosol but not at acidic pH 4.6 of lysosomes. Daily administration of Z-Arg-Lys-AOMK (ip), beginning 1 day before CCI-TBI, resulted in the reduction of the increased cytosolic cathepsin B activity induced by CCI-TBI. The inhibitor also reduced cathepsin B activities in homogenates of the brain cortex and hippocampus which were increased by CCI-TBI. Furthermore, the Z-Arg-Lys-AOMK inhibitor resulted in the reduction of motor function deficit resulting from CCI-TBI. These findings demonstrate the activation of cytosolic cathepsin B activity in CCI-TBI mouse brain injury.

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