 
            IndraLab
Statements
USP7 inhibits apoptotic process. 121 / 121
                        
    
      
      
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
        
      
      
    
      
      
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                                  "Ubiquitin-specific peptidase 7, a widely studied deubiquitinase, promoted chondrocyte proliferation and suppressed tumour necrosis factor alpha (TNF-α)-induced apoptosis and inflammation via inhibiting eIF2α-ATF4-CHOP signaling and nuclear factor-kappa B (NF-κB)/p65 signaling, thereby preventing the occurrence of OA [56, 57]."
          
                              
          
                               
                            
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                                  "Our finding suggests that EZH2, a tumorigenesis-related gene, can change transcriptional profile by abnormally establishing facultative heterochromatin at euchromatic regions.Both STAT3 and USP7 promote cell proliferation and prevent apoptosis [ [23,[30], [31], [32]]], and are advantageous to cancer cells’ survival."
          
                              
          
                               
                            
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                                  "However, another study reported that USP7 promotes chondrocyte proliferation and inhibits apoptosis and tumor necrosis factor-α-induced inflammatory response by inhibiting the BiP-eIF2α-ATF4-CHOP signaling pathway and NF-κB/p65 signaling pathway of endoplasmic reticulum stress [34]."
          
                              
          
                               
                            
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                                  "Our results show that inhibition of USP7 by a small molecule or genetic depletion can selectively induce apoptosis in several types of SnCs at least in part via restoring p53 activity, which in turn induces the pro‐apoptotic proteins PUMA, NOXA, and FAS and inhibits the interaction of BCL‐XL and BAK because SnCs are more sensitive to the perturbation of mitochondrial apoptotic pathways than non‐SnCs (Chang et al., 2016; Yosef et al., 2016; Zhu et al., 2017)."
          
                              
          
                               
                            
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                                  "These findings suggest that USP7 inhibition selectively induces SnC apoptosis at least in part by increasing p53 translocation to mitochondria and its interaction with BCL‐XL, since SnCs are more dependent on BCL‐2 family proteins for survival compared to non‐SnCs (Chang et al., 2016; Yosef et al., 2016; Zhu et al., 2016)."
          
                              
          
                               
                            
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                                  "Thus, USP7 is a new senolytic target and USP7 inhibitors are novel senolytic agents at least for some SnCs which downregulate their expression of p53 after they become senescent.However, USP7 has multiple targets (Pozhidaeva & Bezsonova, 2019) and p53 knockout only attenuated but did not abrogate USP7 inhibition‐induced SnC apoptosis."