Table 2.

Summary of the phenotypes of caspase-3 deficient mice

GenotypeGenetic backgroundPhenotypeMechanismRef
Caspase-3−/− B6.129S1 Reduction in total skeletal muscle mass; Myoblasts display a differentiation defect Proteolytic function of caspase-3 activates MST1 and leads to myoblast differentiation Fernando et al. (2002)  
Caspase-3−/− C57Bl/6 Deletion preserves hematopoietic stem cell pool but perturbs their differentiation without affecting cell viability Caspase-3 alters signal transduction by limiting activation of the Ras-Raf-MEK-ERK pathway Janzen et al. (2008)  
Caspase-3−/− C57Bl/6 Defects in skin wound healing and in liver regeneration Caspase-3 stimulates production of PGE2, to promote cell proliferation and tissue regeneration, Li et al. (2010b)  
Caspase-3−/− C57BL/6 Decreased incidence of chemically induced skin cancer Caspase-3 activation of ENDOG enhances radiation-induced DNA damage and oncogenic transformation Liu et al. (2015)  
Caspase-3−/− B6.129S1 Embryonic lethal, defective brain development NA Kuida et al. (1996)  
Caspase-3−/− C57BL/6 Increased renal lesions and mild splenomegaly Increased expression of inflammatory Casp12, was observed in these Caspase-3 KO kidneys Suzuki et al. (2020)  
Caspase-3−/−7−/− (conditional cardiac-specific KO mice) C57BL/6 Hypoplastic neonatal heart with reduced number of cardiomyocytes Caspase 3 and 7 regulate expression of genes involved in cell cycle independent of their proteolytic activity Cardona et al. (2015)  
Caspase-3−/−7−/− (conditional intestinal-specific KO mice) C57BL/6N Normal intestinal development NA Ghazavi et al. (2022)  
Caspase-3−/− B6.129S1 Delayed ossification and decreased bone mineral density Caspase-3 regulates the TGF-β/Smad2 signaling pathway and cellular senescence Miura et al. (2004)  
Caspase-3−/− B6.129S1 Diminished cell proliferation and reduced sebaceous gland size Caspase-3 cleaves α-catenin and facilitates activation and nuclear translocation of YAP1 Yosefzon et al. (2018)  
GenotypeGenetic backgroundPhenotypeMechanismRef
Caspase-3−/− B6.129S1 Reduction in total skeletal muscle mass; Myoblasts display a differentiation defect Proteolytic function of caspase-3 activates MST1 and leads to myoblast differentiation Fernando et al. (2002)  
Caspase-3−/− C57Bl/6 Deletion preserves hematopoietic stem cell pool but perturbs their differentiation without affecting cell viability Caspase-3 alters signal transduction by limiting activation of the Ras-Raf-MEK-ERK pathway Janzen et al. (2008)  
Caspase-3−/− C57Bl/6 Defects in skin wound healing and in liver regeneration Caspase-3 stimulates production of PGE2, to promote cell proliferation and tissue regeneration, Li et al. (2010b)  
Caspase-3−/− C57BL/6 Decreased incidence of chemically induced skin cancer Caspase-3 activation of ENDOG enhances radiation-induced DNA damage and oncogenic transformation Liu et al. (2015)  
Caspase-3−/− B6.129S1 Embryonic lethal, defective brain development NA Kuida et al. (1996)  
Caspase-3−/− C57BL/6 Increased renal lesions and mild splenomegaly Increased expression of inflammatory Casp12, was observed in these Caspase-3 KO kidneys Suzuki et al. (2020)  
Caspase-3−/−7−/− (conditional cardiac-specific KO mice) C57BL/6 Hypoplastic neonatal heart with reduced number of cardiomyocytes Caspase 3 and 7 regulate expression of genes involved in cell cycle independent of their proteolytic activity Cardona et al. (2015)  
Caspase-3−/−7−/− (conditional intestinal-specific KO mice) C57BL/6N Normal intestinal development NA Ghazavi et al. (2022)  
Caspase-3−/− B6.129S1 Delayed ossification and decreased bone mineral density Caspase-3 regulates the TGF-β/Smad2 signaling pathway and cellular senescence Miura et al. (2004)  
Caspase-3−/− B6.129S1 Diminished cell proliferation and reduced sebaceous gland size Caspase-3 cleaves α-catenin and facilitates activation and nuclear translocation of YAP1 Yosefzon et al. (2018)  

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