Disease relevance of Casp7

• Caspase 7: increased expression and activation after traumatic brain injury in rats [1].

High impact information on Casp7

• Caspase-7 and caspase-8 were not activated [2].
• The preferred substrate sequence matches the activation sites of caspase 3 and caspase 7 and thus is consistent with the role of granzyme B in activation of these proteases during apoptosis [3].
• Treatment with indirubin derivatives induced the activation of caspase-7 followed by apoptosis in RK3E-ras cells [4].
• CPA and MFA were both shown to effect tumor cell death by stimulating apoptosis, as evidenced by the induction of plasma membrane blebbing, DNA fragmentation, and cleavage of the caspase 3 and caspase 7 substrate poly(ADP-ribose) polymerase (PARP) in drug-treated cells [5].
• These findings, the first to document the up-regulation of caspase 7 in the brain after acute brain injury in rats, suggest that caspase 7 activation could contribute to neuronal cell death on a scale not previously recognized [1].

Biological context of Casp7

• It has been suggested that caspase 7, an apoptosis executioner implicated in cell death proteolysis, is redundant to the main executioner caspase 3 and it is generally believed that it is not present in the brain or present in only minute amounts with highly restricted activity [1].
• While stress signals associated with perturbations of ER functions such as up-regulation of GRP78 was significantly attenuated, other signaling machinery such as activation of caspase-7 transmitting death signals from ER to other organelles could not be altered [6].
• After 30 min at 0xg, immunostaining for the enzyme caspase-7 was present in the cytoplasm of many cells concurrently with DNA fragmentation identified by the TUNEL method [7].

Anatomical context of Casp7

• The activation of caspase 7 protein after TBI, demonstrated by immunoblot by the increase of the active form of caspase 7 peaking 5 days post-injury in the cortex and hippocampus, was found to be up-regulated in both neurons and astrocytes by immunohistochemistry [1].
• The present study was initiated to determine whether AMPA-receptor-induced DCD in PNs is associated with Bax translocation to the mitochondria, cytochrome C release from the mitochondria, changes in mitochondrial potential, and activation of representative initiator and executor caspases that include caspase-9, caspase-3, and caspase-7 [8].

Other interactions of Casp7

• In parallel with these findings, Abeta1-40-induced changes in activation of caspase-9, caspase-7, and caspase-3 were inhibited by pretreatment with SF [9].
• HGF had no effect on apoptotic mediators, such as Fas, Fas-L, or caspase-3 and caspase-7 [10].
• Our results also show that calpain is related to OGD-mediated proteolysis of caspase-3 and -9 but not of caspase-7 [11].

Analytical, diagnostic and therapeutic context of Casp7

• On immunoblotting, there was an increase in the proform of caspase-3 and caspase-7 in Cy/Cy compared to +/+ and Cy/+ kidneys [12].
• Caspase 7-cleavage was investigated by Western blotting and specific antibodies [13].

References