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Abstract
Cells can die through various biochemical pathways related to complex pathophysiological process. Different types of cell death are closely associated with microbial infection. Several regulatory mechanisms of cell death during bacterial infection play important roles to control the pathogens. Bacteria usually manipulate host defense mechanisms to survive and eventually replicate. Host cell death is one of the intrinsic immune defense mechanisms even if infected cells were sacrificed and it induced detrimental effects on host. Understanding the role of cell death during bacterial infection is important to provide insight into the pathogenesis of unknown infectious diseases. In this review, the different forms of cell death are discussed.
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Figure 1.
Caspase activation pathways during apoptosis. When the CD95 or TNFR1 receptor binds its ligand, this recognition event is translated into intracellular signals that eventually lead to caspase activation. Activated caspase-8 cleaves Bid to tBid. The tBID results in activation of Bax to mediate cytochrome c release from mitochondria. Proapoptotic Bax and Bak induce release of pro-apoptotic proteins such as cytochrome c, Smac/Diablo and Omi/HtrA2. Cytochrome c which is released from mitochondria binds to Apaf-1 to facilitate the formation of apoptosome. The apoptosome can recruit and activate the inactive pro-caspase-9, subsequently induces caspase-3 activation. IAP renders the cell resistant to apoptotic stimuli to neutralize Smac/Diablo and Omi/HtrA2.
Abbreviations: IAP; Inhibitors of apoptosis protein, Apaf-1; Apoptotic protease activating factor 1, Bax; Bcl-2-associated X protein, Bak; Bcl-2 homologous antagonist/killer, Smac; Second mitochondria-derived activator of caspases, DIABLO; Direct IAP-binding protein with low PI, tBID; Truncated BH3 interacting domain death agonist, TNFR1; Tumor necrosis factor receptor-1, FADD; Fas-associated protein with death domain, TRADD; Tumor necrosis factor receptor type 1-associated death domain protein, TRAIL; TNF-related apoptosis-inducing ligand, Omi/HTRA2; Omi stress-regulated endoprotease/high temperature requirement protein A2.
Figure 2.
TNF-α mediated NF-κB activation, apoptosis and necroptosis. RIP1 is ubiquitylated in complex I, and has the ability to activate of IKK complex and NEMO, leading to the activation of NF-κB pathway. The deubiquitination of RIP1 forms complex IIa with FADD, RIP3 and caspase-8. Activated caspase-8 induces apoptosis through caspase cascade. When caspase-8 is blocked, phosphorylated RIP1 and RIP3 form necrosome (complex IIb), after which initiates the necroptosis.
Abbreviations: NEMO; NF-kappa-B essential modulator, RIP1; Receptor-interacting protein 1, cIAP2; Cellular inhibitor of apoptosis-1, TRAF; TNF receptor associated factors, FADD; Fas-associated protein with death domain TRADD; Tumor necrosis factor receptor type 1-associated death domain protein.
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