Shigella-induced Apoptosis Is Dependent on Caspase-1 Which Binds to IpaB

Hilbi, Hubert; Moss, Jeremy E.; Hersh, David; Chen, Yajing; Arondel, Josette; Banerjee, Subhashis; Flavell, Richard A.; Yuan, Junying; Sansonetti, Philippe J.; Zychlinsky, Arturo

doi:10.1074/jbc.273.49.32895

Cited by 386 publications

(313 citation statements)

References 47 publications

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“…However, the activation of caspase-1 does not appear to be the only mechanism required for the chlamydia-induced secretion of IL-18 because similarly infected fibroblast cells did not secrete detectable levels of IL-18 despite the activation of caspase-1. Other studies have suggested that the Shigella invasion plasmid Ag B and Salmonella invasion protein B directly bind to caspase-1 and trigger hydrolysis of this cysteine protease into its bioactive forms, which then cleave pro-IL-1␤ and trigger host cell apoptosis (33,34). Although little is known about the subcellular sites and detailed mechanisms responsible for activation of caspase-1 (35-37), we observed that TPCK and lactacystin, two structurally different but specific inhibitors of proteasomes, significantly inhibited IL-18 production induced by chlamydia infection.…”

Section: Discussionmentioning

confidence: 99%

Chlamydia trachomatis Infection of Epithelial Cells Induces the Activation of Caspase-1 and Release of Mature IL-18

Shen

Brunham

2000

The Journal of Immunology

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Th1 cells that secrete IFN-γ are particularly important in protective immunity against intracellular pathogens, including chlamydiae, and IL-18 together with IL-12 are strong inducers of IFN-γ secretion by CD4 T cells. Because epithelial cells are known to synthesize IL-18, we investigated the effects of Chlamydia trachomatis infection of human epithelial cell lines on IL-18 secretion. We confirmed that several human epithelial cell lines constitutively express pro-IL-18 and that C. trachomatis infection causes cells to secrete mature IL-18. This was observed for several different serovars and biovars of C. trachomatis. Chlamydia-induced secretion of IL-18 from epithelial cells was regulated at the posttranscriptional level and was dependent on the activation of caspase-1. IL-1α or other secreted factor(s) from chlamydia-infected epithelial cells as well as chlamydial structural component(s) were not involved in inducing IL-18 secretion. Activation of caspase-1 and increased secretion of mature IL-18 was correlated with chlamydial, but not with host protein synthesis. In contrast to epithelial cell lines, fibroblast cell lines constitutively expressed much lower levels of pro-IL-18 and did not secrete mature IL-18 after chlamydial infection even though caspase-1 was activated. Taken together, the results suggest that a chlamydia-derived factor(s) is essential for the secretion of mature IL-18 through caspase-1 activation in infected epithelial cells.

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Section: Discussionmentioning

confidence: 99%

Chlamydia trachomatis Infection of Epithelial Cells Induces the Activation of Caspase-1 and Release of Mature IL-18

Shen

Brunham

2000

The Journal of Immunology

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“…Activation of caspase-1 has mostly been implicated in inflammatory responses; however, its implication in apoptotic processes has also been documented (Hilbi et al, 1998;Liu and Abrams, 2003). In Fas-induced apoptosis, the activation of the primarily inflammation associated caspase-1 and -4 provides an amplification loop to enhance apoptosis, a function that has often been implicated in pathways involving caspase-1 activation.…”

Section: Activation and Processing Of Ceacam1 During Apoptosis S Nittmentioning

confidence: 99%

The CEACAM1-mediated apoptosis pathway is activated by CEA and triggers dual cleavage of CEACAM1

et al. 2008

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Marked reduction in apoptosis is a hallmark of early colon tumour growth and the vast majority of these tumours exhibit a loss of expression of the glycoprotein carcinoembryonic-antigen-related cell adhesion molecule 1 (CEACAM1). We recently reported that the CEACAM1 functions as a mediator of apoptosis implicating this cell surface protein in early tumour development. However, the mechanistic involvement of CEACAM1 in cell death pathways is unclear. Here, we show that apoptosis triggers cleavage of the long form of CEACAM1 (CEACAM1-4L) at intracellular and extracellular sites in Jurkat cells and HEK293 cells. Signalling through CEACAM1 leads to caspase activation including caspase-1 and -3 and also involves non-caspase proteases. Moreover, we provide evidence that the naturally occurring CEACAM family member CEA is an inducer of CEACAM1-mediated apoptosis in HT29 colon cancer cells, an effect that depends on the abundance of CEACAM1 on the cell surface. Together, our results demonstrate that the CEACAM1-dependent cell death pathway involves dual cleavage of CEACAM1 and caspase activation and can be activated by CEA.

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“…However, some virulent bacteria are able to evade killing by macrophages and actually induce macrophage death. It is known that the mechanism of macrophage death induced by different pathogens varies [11][12][13][14]. Bacterial endotoxin (lipopolysaccharide; LPS) is a complex glycolipid found in the outer membrane of all gram-negative bacteria, and is believed to play a crucial role in induced cellular responses to gram-negative bacteria.…”

Section: Introductionmentioning

confidence: 99%

MEF2C mediates the activation induced cell death (AICD) of macrophages

Wei

2006

Cell Res

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Activation-induced cell death (AICD) of immune cells is widely believed to be crucial for the regulation of immune responses. Although macrophage apoptosis has been observed under a variety of pathological conditions, questions as to whether there is AICD of macrophages and how macrophage life span is regulated have not been well addressed. AICD in macrophages requires two signals. One is cell activation triggered by LPS or other bacterial components. The other is an event that exists in AICD-susceptible (primed) but not unsusceptible (resting) macrophages. Here we show that RAW264.7 cell is susceptible to LPS stimulation when it is primed with Salmonella typhimurium, type 5 adenovirus (Ad5) or IFN-g. We found that the stability of the transcription factor MEF2C is increased in primed RAW264.7 cell. Transfection of a dominant negative form of MEF2C protects primed macrophage from cell death triggered by LPS. Our data demonstrate that the increase of MEF2C protein stability is a key factor in the AICD of macrophage.

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Shigella-induced Apoptosis Is Dependent on Caspase-1 Which Binds to IpaB

Cited by 386 publications

References 47 publications

Chlamydia trachomatis Infection of Epithelial Cells Induces the Activation of Caspase-1 and Release of Mature IL-18

Chlamydia trachomatis Infection of Epithelial Cells Induces the Activation of Caspase-1 and Release of Mature IL-18

The CEACAM1-mediated apoptosis pathway is activated by CEA and triggers dual cleavage of CEACAM1

MEF2C mediates the activation induced cell death (AICD) of macrophages

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