Pathogen-Associated Molecular Patterns Sensitize Macrophages to Fas Ligand-Induced Apoptosis and IL-1β Release

Fukui, Masayuki; Imamura, Ryu; Umemura, Masayuki; Kawabe, Takahiro; Suda, Takafumi

doi:10.4049/jimmunol.171.4.1868

Cited by 49 publications

(44 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In some experiments, the proportion of necrosis was assessed by the release of cytoplasmic lactate dehydrogenase into culture supernatants using the CytoTox 96 kit (Promega), according to the manufacturer's protocol. In some experiments, cell death was assessed by WST1 assay, as described previously (24).…”

Section: Methodsmentioning

confidence: 99%

Caspase-1 Protein Induces Apoptosis-associated Speck-like Protein Containing a Caspase Recruitment Domain (ASC)-mediated Necrosis Independently of Its Catalytic Activity

Motani

Kushiyama

Imamura

et al. 2011

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background: ASC mediates apoptosis and necrosis of tumor cells and necrosis of microbe-infected macrophages. Results: ASC mediates necrosis only when cells express caspase-1; however, inhibition of caspase-1 proteolytic activity did not suppress the necrosis. Conclusion: Caspase-1 but not its proteolytic activity is essential for ASC-mediated necrosis. Significance: This study explains why ASC induces apoptosis or necrosis depending on the cell type.

show abstract

Section: Methodsmentioning

confidence: 99%

Caspase-1 Protein Induces Apoptosis-associated Speck-like Protein Containing a Caspase Recruitment Domain (ASC)-mediated Necrosis Independently of Its Catalytic Activity

Motani

Kushiyama

Imamura

et al. 2011

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…Total RNA from cultured cell lines was prepared using the RNeasy mini kit (Qiagen, Hilden, Germany). RT-PCR analysis was performed as described previously (13). The primers used to detect human PYPAF2 mRNA were as follows: sense, 5Ј-gcaaaggatgaagtcagaga-3Ј; antisense, 5Ј-ccctccacccttatgtagat-3Ј, while those for PYPAF3 mRNA were as follows: sense, 5Ј-gcagtgggctgaattcttct-3Ј; antisense, 5Ј-gcctgacagagaatccacaa-3Ј.…”

Section: Methodsmentioning

confidence: 99%

PYPAF3, a PYRIN-containing APAF-1-like Protein, Is a Feedback Regulator of Caspase-1-dependent Interleukin-1β Secretion

Kinoshita

Wang

Hasegawa

et al. 2005

Journal of Biological Chemistry

Self Cite

132

109

View full text Add to dashboard Cite

PYPAF3 is a member of the PYRIN-containing apoptotic protease-activating factor-1-like proteins (PYPAFs, also called NALPs). Among the members of this family, PYPAF1, PYPAF5, PYPAF7, and NALP1 have been shown to induce caspase-1-dependent interleukin-1␤ secretion and NF-B activation in the presence of the adaptor molecule ASC. On the other hand, we recently discovered that PYNOD, another member of this family, is a suppressor of these responses. Here, we show that PYPAF3 is the second member that inhibits caspase-1-dependent interleukin-1␤ secretion. In contrast, PYPAF2/NALP2 does not inhibit this response but rather inhibits the NF-B activation that is induced by the combined expression of PYPAF1 and ASC. Both PYPAF2 and PYPAF3 mRNAs are broadly expressed in a variety of tissues; however, neither is expressed in skeletal muscle, and only PYPAF2 mRNA is expressed in heart and brain. They are also expressed in many cell lines of both hematopoietic and non-hematopoietic lineages. Stimulation of monocytic THP-1 cells with lipopolysaccharide or interleukin-1␤ induced PYPAF3 mRNA expression. Furthermore, the stable expression of PYPAF3 in THP-1 cells abrogated the ability of the cells to produce interleukin-1␤ in response to lipopolysaccharide. These results suggest that PYPAF3 is a feedback regulator of interleukin-1␤ secretion. Thus, PYPAF2 and PYPAF3, together with PYNOD, constitute an anti-inflammatory subgroup of PYPAFs.

show abstract

“…RT-PCR analysis was performed as described previously (24). The following primers were used: p19 sense, 5Ј-gggaacaagatgctggattg-3Ј; p19 antisense, 5Ј-atggtagccatgggaacctg-3Ј; p40 sense, 5Ј-tgttgtagaggtggactggac-3Ј; p40 antisense, 5Ј-ccttcttgtggagcagcaga-3Ј; p35 sense, 5Ј-gccacccttgccctcctaaa-3Ј; and p35 antisense, 5Ј-caccagcatgcccttgtcta-3Ј.…”

Section: Rt-pcr Analysis For Il-23 P19 Mrnamentioning

confidence: 99%

Fas Ligand Induces Cell-Autonomous IL-23 Production in Dendritic Cells, a Mechanism for Fas Ligand-Induced IL-17 Production

Kidoya

Umemura

Kawabe

et al. 2005

The Journal of Immunology

Self Cite

View full text Add to dashboard Cite

Fas ligand (FasL) has the potential to induce inflammation accompanied by massive neutrophil infiltration. We previously reported that FasL rapidly induces the production of various inflammatory cytokines including IL-1β and IL-17. In this study, we investigated the mechanism of the FasL-induced IL-17 production. We found that the culture supernatant of mouse resident peritoneal exudate cells (PEC) cocultured with FasL-expressing tumor (FFL) cells induced IL-17 production in freshly isolated resident PEC. Anti-IL-1β Ab strongly inhibited the IL-17-inducing activity. However, rIL-1β by itself induced only weak IL-17 production. Intriguingly, anti-IL-12 Ab but not an IL-15-neutralizing agent, IL15R-Fc, strongly inhibited the FasL-induced IL-17-inducing activity. IL-23, which shares the p40 subunit with IL-12, but not IL-12 itself, induced IL-17 production synergistically with IL-1β in resident PEC. FasL induced the production of IL-23 in PEC in vivo and in vitro, and IL-17 production following the i.p. injection of FFL cells was severely impaired in p40−/− mice, indicating that IL-23 plays an important role in the FasL-induced IL-17 production. FFL also induced the production of IL-23 in bone marrow- or PEC-derived dendritic cells (DCs). Finally, FasL induced only weak p40 production in a mixture of p40−/− and Fas−/− DC, indicating that FasL induces IL-23 production in DC mainly in a cell-autonomous manner.

show abstract

Pathogen-Associated Molecular Patterns Sensitize Macrophages to Fas Ligand-Induced Apoptosis and IL-1β Release

Cited by 49 publications

References 51 publications

Caspase-1 Protein Induces Apoptosis-associated Speck-like Protein Containing a Caspase Recruitment Domain (ASC)-mediated Necrosis Independently of Its Catalytic Activity

Caspase-1 Protein Induces Apoptosis-associated Speck-like Protein Containing a Caspase Recruitment Domain (ASC)-mediated Necrosis Independently of Its Catalytic Activity

PYPAF3, a PYRIN-containing APAF-1-like Protein, Is a Feedback Regulator of Caspase-1-dependent Interleukin-1β Secretion

Fas Ligand Induces Cell-Autonomous IL-23 Production in Dendritic Cells, a Mechanism for Fas Ligand-Induced IL-17 Production

Contact Info

Product

Resources

About