Publications
2013
Kobayashi Taira, Ogawa Michinaga, Sanada Takahito, Mimuro Hitomi, Kim Minsoo, Ashida Hiroshi, Akakura Reiko, Yoshida Mitsutaka, Kawalec Magdalena, Reichhart Jean-Marc, Mizushima Tsunehiro, Sasakawa Chihiro
The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection Article de journal
Dans: Cell Host Microbe, vol. 13, no. 5, p. 570–583, 2013, ISSN: 1934-6069.
Résumé | Liens | BibTeX | Étiquettes: Animal, Animals, Bacillary, Bacterial, Bacterial Proteins, Caspases, Cell Death, Cell Line, Disease Models, DNA, Dysentery, Enzyme Inhibitors, Epithelial Cells, Escherichia coli, Gene Knockout Techniques, Guinea Pigs, Host-Pathogen Interactions, Humans, Initiator, M3i, Protein Binding, Protein Interaction Mapping, reichhart, Salmonella typhimurium, Sequence Analysis, Shigella flexneri, Virulence Factors
@article{kobayashi_shigella_2013,
title = {The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection},
author = {Taira Kobayashi and Michinaga Ogawa and Takahito Sanada and Hitomi Mimuro and Minsoo Kim and Hiroshi Ashida and Reiko Akakura and Mitsutaka Yoshida and Magdalena Kawalec and Jean-Marc Reichhart and Tsunehiro Mizushima and Chihiro Sasakawa},
doi = {10.1016/j.chom.2013.04.012},
issn = {1934-6069},
year = {2013},
date = {2013-05-01},
journal = {Cell Host Microbe},
volume = {13},
number = {5},
pages = {570--583},
abstract = {Caspase-mediated inflammatory cell death acts as an intrinsic defense mechanism against infection. Bacterial pathogens deploy countermeasures against inflammatory cell death, but the mechanisms by which they do this remain largely unclear. In a screen for Shigella flexneri effectors that regulate cell death during infection, we discovered that Shigella infection induced acute inflammatory, caspase-4-dependent epithelial cell death, which is counteracted by the bacterial OspC3 effector. OspC3 interacts with the caspase-4-p19 subunit and inhibits its activation by preventing caspase-4-p19 and caspase-4-p10 heterodimerization by depositing the conserved OspC3 X1-Y-X₂-D-X₃ motif at the putative catalytic pocket of caspase-4. Infection of guinea pigs with a Shigella ospC3-deficient mutant resulted in enhanced inflammatory cell death and associated symptoms, correlating with decreased bacterial burdens. Salmonella Typhimurium and enteropathogenic Escherichia coli infection also induced caspase-4-dependent epithelial death. These findings highlight the importance of caspase-4-dependent innate immune responses and demonstrate that Shigella delivers a caspase-4-specific inhibitor to delay epithelial cell death and promote infection.},
keywords = {Animal, Animals, Bacillary, Bacterial, Bacterial Proteins, Caspases, Cell Death, Cell Line, Disease Models, DNA, Dysentery, Enzyme Inhibitors, Epithelial Cells, Escherichia coli, Gene Knockout Techniques, Guinea Pigs, Host-Pathogen Interactions, Humans, Initiator, M3i, Protein Binding, Protein Interaction Mapping, reichhart, Salmonella typhimurium, Sequence Analysis, Shigella flexneri, Virulence Factors},
pubstate = {published},
tppubtype = {article}
}
2011
Ali-Boucetta Hanene, Al-Jamal Khuloud T, Müller Karin H, Li Shouping, Porter Alexandra E, Eddaoudi Ayad, Prato Maurizio, Bianco Alberto, Kostarelos Kostas
Cellular uptake and cytotoxic impact of chemically functionalized and polymer-coated carbon nanotubes Article de journal
Dans: Small (Weinheim an Der Bergstrasse, Germany), vol. 7, no. 22, p. 3230–3238, 2011, ISSN: 1613-6829.
Résumé | Liens | BibTeX | Étiquettes: Annexin A5, carbon, Cell Death, Cell Line, Endocytosis, Flow Cytometry, Fluorescein-5-isothiocyanate, Humans, I2CT, L-Lactate Dehydrogenase, mitochondria, Nanotubes, Polymers, Propidium, Surface Properties, Team-Bianco, tumor, water
@article{ali-boucetta_cellular_2011,
title = {Cellular uptake and cytotoxic impact of chemically functionalized and polymer-coated carbon nanotubes},
author = {Hanene Ali-Boucetta and Khuloud T Al-Jamal and Karin H Müller and Shouping Li and Alexandra E Porter and Ayad Eddaoudi and Maurizio Prato and Alberto Bianco and Kostas Kostarelos},
doi = {10.1002/smll.201101004},
issn = {1613-6829},
year = {2011},
date = {2011-11-01},
journal = {Small (Weinheim an Der Bergstrasse, Germany)},
volume = {7},
number = {22},
pages = {3230--3238},
abstract = {The impact of nanomaterials such as carbon nanotubes on biological matter is a topic of increasing interest and concern and requires a multifaceted approach to be resolved. A modified cytotoxic (lactate dehydrogenase (LDH)) assay is developed in an attempt to offer a valid and reliable methodology for screening carbon nanotube toxicity in vitro. Two of the most widely used types of surface-modified multiwalled carbon nanotubes (MWNTs) are tested: ammonium-functionalized MWNTs (MWNT-NH3+ ) and Pluronic F127 coated MWNTs (MWNT:F127). Chemically functionalized MWNTs show significantly greater cellular uptake into lung epithelial A549 cells compared to the non-covalently Pluronic F127-coated MWNTs. In spite of this, MWNT:F127 exhibit enhanced cytotoxicity according to the modified LDH assay. The validity of the modified LDH assay is further validated by direct comparison with other less reliable or accurate cytotoxicity assays. These findings indicate the reliability of the modified LDH assay as a screening tool to assess carbon nanotube cytotoxicity and illustrate that high levels of carbon nanotube cellular internalization do not necessarily lead to adverse responses.},
keywords = {Annexin A5, carbon, Cell Death, Cell Line, Endocytosis, Flow Cytometry, Fluorescein-5-isothiocyanate, Humans, I2CT, L-Lactate Dehydrogenase, mitochondria, Nanotubes, Polymers, Propidium, Surface Properties, Team-Bianco, tumor, water},
pubstate = {published},
tppubtype = {article}
}
2010
Silverman Gary A, Whisstock James C, Bottomley Stephen P, Huntington James A, Kaiserman Dion, Luke Cliff J, Pak Stephen C, Reichhart Jean-Marc, Bird Phillip I
Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems Article de journal
Dans: J. Biol. Chem., vol. 285, no. 32, p. 24299–24305, 2010, ISSN: 1083-351X.
Résumé | Liens | BibTeX | Étiquettes: Animals, Biological, Caenorhabditis elegans, Cell Death, Cell Differentiation, Cell Survival, Homeostasis, Humans, Immunity, Innate, M3i, Mice, Models, Phenotype, reichhart, Serpins, Transgenes, transgenic
@article{silverman_serpins_2010,
title = {Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems},
author = {Gary A Silverman and James C Whisstock and Stephen P Bottomley and James A Huntington and Dion Kaiserman and Cliff J Luke and Stephen C Pak and Jean-Marc Reichhart and Phillip I Bird},
doi = {10.1074/jbc.R110.112771},
issn = {1083-351X},
year = {2010},
date = {2010-08-01},
journal = {J. Biol. Chem.},
volume = {285},
number = {32},
pages = {24299--24305},
abstract = {Serpins compose the largest superfamily of peptidase inhibitors and are well known as regulators of hemostasis and thrombolysis. Studies using model organisms, from plants to vertebrates, now show that serpins and their unique inhibitory mechanism and conformational flexibility are exploited to control proteolysis in molecular pathways associated with cell survival, development, and host defense. In addition, an increasing number of non-inhibitory serpins are emerging as important elements within a diversity of biological systems by serving as chaperones, hormone transporters, or anti-angiogenic factors.},
keywords = {Animals, Biological, Caenorhabditis elegans, Cell Death, Cell Differentiation, Cell Survival, Homeostasis, Humans, Immunity, Innate, M3i, Mice, Models, Phenotype, reichhart, Serpins, Transgenes, transgenic},
pubstate = {published},
tppubtype = {article}
}