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Philippe A. Tessier
Researcher at Laval University
Publications - 76
Citations - 5928
Philippe A. Tessier is an academic researcher from Laval University. The author has contributed to research in topics: Proinflammatory cytokine & Inflammation. The author has an hindex of 36, co-authored 74 publications receiving 5079 citations. Previous affiliations of Philippe A. Tessier include University of New South Wales.
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Proinflammatory Activities of S100: Proteins S100A8, S100A9, and S100A8/A9 Induce Neutrophil Chemotaxis and Adhesion
TL;DR: S100A8, S100A9, and S 100A8/A9 are potent stimulators of neutrophils and strongly suggest that these proteins are involved in neutrophil migration to inflammatory sites.
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Innate Lymphoid Cells Promote Anatomical Containment of Lymphoid-Resident Commensal Bacteria
Gregory F. Sonnenberg,Laurel A. Monticelli,Theresa Alenghat,Thomas C. Fung,Natalie A. Hutnick,Jun Kunisawa,Naoko Shibata,Stephanie Grunberg,Rohini Sinha,Adam M. Zahm,Mélanie R. Tardif,Taheri Sathaliyawala,Masaru Kubota,Donna L. Farber,Ronald G. Collman,Abraham Shaked,Lynette A. Fouser,David B. Weiner,Philippe A. Tessier,Joshua R. Friedman,Hiroshi Kiyono,Frederic D. Bushman,Kyong-Mi Chang,Kyong-Mi Chang,David Artis +24 more
TL;DR: It is shown that interleukin-22 (IL-22)–producing innate lymphoid cells (ILCs) are present in intestinal tissues of healthy mammals, indicating that ILCs regulate selective containment of lymphoid-resident bacteria to prevent systemic inflammation associated with chronic diseases.
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S100A8 and S100A9 activate MAP kinase and NF-κB signaling pathways and trigger translocation of RAGE in human prostate cancer cells
TL;DR: The findings show that S 100A8 and S100A9 are linked to the activation of important features of prostate cancer cells and a possible function as extracellular ligands.
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The S100 Family Heterodimer, MRP-8/14, Binds with High Affinity to Heparin and Heparan Sulfate Glycosaminoglycans on Endothelial Cells
TL;DR: It is concluded that the MRp-8/14 complex binds to endothelial cells via the MRP-14 subunit interacting chiefly with heparan sulfate proteoglycans, and this binding activity may explain the immobilization of theMRP-8-14 complex on endothelium that is observed in vivo.
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Blockade of S100A8 and S100A9 suppresses neutrophil migration in response to lipopolysaccharide.
TL;DR: The results suggest that S 100A8 and S100A9 play a role in the inflammatory response to LPS by inducing the release of neutrophils from the bone marrow and directing their migration to the inflammatory site.