| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8713101 | Journal of Allergy and Clinical Immunology | 2018 | 53 Pages |
Abstract
These data demonstrate that Siglec-8 functions uniquely as an activating receptor on IL-5-primed eosinophils through a novel pathway involving regulation of β2-integrin-dependent adhesion, NADPH oxidase, and a subset of protein kinases.
Keywords
ITIMECPPI3KJnkIC50NADPHSiglec-8DAPIp38c-Jun N-terminal kinasec-Jun N-terminal kinase (JNK)ROSβ2-integrinAktEosinophilApoptosisDAVIDSialic acid–binding immunoglobulin-like lectinSiglecInhibitory concentration of 50%phosphatidylinositide 3-kinasePhosphoproteomicsGene ontologydatabase for annotation, visualization and integrated discoveryEosinophil cationic proteinreduced nicotinamide adenine dinucleotide phosphateReactive oxygen species
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Authors
Daniela J. BS, Jeremy A. PhD, David B. PhD, Yun MS, Michael PhD, Bruce S. MD,