Search

Your search keyword '"Myou, Shigeharu"' showing total 9 results
Start Over Author "Myou, Shigeharu" Publisher american thoracic society
9 results on '"Myou, Shigeharu"'

9. Regulation of interleukin-5-induced beta2-integrin adhesion of human eosinophils by phosphoinositide 3-kinase.

Author

Sano M, Leff AR, Myou S, Boetticher E, Meliton AY, Learoyd J, Lambertino AT, Munoz NM, and Zhu X

Subjects
Androstadienes metabolism, Androstadienes pharmacology, Blotting, Western, Cell Membrane metabolism, Cell Separation, Chromones pharmacology, Cytosol metabolism, Dose-Response Relationship, Drug, Enzyme Activation, Extracellular Signal-Regulated MAP Kinases metabolism, Gene Products, tat genetics, Genes, Dominant, HIV Long Terminal Repeat, Humans, Hypersensitivity, Immediate immunology, Immunoblotting, Immunoprecipitation, Morpholines pharmacology, Phosphorylation, Protein Binding, Protein Isoforms, Protein Kinase C metabolism, Protein Kinase C-delta, Protein Serine-Threonine Kinases metabolism, Protein Structure, Tertiary, Protein Transport, Proto-Oncogene Proteins metabolism, Proto-Oncogene Proteins c-akt, Recombinant Fusion Proteins metabolism, Recombinant Proteins metabolism, Serum Albumin, Bovine metabolism, Signal Transduction, Vascular Cell Adhesion Molecule-1 metabolism, Wortmannin, CD18 Antigens metabolism, Cell Adhesion, Eosinophils metabolism, Interleukin-5 metabolism, Phosphatidylinositol 3-Kinases metabolism
Abstract

We examined the role of phosphoinositide 3-kinase (PI3K) in integrin-mediated eosinophil adhesion. Deltap85, a dominant-negative form of the class IA PI3K adaptor subunit, was fused to an HIV-TAT protein transduction domain (TAT-Deltap85). Recombinant TAT-Deltap85 inhibited interleukin (IL)-5-stimulated phosphorylation of protein kinase B, a downstream target of PI3K. beta(2)-Integrin-dependent adhesion caused by IL-5 to the plated intracellular adhesion molecule-1 surrogate, bovine serum albumin, was inhibited by TAT-Deltap85 in a concentration-dependent manner. Similarly, two PI3K inhibitors, wortmannin and LY294002, blocked eosinophil adhesion to plated bovine serum albumin. By contrast, beta(1)-integrin-mediated eosinophil adhesion to vascular cell adhesion moelcule-1 was not blocked by TAT-Deltap85, wortmannin, or LY294002. Rottlerin, a protein kinase C (PKC)-delta inhibitor, also blocked beta(2)-integrin adhesion of eosinophils caused by IL-5, whereas beta(1) adhesion to vascular cell adhesion molecule-1 was not affected. IL-5 caused translocation of PKCdelta from the cytosol to cell membrane; inhibition of PI3K by wortmannin blocked translocation of PKCdelta. Western blot analysis demonstrated that extracellular signal-regulated kinase phosphorylation, a critical intermediary in adhesion elicited by IL-5, was blocked by inhibition of either PI3K or PKC-delta. These data suggest that extracellular signal-regulated kinase-mediated adhesion of beta(2)-integrin caused by IL-5 is mediated in human eosinophils by a class IA PI3K through activation of a PKCdelta pathway.

Published
2005
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results