Mechanisms involved in human eosinophil chemotaxis induced by the newly cloned C-C chemokine eotaxin.
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概要
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The present study was performed in order to investigate the mechanism(s) involved in eotaxin-induced normal human eosinophil chemotaxis using a 48-well microchemotaxis chamber assay. Eotaxin, at a wide range of doses, induced eosinophil chemotaxis with optimal activity at 100 ng/mL. To elucidate the role of Ca2+ as a second messenger, eosinophils were depleted of intracellular Ca2+ which, per se, did not modify eosinophil chemotaxis. To gain insight of the possible intracellular signal transduction, we blocked pertussis toxin (PTX)-sensitive Gi proteins as well as several protein kinases. It was found that the inhibition of tyrosine kinase with herbimycin A and the inhibition of mitogen-activated protein kinase (MAPK) with MEK-1 inhibitor (PD98059) significantly blocked chemotaxis; however, inhibition of protein kinase C with staurosporine, protein kinase A with H-89 and Gi proteins with PTX did not affect chemotaxis. These results suggest a signal transduction pathway(s) involving Ca2+-independent tyrosine kinase and MAPK activities.
- Japanese Society of Allergologyの論文
Japanese Society of Allergology | 論文
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