Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils

Honda, K. ; Chihara, J.

Copenhagen : Munksgaard International Publishers
Published 1999
ISSN:
1398-9995
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Background: The CC chemokine eotaxin has been shown to possess selective chemotactic activity for eosinophils, the major effector cells in allergic inflammation. Reactive oxygen species (ROS) from eosinophils may damage cells or tissue, such as the mucosal epithelium. In this study, we examined the effect of eotaxin on ROS from eosinophils and compared its activity with RANTES and interleukin (IL)-5. Moreover, we examined the signal transduction of eotaxin and the effect of dexamethasone on ROS from eosinophils. Methods: Eosinophils were isolated by modified CD16-negative selection. ROS in luminol-dependent or lucigenin-dependent chemiluminescence reaction were examined. Calcium ionophore A23187 was added to the mixture of eosinophils with luminol or lucigenin, and then ROS were determined. Results: Eotaxin primed the production of ROS in a dose-dependent manner. ROS from untreated eosinophils evoked with calcium ionophore A23187 in luminol-dependent chemiluminescence gave a maximal value of 4957±1035 intensity counts (IC) (mean±SE, n=7) and an integral value of 15.75±3.14 IC (×10−4), while eosinophils that were treated with eotaxin gave maximal values of 11 142±2300 IC (10 nM) and 29 165±3718 IC (100 nM) and integral values of 41.07±5.44 IC (×10−4) (10 nM) and 152.90±22.38 IC (×10−4) (100 nM). Moreover, eotaxin was less effective as a priming agent with lucigenin-sensitive pathways than luminol-sensitive pathways. Among several kinds of eosinophils activating cytokines and chemokines, the priming effect of eotaxin on ROS was the most potent. Eotaxin-primed ROS were inhibited by pertussis toxin, which ADP-ribolysates G proteins; wortmannin, a phosphatidylinositol-3-kinase inhibitor; and genistein, a tyrosine kinase inhibitor, suggesting the involvement of pertussis toxin-sensitive G proteins, phosphatidylinositol-3-kinase, and tyrosine kinase in the signal transduction of eotaxin. Moreover, dexamethasone inhibited ROS from not only untreated eosinophils but also eosinophils treated with eotaxin. Conclusions: Eotaxin may play an important role in the pathogenesis of allergic inflammation through eosinophil activation by priming of eosinophil oxidative metabolism, as well as by involvement in selective eosinophil chemotaxis.
Type of Medium:
Electronic Resource
URL:
_version_ 1798290256138600448
autor Honda, K.
Chihara, J.
book_url http://dx.doi.org/10.1034/j.1398-9995.1999.00170.x
datenlieferant nat_lic_papers
hauptsatz hsatz_simple
identnr NLZ242308333
insertion_date 2012-04-27
iqvoc_descriptor_title iqvoc_00000080:production
issn 1398-9995
journal_name Allergy
materialart 1
notes Background: The CC chemokine eotaxin has been shown to possess selective chemotactic activity for eosinophils, the major effector cells in allergic inflammation. Reactive oxygen species (ROS) from eosinophils may damage cells or tissue, such as the mucosal epithelium. In this study, we examined the effect of eotaxin on ROS from eosinophils and compared its activity with RANTES and interleukin (IL)-5. Moreover, we examined the signal transduction of eotaxin and the effect of dexamethasone on ROS from eosinophils. Methods: Eosinophils were isolated by modified CD16-negative selection. ROS in luminol-dependent or lucigenin-dependent chemiluminescence reaction were examined. Calcium ionophore A23187 was added to the mixture of eosinophils with luminol or lucigenin, and then ROS were determined. Results: Eotaxin primed the production of ROS in a dose-dependent manner. ROS from untreated eosinophils evoked with calcium ionophore A23187 in luminol-dependent chemiluminescence gave a maximal value of 4957±1035 intensity counts (IC) (mean±SE, n=7) and an integral value of 15.75±3.14 IC (×10−4), while eosinophils that were treated with eotaxin gave maximal values of 11 142±2300 IC (10 nM) and 29 165±3718 IC (100 nM) and integral values of 41.07±5.44 IC (×10−4) (10 nM) and 152.90±22.38 IC (×10−4) (100 nM). Moreover, eotaxin was less effective as a priming agent with lucigenin-sensitive pathways than luminol-sensitive pathways. Among several kinds of eosinophils activating cytokines and chemokines, the priming effect of eotaxin on ROS was the most potent. Eotaxin-primed ROS were inhibited by pertussis toxin, which ADP-ribolysates G proteins; wortmannin, a phosphatidylinositol-3-kinase inhibitor; and genistein, a tyrosine kinase inhibitor, suggesting the involvement of pertussis toxin-sensitive G proteins, phosphatidylinositol-3-kinase, and tyrosine kinase in the signal transduction of eotaxin. Moreover, dexamethasone inhibited ROS from not only untreated eosinophils but also eosinophils treated with eotaxin. Conclusions: Eotaxin may play an important role in the pathogenesis of allergic inflammation through eosinophil activation by priming of eosinophil oxidative metabolism, as well as by involvement in selective eosinophil chemotaxis.
package_name Blackwell Publishing
publikationsjahr_anzeige 1999
publikationsjahr_facette 1999
publikationsjahr_intervall 8004:1995-1999
publikationsjahr_sort 1999
publikationsort Copenhagen
publisher Munksgaard International Publishers
reference 54 (1999), S. 0
search_space articles
shingle_author_1 Honda, K.
Chihara, J.
shingle_author_2 Honda, K.
Chihara, J.
shingle_author_3 Honda, K.
Chihara, J.
shingle_author_4 Honda, K.
Chihara, J.
shingle_catch_all_1 Honda, K.
Chihara, J.
Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
Munksgaard International Publishers
Background: The CC chemokine eotaxin has been shown to possess selective chemotactic activity for eosinophils, the major effector cells in allergic inflammation. Reactive oxygen species (ROS) from eosinophils may damage cells or tissue, such as the mucosal epithelium. In this study, we examined the effect of eotaxin on ROS from eosinophils and compared its activity with RANTES and interleukin (IL)-5. Moreover, we examined the signal transduction of eotaxin and the effect of dexamethasone on ROS from eosinophils. Methods: Eosinophils were isolated by modified CD16-negative selection. ROS in luminol-dependent or lucigenin-dependent chemiluminescence reaction were examined. Calcium ionophore A23187 was added to the mixture of eosinophils with luminol or lucigenin, and then ROS were determined. Results: Eotaxin primed the production of ROS in a dose-dependent manner. ROS from untreated eosinophils evoked with calcium ionophore A23187 in luminol-dependent chemiluminescence gave a maximal value of 4957±1035 intensity counts (IC) (mean±SE, n=7) and an integral value of 15.75±3.14 IC (×10−4), while eosinophils that were treated with eotaxin gave maximal values of 11 142±2300 IC (10 nM) and 29 165±3718 IC (100 nM) and integral values of 41.07±5.44 IC (×10−4) (10 nM) and 152.90±22.38 IC (×10−4) (100 nM). Moreover, eotaxin was less effective as a priming agent with lucigenin-sensitive pathways than luminol-sensitive pathways. Among several kinds of eosinophils activating cytokines and chemokines, the priming effect of eotaxin on ROS was the most potent. Eotaxin-primed ROS were inhibited by pertussis toxin, which ADP-ribolysates G proteins; wortmannin, a phosphatidylinositol-3-kinase inhibitor; and genistein, a tyrosine kinase inhibitor, suggesting the involvement of pertussis toxin-sensitive G proteins, phosphatidylinositol-3-kinase, and tyrosine kinase in the signal transduction of eotaxin. Moreover, dexamethasone inhibited ROS from not only untreated eosinophils but also eosinophils treated with eotaxin. Conclusions: Eotaxin may play an important role in the pathogenesis of allergic inflammation through eosinophil activation by priming of eosinophil oxidative metabolism, as well as by involvement in selective eosinophil chemotaxis.
1398-9995
13989995
shingle_catch_all_2 Honda, K.
Chihara, J.
Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
Munksgaard International Publishers
Background: The CC chemokine eotaxin has been shown to possess selective chemotactic activity for eosinophils, the major effector cells in allergic inflammation. Reactive oxygen species (ROS) from eosinophils may damage cells or tissue, such as the mucosal epithelium. In this study, we examined the effect of eotaxin on ROS from eosinophils and compared its activity with RANTES and interleukin (IL)-5. Moreover, we examined the signal transduction of eotaxin and the effect of dexamethasone on ROS from eosinophils. Methods: Eosinophils were isolated by modified CD16-negative selection. ROS in luminol-dependent or lucigenin-dependent chemiluminescence reaction were examined. Calcium ionophore A23187 was added to the mixture of eosinophils with luminol or lucigenin, and then ROS were determined. Results: Eotaxin primed the production of ROS in a dose-dependent manner. ROS from untreated eosinophils evoked with calcium ionophore A23187 in luminol-dependent chemiluminescence gave a maximal value of 4957±1035 intensity counts (IC) (mean±SE, n=7) and an integral value of 15.75±3.14 IC (×10−4), while eosinophils that were treated with eotaxin gave maximal values of 11 142±2300 IC (10 nM) and 29 165±3718 IC (100 nM) and integral values of 41.07±5.44 IC (×10−4) (10 nM) and 152.90±22.38 IC (×10−4) (100 nM). Moreover, eotaxin was less effective as a priming agent with lucigenin-sensitive pathways than luminol-sensitive pathways. Among several kinds of eosinophils activating cytokines and chemokines, the priming effect of eotaxin on ROS was the most potent. Eotaxin-primed ROS were inhibited by pertussis toxin, which ADP-ribolysates G proteins; wortmannin, a phosphatidylinositol-3-kinase inhibitor; and genistein, a tyrosine kinase inhibitor, suggesting the involvement of pertussis toxin-sensitive G proteins, phosphatidylinositol-3-kinase, and tyrosine kinase in the signal transduction of eotaxin. Moreover, dexamethasone inhibited ROS from not only untreated eosinophils but also eosinophils treated with eotaxin. Conclusions: Eotaxin may play an important role in the pathogenesis of allergic inflammation through eosinophil activation by priming of eosinophil oxidative metabolism, as well as by involvement in selective eosinophil chemotaxis.
1398-9995
13989995
shingle_catch_all_3 Honda, K.
Chihara, J.
Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
Munksgaard International Publishers
Background: The CC chemokine eotaxin has been shown to possess selective chemotactic activity for eosinophils, the major effector cells in allergic inflammation. Reactive oxygen species (ROS) from eosinophils may damage cells or tissue, such as the mucosal epithelium. In this study, we examined the effect of eotaxin on ROS from eosinophils and compared its activity with RANTES and interleukin (IL)-5. Moreover, we examined the signal transduction of eotaxin and the effect of dexamethasone on ROS from eosinophils. Methods: Eosinophils were isolated by modified CD16-negative selection. ROS in luminol-dependent or lucigenin-dependent chemiluminescence reaction were examined. Calcium ionophore A23187 was added to the mixture of eosinophils with luminol or lucigenin, and then ROS were determined. Results: Eotaxin primed the production of ROS in a dose-dependent manner. ROS from untreated eosinophils evoked with calcium ionophore A23187 in luminol-dependent chemiluminescence gave a maximal value of 4957±1035 intensity counts (IC) (mean±SE, n=7) and an integral value of 15.75±3.14 IC (×10−4), while eosinophils that were treated with eotaxin gave maximal values of 11 142±2300 IC (10 nM) and 29 165±3718 IC (100 nM) and integral values of 41.07±5.44 IC (×10−4) (10 nM) and 152.90±22.38 IC (×10−4) (100 nM). Moreover, eotaxin was less effective as a priming agent with lucigenin-sensitive pathways than luminol-sensitive pathways. Among several kinds of eosinophils activating cytokines and chemokines, the priming effect of eotaxin on ROS was the most potent. Eotaxin-primed ROS were inhibited by pertussis toxin, which ADP-ribolysates G proteins; wortmannin, a phosphatidylinositol-3-kinase inhibitor; and genistein, a tyrosine kinase inhibitor, suggesting the involvement of pertussis toxin-sensitive G proteins, phosphatidylinositol-3-kinase, and tyrosine kinase in the signal transduction of eotaxin. Moreover, dexamethasone inhibited ROS from not only untreated eosinophils but also eosinophils treated with eotaxin. Conclusions: Eotaxin may play an important role in the pathogenesis of allergic inflammation through eosinophil activation by priming of eosinophil oxidative metabolism, as well as by involvement in selective eosinophil chemotaxis.
1398-9995
13989995
shingle_catch_all_4 Honda, K.
Chihara, J.
Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
Munksgaard International Publishers
Background: The CC chemokine eotaxin has been shown to possess selective chemotactic activity for eosinophils, the major effector cells in allergic inflammation. Reactive oxygen species (ROS) from eosinophils may damage cells or tissue, such as the mucosal epithelium. In this study, we examined the effect of eotaxin on ROS from eosinophils and compared its activity with RANTES and interleukin (IL)-5. Moreover, we examined the signal transduction of eotaxin and the effect of dexamethasone on ROS from eosinophils. Methods: Eosinophils were isolated by modified CD16-negative selection. ROS in luminol-dependent or lucigenin-dependent chemiluminescence reaction were examined. Calcium ionophore A23187 was added to the mixture of eosinophils with luminol or lucigenin, and then ROS were determined. Results: Eotaxin primed the production of ROS in a dose-dependent manner. ROS from untreated eosinophils evoked with calcium ionophore A23187 in luminol-dependent chemiluminescence gave a maximal value of 4957±1035 intensity counts (IC) (mean±SE, n=7) and an integral value of 15.75±3.14 IC (×10−4), while eosinophils that were treated with eotaxin gave maximal values of 11 142±2300 IC (10 nM) and 29 165±3718 IC (100 nM) and integral values of 41.07±5.44 IC (×10−4) (10 nM) and 152.90±22.38 IC (×10−4) (100 nM). Moreover, eotaxin was less effective as a priming agent with lucigenin-sensitive pathways than luminol-sensitive pathways. Among several kinds of eosinophils activating cytokines and chemokines, the priming effect of eotaxin on ROS was the most potent. Eotaxin-primed ROS were inhibited by pertussis toxin, which ADP-ribolysates G proteins; wortmannin, a phosphatidylinositol-3-kinase inhibitor; and genistein, a tyrosine kinase inhibitor, suggesting the involvement of pertussis toxin-sensitive G proteins, phosphatidylinositol-3-kinase, and tyrosine kinase in the signal transduction of eotaxin. Moreover, dexamethasone inhibited ROS from not only untreated eosinophils but also eosinophils treated with eotaxin. Conclusions: Eotaxin may play an important role in the pathogenesis of allergic inflammation through eosinophil activation by priming of eosinophil oxidative metabolism, as well as by involvement in selective eosinophil chemotaxis.
1398-9995
13989995
shingle_title_1 Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
shingle_title_2 Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
shingle_title_3 Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
shingle_title_4 Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
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source_archive Blackwell Publishing Journal Backfiles 1879-2005
timestamp 2024-05-06T08:13:50.134Z
titel Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
titel_suche Eosinophil activation by eotaxin – eotaxin primes the production of reactive oxygen species from eosinophils
topic WW-YZ
uid nat_lic_papers_NLZ242308333