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Induction of myeloperoxidase and nitrotyrosine formation in a human eosinophilic leukemia cell line, EoL‐1
Author(s) -
Kodama Norio,
Kambayashi Yasuhiro,
Kubo Masayuki,
Nobukuni Yoshitaka,
Kimura Shingo,
Nakamura Hiroyuki,
Ogino Keiki
Publication year - 2003
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.1051
Subject(s) - eosinophil peroxidase , peroxidase , myeloperoxidase , microbiology and biotechnology , chemistry , cell culture , nitrotyrosine , leukemia , biochemistry , biology , enzyme , immunology , inflammation , nitric oxide synthase , genetics
Abstract The human eosinophilic leukemia cell line, EoL‐1, differentiated with butyrate as an eosinophilic cellular model was evaluated for peroxidase‐dependent tyrosine nitration. Butyrate suppressed cell growth and induced eosinophilic granules in EoL‐1 cells after 9 days of culture. Peroxidase activity was detected biochemically and histochemically from 3‐day cultures and it increased in a time dependent manner. This peroxidase activity was inhibited by cyanide. Nitrotyrosine formation catalysed by peroxidase using hydrogen peroxide and nitrite was detected at a high level similar to that of mature eosinophils. However, no expression of eosinophil peroxidase (EPO) was detected by RT‐PCR or immunocytochemistry. In contrast, the induction of myeloperoxidase (MPO) by butyrate was clearly detected by RT‐PCR, Northern blot, and immunocytochemical staining. These results suggest that butyrate induces MPO rather than EPO in EoL‐1 cells and that the formation of nitrotyrosine in butyrate‐induced cells is dependent on MPO. Copyright © 2003 John Wiley & Sons, Ltd.