Possible Involvement of Optimally Phosphorylated L-Plastin in Activation of Superoxide-Generating NADPH Oxidase
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- Oshizawa Tadashi
- Division of Cellular and Gene Therapy Products
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- Yamaguchi Teruhide
- Division of Cellular and Gene Therapy Products
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- Suzuki Kazuhiro
- Division of Biosignaling, National Institute of Health Sciences
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- Yamamoto Yukio
- Department of Medical Biology, The Tokyo Metropolitan Institute of Medical Science
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- Hayakawa Takao
- National Institute of Health Sciences
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The involvement of protein phosphatases in the activation of superoxide (O2-)- generating enzyme in human neutrophils was examined using calyculin A, an inhibitor of protein phosphatase type 1 and 2 A. Calyculin A inhibited the phorbol myristate acetate (PMA)- and opsonized zymosan (OZ)-activated O2- generation by human neutrophils. This inhibitory effect of calyculin A on PMA-activated O2- generation was reversed by the addition of KT5926, a specific inhibitor of myosin light chain kinase and Ca2+/calmodulin-dependent protein kinase II. These results suggest that the addition of calyculin A may cause hyperphosphorylation of some protein(s) that plays a crucial role in the PMA-dependent activation of O2- generating enzyme, and that this protein hyperphosphorylation may be evoked by a KT5926-sensitive kinase or its downstream kinase. Whereas two-dimensional analysis involving 32P revealed that calyculin A caused the hyperphosphorylation of many proteins, KT5926 mainly reduced the calyculin A-induced hyperphosphorylation of a 67 kDa protein in activated neutrophils, suggesting that the hyperphosphorylation of the 67 kDa protein might inhibit the PMA-dependent activation of NADPH oxidase. The 67 kDa cytosolic protein was moderately phosphorylated on the addition of PMA. On the other hand, in the absence of calyculin A, KT5926 inhibited both PMA-induced O2- generation and phosphorylation of the 67 kDa protein. Amino acid sequence analysis of peptides derived from the 67 kDa protein revealed that the 67 kDa protein was identical to L-plastin, an actin-bundling protein. We conclude that optimally phosphorylated L-plastin may play some crucial role in the activation of NADPH oxidase.
収録刊行物
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- The Journal of Biochemistry
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The Journal of Biochemistry 134 (6), 827-834, 2003
社団法人 日本生化学会
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詳細情報 詳細情報について
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- CRID
- 1390282679941545216
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- NII論文ID
- 130003534634
- 50000393691
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- NII書誌ID
- AA00694073
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- COI
- 1:CAS:528:DC%2BD2cXis1Kksrc%3D
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- ISSN
- 17562651
- 0021924X
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- NDL書誌ID
- 6830734
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- PubMed
- 14769871
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可