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J. Biochem, 1990, Vol. 108, No. 2 169-174
© 1990 Japanese Biochemical Society

research-article

Translocation of the 46 kDa Protein(s) in Response to Activation of NADPH Oxidase in Guinea Pig Polymorphonuclear Leukocytes1

Toshiaki Ohtsuka, Mayumi Nakamura, Masanori Hiura, Klyomi Yoshida, Naoki Okamura2 and Sadahiko Ishibashi

Department of Physiological Chemistry, Hiroshima University School of Medicine Minami-ku, Hiroshima 734

2To whom correspondence should be addressed

Treatment of guinea pig polymorphonuclear leukocytes (PMNL) with phorbol 12-myristate 13-acetate (PMA) induced an increase in phosphorylatlon of 46 kDa protein(s) in parallel with activation of NADPH oxidase. In response to PMA stimulation, phosphorylated 46 kDa protein(s) increased markedly in the membrane fraction, accompanied by a decrease in the unphosphorylated form(s) in the cytosol. The results indicate that the 46 kDa protein(s) may be translocated concomitantly with its phosphorylation. On the other hand, in a cell-free activation system reconstituted from the cytosol and plasma membranes of unstimulated PM1NL, arachidonic acid caused the translocation of the 46 kDa protein(s) from the cytosol to the plasma membranes concomitantly with an enhancement of NADPH oxidase activity. These results suggest that activation of NAI)PH oxidase is dependent on an association of 46 kDa protein(s) with the membranes both in intact PMINL and In the cell-free system.

1This work was supported by a Grant-in-Aid for Co-operative Research from the Ministry of Education, Science and Culture of Japan.


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Simultaneous Presence of p47phox and Flavocytochrome b-245 Are Required for the Activation of NADPH Oxidase by Anionic Amphiphiles. EVIDENCE FOR AN INTERMEDIATE STATE OF OXIDASE ACTIVATION
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