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J. Biochem, 1987, Vol. 101, No. 4 897-903
© 1987 Japanese Biochemical Society

other

Significance of Phosphorylation/Dephosphorylation of 46K Protein(s)in Regulation of Superoxide Anion Production in Intact Guinea Pig Polymorphonuclear Leukocytes1

Toshiaki OHTSUKA, Masaki OZAWA, Tadao OKAMOTO, Motoyuki UCHIDA, Naoki OKAMURA and Sadahiko ISHIBASHI

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

Superoxide anion (O2–) production stimulated by concanavalin A (Con A) in guinea pig polymorphonuclear leukocytes (PMNL) was suppressed by addition of methyl-{alpha}-mannoside, a Con A inhibitor, and resumed upon readdition of Con A. The reversible change in the O2– production was assumed to reflect the change in NADPH oxidase activity measured for the 30,000 × g particulate fraction. The stimulation by Con A of the phosphorylation of 46K protein(s), as observed previously with several membrane-perturbing agents in parallel with an activation of NADPH oxidase in intact guinea pig PMNL (Okamura, N., et al. (1984) Arch. Biochem. Biophys. 228, 270–277), was also suppressed by methyl-{alpha}-mannoside and resumed upon readdition of Con A. Similar parallelism between the phosphorylation and NADPH oxidase activity was also observed in the case of stimulation by N-formyl-methionyl-leucyl-phenylalanine (FMLP) and phorbol 12-myristate 13-acetate (PMA), though both processes were reversible after the stimulation by FMLP but not reversible after that by PMA. Thus, such a parallelism observed in both intact PMNL and 30,000 × g particulate fraction indicates possible involvement of the protein phosphorylation in the regulation of the production of active oxygen metabolites in PMNL.

1This study was supported by Grant-in-Aid for Special Project Research (No. 60214029) from the Ministry of Education, Science and Culture of Japan.


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