G-protein dissociation, GTP-GDP exchange and GTPase activity in control and PMA treated neutrophils stimulated by fMet-Leu-Phe |
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| Authors: | T Matsumoto T F Molski Y Kanaho E L Becker R I Sha'afi |
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| Institution: | 1. Clinical Health Radiation Research Department, National Centre for Radiation Research and Technology, Atomic Energy Authority, PO Box 29, Nasr City, Cairo, Egypt;2. Biochemistry Lab. Chemistry Department, Faculty of Education, Ain Shams University, Egypt;1. Department of Pediatrics, Shimane University Faculty of Medicine, 89-1, En-ya-cho, Izumo, Shimane 693-8501, Japan;2. Department of Pediatrics, Hokkaido University School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo 060-8638, Japan;3. Department of Pediatrics, Tsugaru General Hospital, 12-3, Iwaki-cho, Goshogawara, Aomori 037-0074, Japan;4. Department of Pediatrics and Child Health, Nihon University School of Medicine, 1-6, Kanda-Surugadai, Chiyoda-ku, Tokyo 101-8309, Japan;5. Department of Pediatrics, Graduate School of Medicine, Gifu University, 1-1, Yanagito, Gifu 501-1194, Japan;6. Department of Pediatrics, Osaka University Faculty of Medicine, 2-2, Yamadaoka, Suita, Osaka 565-0871, Japan;7. Department of Pediatrics, Osaka Hospital, Japan Community Healthcare Organization, 4-2-78, Fukushima, Fukushima-ku, Osaka 553-0003, Japan;8. Department of Pediatrics, Yawatahama City General Hospital, 638, Ohira-ichibankochi, Yawatahama, Ehime 796-8502, Japan;9. Department of Pediatrics, Ehime University Graduate School of Medicine, Shitsukawa, Toon, Ehime 791-0295, Japan;10. Department of Community and Emergency Medicine, Ehime University School of Medicine, Shitsukawa, Toon, Ehime 791-0295, Japan;11. Department of Pediatrics, Kagoshima City Hospital, 37-1, Uearata-cho, Kagoshima 890-8760, Japan;12. Department of Neurology, Division of Clinical Medicine, Faculty of Medicine, University of Tsukuba, 1-1-1, Tennoudai, Tsukuba, Ibaraki 305-8575, Japan;13. Hokkaido University Hospital Clinical Research and Medical Innovation Center, Research and Development Division, Kita 14, Nishi 5, Kita-ku, Sapporo 060-8648, Japan;14. Hokkaido University Hospital Clinical Research and Medical Innovation Center, Biostatistics Division, Kita 14, Nishi 5, Kita-ku, Sapporo 060-8648, Japan;15. Department of Biostatistics, School of Public Health, Graduate School of Medicine, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan;p. Hokkaido University Hospital Clinical Research and Medical Innovation Center, Kita 14, Nishi 5, Kita-ku, Sapporo 060-8648, Japan |
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| Abstract: | The addition of the chemotactic factor fMet-Leu-Phe to cell homogenates causes a decrease in the pertussis toxin catalyzed ADP-ribosylation of a 41 kDa protein. The fMet-Leu-Phe induced decrease is not abolished in homogenates prepared from phorbol 12-myristate 13-acetate treated neutrophils. This decreased ribosylation probably reflects a dissociation of the GTP-binding protein oligomer that is not followed by association, possibly because of the release of the alpha-subunit into the suspending medium. Furthermore, fMet-Leu-Phe stimulates the binding of radiolabelled guanylylimidodiphosphate to membrane preparations. Again, the stimulated binding of guanylylimidodiphosphate is not affected by treating the intact neutrophils with phorbol 12-myristate 13-acetate. In addition leukotriene B4, platelet activating factor and fMet-Leu-Phe activate a high-affinity GTPase in membrane preparations. The basal level of this GTPase activity is dramatically inhibited in membrane preparations isolated from cells treated with phorbol 12-myristate 13-acetate. On the other hand, the fMet-Leu-Phe stimulated component is only marginally reduced. The present findings suggest that PMA does not prevent receptor G-protein interaction. |
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