1990 Fiscal Year Final Research Report Summary
Studies on the effects of ADP-ribosyltransferase activities of staphylococcal cytolytic toxins on the signal transduction in cell membrane.
Project/Area Number |
01570228
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Research Category |
Grant-in-Aid for General Scientific Research (C)
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Allocation Type | Single-year Grants |
Research Field |
細菌学
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Research Institution | Chiba University |
Principal Investigator |
NODA Masatoshi Chiba University, School of Medicine, Professor, 医学部, 教授 (60164703)
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Co-Investigator(Kenkyū-buntansha) |
MORINAGA Naoko Chiba University, School of Medicine, Assistant, 医学部, 助手 (20092108)
KATO Iwao Chiba University, School of Medicine, Professor, 医学部, 教授 (40012702)
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Project Period (FY) |
1989 – 1990
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Keywords | Staphylococcal alpha-toxin / Leukocidin S and F comp. / ADP-ribosyltransferase / Phospholipase A_2 / Phospholipase C / GTP-binding protein / Protein kinase C / PI代謝 |
Research Abstract |
1. Staphylococcal alpha-toxin resulted in ADP-ribosylation of the 37 and 41 kDa proteins of a membrane preparation from rabbit erythrocytes. In the presence of 100 muM GTP, the toxin ADP-ribosylated proteins of 54 and 59 kDa and potentiated ADP-ribosylation of the 37 and 41 kDa forms. GTP had no effect on ADP-ribosylation of membrane proteins in the absence of alpha-toxin. 2. Incubation of a membrane preparation of rabbit polymorphonuclear leukocytes with the S and F components of staphylococcal leukocidin resulted in ADP-ribosylation of the 37 and 41 kDa proteins, respectively. Furthermore, the 37, 41, 54 and 59 kDa proteins were ADP-ribosylated by leukocidin in the presence of GTP. 3. The ADP-ribosylation of these proteins was observed to be dependent on the incubation time and toxin dose and was abolished by prior boiling. Addition of agmatine did not attenuate ADP-ribosylation of these proteins. 4. The S component of staphylococcal leukocidin ADP-ribosylated 37 kDa GTP-binding protein involved in the transduction to activate phospholipase A_<2'> and the F component resulted in ADP-ribosylation of 41 kDa GTP-binding protein involved in the transduction to activate phosphoinositide-specific phospholipase C.
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