1986 Fiscal Year Final Research Report Summary
Studies on biological modifier produced by bacteria
Project/Area Number |
59370017
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Research Category |
Grant-in-Aid for Co-operative Research (A)
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Allocation Type | Single-year Grants |
Research Field |
細菌学
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Research Institution | The Institute of Medical Science, The University of Tokyo (1985-1986) Osaka University (1984) |
Principal Investigator |
TAKEDA Yoshifumi The Institute of Medical Science. The University of Tokyo, 医科学研究所, 教授 (30029772)
|
Co-Investigator(Kenkyū-buntansha) |
HONDA Takeshi Research Institute for Microbial Diseases, Osaka University, 微生物病研究所, 助教授 (60029808)
ARAI Tadashi Research Institue for Chemobiodynamics, Chiba University, 生物活性研究所, 教授 (30009419)
NAKANO Masayasu Jichi Medical School, 医学部, 教授 (70048958)
KATO Iwao School of Medicine, Chiba University, 医学部, 教授 (40012702)
SHIMONISHI Yasutsugu Institue for Protein Research, Osaka University, 蛋白質研究所, 教授 (00029951)
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Project Period (FY) |
1984 – 1986
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Keywords | Bacterial toxin / Bacterial lipopolysaccharide / Biological modifier / 下痢原因毒素 / 耐熱性毒素 |
Research Abstract |
1) The mechanism of signal trunsduction of bacterial enterotoxin in intestinal tissue was investigated as one of the projects. In watery diarrhea caused by heat-stable enterotoxin (ST) of Enterotoxigenic Escherichia coli, it was found that an activation of cyclic GMP dependent protein kinase is a necessary step in its signal transduction and that one of the proteins (81K-, 43K- and 37K- dalfons) phosphorylated by cyclic GMP-dependent protein kinase was also phosphorylated by cyclic AMP-dependent protein kinase in itestinal cells exposed to cholera enterotoxin. This finding suggests that ST and cholear enterotoxin work through a common mechanism after increase of cyclic nucleotide content in intestinal tissue by their primary actions. Similar signal trunsduction pathway was observed in the action of Pseudomonal leukocidin by which <Ca^(2+)> -dependent protein knase of polymorphonuclear leukocyte was activated, following phosphorylation of lysosomal protein. 2) A detailed comparison of structural analysis of heat-stable enterotoxins produced by many enterotoxigenic pathogens indicated the common structure related to heat stability and biological activity. Immunological studies on the structure of cholera enterotoxin suggests the development of new effective vaccine against cholera. 3) It was found that bacterial lipopolysaccharide stimulated the release of interleukin from T cell and enhanced the growth of the cell, indicating the significant role of LPS in immune response.
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