1997 Fiscal Year Final Research Report Summary
The Signal Transduction Mechanisms of a GPI-anchored Complement Regulatory Protein, CD59.
| Project/Area Number |
08672654
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Laboratory medicine
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| Research Institution | Osaka Medical College |
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Principal Investigator |
HATANAKA Michiyo Osaka Medical College, Clinical Pathology, Assistant Professor, 医学部, 助手 (50218484)
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| Co-Investigator(Kenkyū-buntansha) |
SEYA Tsukasa Osaka Medical Center for Cancer and Cardiovascular Diseases., 6部, 部長
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| Project Period (FY) |
1996 – 1997
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| Keywords | GPI-anchored protein / complement regulatory protein / CD59 / dimer formation / signal transduction / C9 / peptide / intracellular Ca^<2+> concentration |
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| Research Abstract |
Many proteins are attached to the cell membranes via glycosyl phosphatidyl anchor rather than by a transmembrane anchor and have no direct contact with the inside of the cells. Despite this, cross-linking of GPI-anchored proteins with antibodies causes activation of T cells and neutrophils. The activation is likely to be mediated through Src kinases. It has been suggested that interaction of the GPI-anchored molecule with kinases requires a transmembrane-transducing element, the identity of which remained controversial.
In this study, we focused on a GPI-anchored complement regulatory protein, CD59, as a model, to elucidate the GPI-anchored protein mediating signaling. We identified CD59 associating protein by cross-linking of surface proteins with chemical cross-linker followed by Western blotting with anti-CD59 antibody. The Cd59-associating molecules were estimated to be 13-18 kDa in size. Two-dimensional electrophoresis of the cross-linked products revealed no trace of molecules other than CD59. The cross-linked products showed the same N-terminal sequences as CD59 and a strikingly similar amino acid composition to that of CD59. Thus, most likely, the cross-linked products are CD59 dimers. The finding that CD59 localized on outer membranes is all in the form of dimers suggests the importance of dimerization for CD59 functioning.
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[Publications] Hatanaka, M., Seya, T., Miyagawa, S., Matsumoto, M., Hara, T., Tanaka, K., and Shimizu, A.: "Cellular distribution of a GPI-anchored complement regulatory protein CD59 : homodimerization on the surface of HeLa and CD59-transfected CHO cells." J.Biochem.123 (in press). (1998)
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[Publications] Seya, T., Kurita, M., Iwata, K., Yanagi, Y., Tanaka, K., Hatanaka, M., Matsumoto, M., Hirano, A., Ueda, S., and Nagasawa, S.: "The CD46 transmembrane domain is required for efficient measles virus-mediated syncytium formation." Biochem.J.322. 135-144 (1997)
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[Publications] Hatanaka, M., Seya, T., Matsumoto, M., Hara, T., Nonaka, M., Inoue, N., Takeda, J., and Shimizu, A.: "Mechanisms by which GPI-anchored complement regulatory proteins, DAF and CD59, are lost in human leukemia cell lines." Biochem.J.314. 969-976 (1996)
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[Publications] Miyagawa, S., Mikata, S., Shirakura, R., Matsuda, H., Nagasawa, S., Terado, A., Hatanaka, M., Matsumoto, M., and Seya, T.: "C5b-8 step lysis of swine endotherial cells by human complement and functional feature of transfectected Cd59." Scand.J.Immunol.43. 361-366 (1996)
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[Publications] Seya, T., Matsumoto, M., Hatanaka, M., Okada, M., Masaki, T.et al.: "A rapid and efficient purification procedure of human complement receptor type 1 (CR1, CD35)." J.Biochem.Biophys.Methods.32. 69-76 (1996)
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