1999 Fiscal Year Final Research Report Summary
Analysis of cellular factors during Sendai virus-induced cell fusion.
| Project/Area Number |
10660070
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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 |
応用微生物学・応用生物化学
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| Research Institution | IWATE UNIVERSITY |
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Principal Investigator |
TAIRA Hideharu Iwate University, Fac. Agric., Professor, 農学部, 教授 (70045756)
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| Project Period (FY) |
1998 – 1999
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| Keywords | Sendai virus / cell fusion / calpain / erythrocyte / ankyrin |
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| Research Abstract |
Sendai virus induces the fusion of human erythrocytes in the presence of exogenous CaィイD12+ィエD1. Fused erythrocytes of large sizes having a diameter of more than 10 times as compared to that of a single erythrocytes were detected. Under these conditions, calcium-activated neutral protease (μ-calpain) in erythrocytes was activated autolytically in accordance with fusion.
To identify the protein species which are degraded upon activation of intracellular μ-calpain, the proteins recovered in the membrane fractions were analyzed by SDS-PAGE and immunoblotting. Limited and specific degradation of ankyrin, one of the membrane skeleton proteins, was observed.
A specific calpain inhibitor, Cbz-Leu-Leu-aldehyde (ZLLal), inhibited membrane fusion, autolytic activation of μ-calpain and the degradation of ankyrin. A specific inhibitor of the proteasome, Lactacystin, did not inhibit the activation of μ-calpain and the degradation of ankyrin by treatment with CaィイD12+ィエD1 and A23187. These results suggested that Sendai virus induced fusion of erythrocytes is regulated by the activation of μ-calpain, followed by the degradation of ankyrin.
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