2005 Fiscal Year Final Research Report Summary
Morphofunctional analysis of the membrane skeletal protein 4.1B
| Project/Area Number |
16590141
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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 |
General anatomy (including Histology/Embryology)
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| Research Institution | University of Yamanashi |
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Principal Investigator |
TERADA Nobuo University of Yamanashi, Department of Research, Interdisciplinary Graduate School of Medicine and Engineering, Research Associate, 大学院・医学工学総合研究部, 助教授 (60293461)
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| Project Period (FY) |
2004 – 2005
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| Keywords | Membrane skeleton / Protein 4.1 / cell adhesion / immunohistochemistry / freezing methods |
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| Research Abstract |
Erythrocytes dynamically change their membrane skeletons under their membranes to resist shear stresses during flowing in vessels, to transport oxygen in whole body. One of the membrane skeletal proteins, 4.1 family members, interacts with spectrin-actin networks and also to the intramembranous proteins. The protein 4.1B was originally found to be localized in paranodes and juxtaparanodes of myelinated nerve fibers. By using specific antibody against 4.1B, we found that 4.1B localized also along cell membranes of unmyelinated nerve fiber axons. In addition to the nervous system, 4.1B and another 4.1 family member, 4.1G, are broadly immunolocalized in the kidney, intestine, pancreas, testis and the thymus. Our recent immunohistochemical studies on protein 4.1 family proteins have indicated their significance for the cell-cell and/or cell-matrix adhesion in various rodent organs. On the other hand, analyses for dynamic states of tissues and organs were performed with in vivo cryotechnique. Thus, in this study, we have proven that the 4.1 family-containing membrane skeletons are a general structure under the cell membranes, and our studies probably give clues what tissues and/or organs use this system for analyzing molecular complexes.
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