2005 Fiscal Year Final Research Report Summary
Functional analyses of basement membrane components in association and dissociation of hemidesmosomal adhesion structures
| Project/Area Number |
15390341
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Dermatology
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| Research Institution | Nagoya University |
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Principal Investigator |
OWARIBE Katsushi Nagoya University, Graduate School of Science, Professor, 大学院・理学研究科, 教授 (90109257)
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| Co-Investigator(Kenkyū-buntansha) |
HIRAKO Yoshiaki Nagoya University, Graduate School of Science, Lecturer, 大学院・理学研究科, 講師 (50377909)
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| Project Period (FY) |
2003 – 2005
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| Keywords | hemidesmosome / basement membrane / laminin 5 / BP180 / type XVII collagen / matrix metalloproteinase |
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| Research Abstract |
Supported by this grant, we have obtained following achievements.
1 We have succeeded in isolating a basement membrane (BM) fraction and prepared a panel of monoclonal antibodies to BM components. Using the antibodies we demonstrated that glandular myoepithelial cells have both the epithelial-type hemidesmosome (HD) and the smooth muscle-type adherens junction as cell-matrix adhesion apparatus. We also showed that processing of laminin γ2 subunit facilitates the turnover of laminin 5 in the matrix.
2 We demonstrated that the cleavage of the extracellular domain of BP180/type XVII collagen is done by a matrix metalloproteinase on the cell surface, not in the intracellular membrane.
3 We investigated HD-type adhesion structures in simple epithelia, and found an expression of BP180, in addition to type II HD-components consisting of plectin and integrin α6β4, in colon epithelial cells, and no HD component except integrin α6β4 in uriniferous tubular epithelial cells, suggesting the presence of novel adhesion structure.
4 We isolated a 180/200 kD protein from rabbit smooth muscle cells and identified it as mammalian synemin, an intermediate filament protein, and demonstrated that this protein is expressed in all four types of muscle cells including myoepithelial cells, interacting with other IF-proteins such as keratin and desmin.
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