Molecular mechanism underlying cell adhesion to basement membrane laminins

2015 Fiscal Year Final Research Report

• Project/Area Number: 25440047
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Functional biochemistry
• Research Institution: Osaka University
• Principal Investigator: Yamada Masashi 大阪大学, たんぱく質研究所, 助教 (90304055)
• Co-Investigator(Renkei-kenkyūsha): SEKIGUCHI Kiyotoshi 大阪大学, たんぱく質研究所, 教授 (50187845)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Keywords: 細胞外マトリックス / 基底膜 / ラミニン / インテグリン / テトラスパニン

Outline of Final Research Achievements

Analysis of a disease-associated mutation of the laminin-binding integrin α3: A missense mutation that causes substitution of Arg628 with Pro (R628P) in the calf-1 domain of human α3 was shown to be associated with disorders of the lung, kidney, and skin. We found that the R628P mutation leads to aberrations in the posttranslational processing of α3. This mutation abolished the interaction of α3 with the tetraspanin CD151 but not integrin β1.
The role of laminin-binding integrins in epithelial polarity: To elucidate the mechanism underlying epithelial polarity formation, we employed and compared tumor and non-tumor cell lines with distinct abilities to develop epithelial polarity. We found that expression levels of laminin-binding integrins were quite low in some cancer cells compared with non-tumor cells. Furthermore, the exogenous expression of the laminin-binding integrin in these cells promoted the formation of epithelial polarity in 3D culture.

Free Research Field

分子細胞生物学