1998 Fiscal Year Final Research Report Summary
Characterization of interaction between new cadherins and cytoplasmic proteins
Project/Area Number |
09680713
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Cell biology
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Research Institution | Institute for Developmental Research |
Principal Investigator |
SUZUKI Shintaro Institute for Developmental Research, Department of Developmental Biology ; Director, 発生学部門, 部長 (20128432)
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Project Period (FY) |
1997 – 1998
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Keywords | cell adhesion / cadherin / cytoplasmic domain / catenin / cytoskeleton / phosphorylation / regulation / integrin |
Research Abstract |
The interaction between cadherin-4 and cadherin-5 and cytoplasmic proteins was examined and the following results were obtained. (i) These cadherins interacted with several new molecules in addition to catenins. (ii) Deletion experiments of the cytoplasmic domains showed that the cadherins without the cytoplasmic domains had Ca^<2+> dependent clustering activity as well as cell aggregation activity, indicating that the extracellular domains have the core cadherin activity. (iii) Phosphorylation of serine/threonine decreased the cell adhesion activity of the cadherins. Pl2Octn appears to have cell adhesion inhibitory activity and to be involved in the process. (iv) We also examined some properties of a novel protocadherin, OL-protocadherin, and found that the protocadherin had a possible binding site for PDZ domain. Since OL-protocadherin was expressed in synapses of the main olfactory system and the limbic system, the protocadherin may be involved in the formation and maintenance of these systems.
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Research Products
(6 results)
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[Publications] Mohri, T, Kameshita, S.Suzuki, S, Hioki, K, Tokunaga, R, Taketani, R.: "Rapid Adhesion and Spread of Non-adherent Colon Cancer Colo201 Cells Induced by the Protein Kinase Inhibitors, K252a and KT5720 and Suppression of the Adhesion by Immunosuppressants FK506 and Cyclosporin A." Cell Struc.Func. 23. 255-264 (1998)
Description
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