| Project/Area Number |
09670221
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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 |
Experimental pathology
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| Research Institution | SHINSHU UNIVERSITY |
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Principal Investigator |
SANO Kenji SHINSHU UNIVERSITY SCHOOLOF MEDICINE,DEPARTMENT OF PATHOLOGY,ASSISTANT PROFESSOR, 医学部・第2病理, 講師 (50205994)
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| Co-Investigator(Kenkyū-buntansha) |
ITO Makoto SHINSHU UNIVERSITY SCHOOLOF MEDICINE,DEPARTMENT OF PATHOLOGY,ASSOCIATE PROFESSOR, 医学部・第2病理, 助教授 (70184687)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1998: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 1997: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | VE cadherin / cadherin 5 / cadherin 10 / endothelium / lymph vessel / Ca^<2+>-dependent homophilic adhesion / VE cadherin / cadhern5 / cadhvin10 / endothelum / カドヘリン / 血管型カドヘリン / リンパ管内皮細胞 |
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| Research Abstract |
The cadherins are a superfamily of genetically and functionally related molecules that mediate Ca2+- dependent intercellular adhesion in a homophilic fashion. So far, many types of cadherins and their interspecies homologue have been reported, and each shows distinct immunological reactivity, binding specificity and tissue distribution. Among cadherins, a vascular type of cadherin (VE-cadherin/cadherin 5) is thought to be specific for vascular endothelial cell. Conversely, there were different kind of cadherins reported from cultured endothelial cells, including N-cadherin and P-cadherin as well as VE cadherin. Endothelial cells of lymph vessels (LECs) are distinct from vascular endothelia (VECs) in several ways, which show specific expression of fins-like tyrosine kinase 4 gene in LECs and different expression of 5'-nucleotidase and alkaline phosphatase between them. These data suggest that LECs could express cadherins other than those reported and identified in VECs. To investigate t
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his hypothesis, PCR was done using the mixed primers and endothelial cDNA preparation of dog's thoracic duct. As a result, the sequences revealed two different types of cDNA clones encoding distinctive amino acid sequences homologous with the known cadherins. One showed relatively high homology with cadherin 5 (78%), but shorter by several residues than human cadherin 5. The other showed high homology with human cadherin 10 (92%) : cDNAs corresponding to full length of human cadherin 10 were isolated from a HUVEC (human umbilical vein endothelial cell) cDNA library. Expression of cadherin 10 in HUVEC and LEC is not reported so far. And expression pattern of cadherin 1 0 using established cell line exhibits wide range of cell types. These data indicate that cadherin 10 is a ubiquitous molecule and serves shared function in various cells and tissues. Transfection of cadherin 10 to L cells, which does not express cadherin 10, revealed the acquisition of aggregation reactivity compared to control L cell transfected with vector alone. But the role of cadherin 10 in vivo remains to be elucidated. The distribution in glial cells and endothelial cell in central nervous system suggest cadherin 10 plays an important role in communication between astrocytes and endothelial cells. Less
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