| Project/Area Number |
06454647
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Structural biochemistry
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| Research Institution | INSTITUTE FOR MOLECULAR SCIENCE OF MEDICINE,AICHI MEDICAL UNIVERSITY |
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Principal Investigator |
KIMATA Koji INSTITUTE FOR MOLECULAR SCIENCE OF MEDICINE,AICHI MEDICAL UNIVERSITY,PROFESSOR, 分子医科学研究所, 教授 (10022641)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥6,300,000 (Direct Cost: ¥6,300,000)
Fiscal Year 1995: ¥2,700,000 (Direct Cost: ¥2,700,000)
Fiscal Year 1994: ¥3,600,000 (Direct Cost: ¥3,600,000)
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| Keywords | Cell adhesion inhibition / Cell-substrate interaction / Anti-adhesion / Chondroitin sulfate / PG-M / Glycocalfin / Annexin / Chondroitin sulfate proteoglycan / annexin VI / glycocalfin / 抗一細胞接着 / annexinVI / 細胞接着 / アルタナティブスプライシンク |
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| Research Abstract |
1) Studies on the mechanisms for nati-adhesive activity of PG-M : In order to suggest a molecular biological strategy for glycocalfin which is a cell-surface receptor postulated to transmit the antiadhesive activity of PG-M to cells we first tried to isolate glycocalfin cDNA.Partial amino acid sequences and the immunoreactivity to various antibodies of glycocalfin purified from cultured human cells by the affinity chromatography using chondroitin sulfate-conjugated gels have revealed the complete identity of glycocalfin to annexin VI.This conclusion has enabled us to obtain the cDNA,because the cDNA is already available. Further studies on the anti-adhesive activity of PG-M using the following three different types of assay methods have convinced the above strategy : Comparisons of cell adhesion to fibronectin-coated U-shape dishes under the centrifugal force ; binding activities of liposome-intercalated integrin to substrates ; adhesion of half-denatured cells to substrates. All the results have suggested that PG-M only interrupt cell-spreading but not cell-binding probably by glycocalfin-mediated signal transduction. (2) Regulation of cell behaviors by anti-adhesion activity of PG-M : We have finished the cDNA analysis, northern analysis, and genomic DNA analysis for chicken, mouse, and human PG-Ms. The results have suggested the presence of multiple forms of PG-M with different anti-adhesive activity due to the different chondroitin sulfate chain number and their tissue- and developmental stage-dependent alterations. For example, the largest form of PG-M (the richest in the chain) was found in the early stages of development. It is likely, therefore, that specific mechanisms may be involved in the anti-adhesion of PG-M.
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