1995 Fiscal Year Final Research Report Summary
REGULATION OF VARIOUS CELL BEHAVIORS BY PROTEOGLYCANS THAT INHIBIT CELL-ADHESION,ANTI-ADHESIVE MOLECULES
| 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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| Keywords | Cell adhesion inhibition / Cell-substrate interaction / Anti-adhesion / Chondroitin sulfate / PG-M / Glycocalfin / Annexin / Chondroitin sulfate proteoglycan |
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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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[Publications] Watanabe, H., L.Gao, Sugiyama, S., Doege, Kimata, K.and Yamada, Y.: "Mouse aggrecan, a large cartilage proteoglycan : protein sequence, gene structure and promoter sequence" Biochem.J.308. 434-440 (1995)
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[Publications] Kato, S., Sugiura, N., Kimata, K., Kujiraoka, T., Toyoda, J.and Akamatsu J.: "Chondroitin sulfate immobilized onto culture substrates modulates 6DNA synthesis, tyrosine aminotransferase induction, and intercellular communication in primary rat hepatocytes" Cell Struct.funct.20. 199-209 (1995)
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[Publications] Fukuoka, M., Uchimura, K., Nakashima, K., Kato, M., Kimata, K.Shinomura, T.and Habuchi, O.: "Molecular cloning and expression of chick chondrocyte chondroitin 6-sulfotransferase" J.Biol.Chem.270. 18575-18580 (1995)
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[Publications] Zhao, M., Yoneda, M., Ohashi, Y., Kurono, S., Iwata, H., Ohnuki, Y.and Kimata, K.: "Evidence for the covalent binding of SHAP,heavy chains of inter-alpha-trypsin inhibitor, to hyaluronan" J.Biol.Chem.270. 23657-23663 (1995)
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[Publications] Sugiura, N., Iwasaki, S., Aoki, S., Hori, Y., Sakurai, S., Suzuki, S.and Kimata, K.: "Suppression of pannus-like extension of synovial by lipid derivatized chondroitin sulphate : in vitro and in vivo studies using epsilonscherichia coli-induced arthritic rabbits" Int.J.Exp.Path.76. 369-379 (1995)
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