1993 Fiscal Year Final Research Report Summary
MODULATION OF CELL BEHAVIORS BY PROTEOGLYCANS WITH ANTI-CELL-SUBSTRATE ADHESION ACTIVITY-STUDIES ON INVOLVING MOLECULES AND THE MECHANISM
| Project/Area Number |
04454595
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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 |
物質生物化学
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| Research Institution | INSTITUTION FOR MOLECULAR SCIENCE OF MEDICINE, AICHI MEDICAL UNIVERSITY |
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Principal Investigator |
KIMATA Koji INSTITUTION 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) |
1992 – 1993
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| Keywords | cell adhesion / anti-adhesion / proteglycans / chondroitin / osteosacoma / PG-M / glycocalfin / annexin |
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| Research Abstract |
Cell adhesion to substrate or cell is a crucial step that regulates a variety of sell behavior. We previously showed that PG-M, a large chondroitin sulfate proteoglycan had an jnhibitory activity for any types of cell-adhesion to ECM and proposed its general role in modulating sell-ECM interactions (J.Biol. Chem., 264, 8012, 1989) Several lines of evidence suggested that the activity could be due to the chondroitin sulfate chains immobilized onto ECM via the core protein moiety. To obtain the direct evidence for the role of PG-M, we investigated the effect of the anitisense specific inhibition of PG-M synthesis on the oncogenic adhesion of human osteosarcoma cells. The inhibition suppressed the malignant cell-adhesive phenotype, consistent with the idea that PG-M controls sell-ECM adhesion. To gain insight into the mechanism, we postulated that the chondroitin sulfate-induced inhibition of sell adhesion might be due to a sell surface receptor capable of intercing specifically with chondroitin sulfate chains, thereby influencing the clustering or conformational change of receptors for ECM molecules. The present results have indicated the occurrence of a 58-kDa protein which had an affinity to the PG-M- OR chondroitin sulfate-immobilized gel column. The interaction of the protein with the column required the presence of Ca^<2+>. According to these properties, 58-kDa protein is now designated glycocalfin could be extracted with a detergent-contergent-containing solution from the membrane fractions of cultured fibroblasts and from the homogenate of minced embryo bodirs. The amino asid sequences of purified of gycocolfin have shown that this molecule is a famiry of annexin VI.Further studies of the protein will answer the question whether our postulated mechanism for the anti-adhesion actibity of immobilized chondroitin sulfate chains could be operative or not.
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Research Products
(19 results)
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[Publications] Iwasaki, M., Nakata, K., Nakahara, H., Nakase, T., Kimura, T., Kimata, K., A.I.Caplan, Ono, K.: "Transforming Growth Factor-beta 1 Stimulates Chondrogenesis and Inhibits Osteogenesis in High Density Culure of Periosteum-Derived Cells" Endocrinology. 132. 1603-1608 (1993)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Sugiura, N., Sakurai, K., Hori, Y., Karasawa, K., Suzuki, S., Kimata, K.: "Preparation of Lipid-derivatized Glycosaminoglycans to Probe a Regulatory Function of the Carbohydrate Moieties of Proteoglycans in Cell-Matrix Interaction" The Journal of Biological Chemistry. 268. 15779-15787 (1993)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Nakase, T., Nakahara, H., Iwasaki M.Kimura, T., Kimata, K., Watanabe K., A., I.Caplan, Ono, K.: "Cional Analysis for Developmental Potentialof Chick Periosteum-Derived cells-Agar Gel Culture System" Biochemical and Biophysical Research Communication. 195. 1422-1488 (1993)
Description
「研究成果報告書概要(欧文)」より
