2006 Fiscal Year Final Research Report Summary
Spatio-temporal regulation of morphogenesis by heparan sulfate chains
| Project/Area Number |
14082206
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | Aichi Medical University |
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Principal Investigator |
KIMATA Koji Aichi Medical University, Institute medical Science, Professor (10022641)
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| Co-Investigator(Kenkyū-buntansha) |
HABUCHI Osami Aichi University, Education, Professor (90024067)
HABUCHI Hiroko Aichi Medical University, Institute for medical, Assistant Professor (90329821)
NAGAI Naoko Aichi Medical University, Institute for medical Science, Research Associate (00367799)
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| Project Period (FY) |
2002 – 2006
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| Keywords | Heparan sulfate / Cell growth factors / Morphogen / Concentration gradient / Chondroitin sulfate / Proteoglycans / Glycosaminoglycans / Mutant mouse |
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| Research Abstract |
Heparan sulfate (HS) whose basic backbone structure consists of repeating disaccharide of glucuronosyl glucosamine has astronomical number of different structures by sulfation at different positions and by isomerization of glucuronosyl residue. HS usually locates on the cell surfaces and in the extracellular matrix and its structure alters in a spacio-temporal manner. Most of secretary and soluble cell growth factors, cytokines and morphogens which are well known to be required for important cell activities such as cell proliferation, cell differentiation and cell morphology, for example, FGF and Wnt, have properties to bind to HS. Therefore, we hypothesized that those factors, when they differ, may bind to the HS portions with different structures specifically so that each activity of those factors could be regulated by HS distinctively. In this study we first clarified that different factors actually bind to HS with different O-sulfation positions. We then subjected moue, chicken, Zebrafish, and Drosophila to the alteration of genes for HS O-sulfation enzymes, and observed apparent abnormality of organogenesis and tissue-morphogensis in those animals. We further provided some evidence to show that the observed abnormality was due to altered signalings of those factors which were caused, by the abnormal changes in HS structure. Taken together, our study revealed the occurrence of regulation mechanisms of the activities of cell growth factors and morphogens by HS chains.
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[Journal Article] Heparan sulfate 6-o-sulfotransferase is essential for muscle development in zebrafish.2003
Author(s)
Bink RJ, Habuchi H, Lele Z, Dolk E, Joore J, Rauch QJ, Geisler R, Wilson SW, den Hertog J, Kimata K, Zivkovic D
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Journal Title
J Biol Chem 278
Pages: 31118-31127
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Chondroitin sulfate synthase-2. Molecular cloning and characterization of a novel human glycosyltransferase homologous to chondroitin sulfate glucuronyltransferase, which has dual enzymatic activities.2003
Author(s)
Yada T, Gotoh M, Sato T, Shionyu M, Go M, Kaseyama H, Iwasaki H, Kikuchi N, Kwon YD, Togayachi A, Kudo T, Watanabe H, Narimatsu H, Kimata K
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Journal Title
J Biol Chem 278
Pages: 30235-30247
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Enzymatic synthesis of chondroitin with a novel chondroitin sulfate N-acetylgalactosaminyltransferase that transfers N-acetylgalactosamine to glucuronic acid in initiation and elongation of chondroitin sulfate synthesis2002
Author(s)
Gotoh M, Sato T, Akashima T, Iwasaki H, Kameyama A, Mochizuki H, Yada T, Inaba N, Zhang Y, Kikuchi N, Kwon YD, Togayachi A, Kudo T, Nishihara S, Watanabe H, Kimata K, Narimatsu H
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Journal Title
J Biol Chem 277
Pages: 38189-38196
Description
「研究成果報告書概要(欧文)」より
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