Electron microscopic studies on collagen fibrillogenesis.
| Project/Area Number |
61570009
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
General anatomy (including Histology/Embryology)
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| Research Institution | Department of Anatomy, Nagoya University School of Medicine |
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Principal Investigator |
KOBAYASHI KUNIHIKO Dep. Anat., Nagoya Univ. School Med. Assoc. Prof, 医学部, 助教授 (30001051)
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| Co-Investigator(Kenkyū-buntansha) |
HOSHINO TAKESHI Dep. Anat., Nagoya Univ. School Med. Prof., 医学部, 教授 (40000913)
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| Project Period (FY) |
1986 – 1987
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| Project Status |
Completed (Fiscal Year 1987)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1987: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1986: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | Collagen / Fubrillogenesis / Electron microscopy / Intermolecular association / negative staining / molecular bundle (SLS) / 4D-staggered linear polymer / テロペプチド / Segment-long-spacing |
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| Research Abstract |
1. We previously found that collagen molecules associate at pH 4.5 to specifically form 4D-staggered linear polymers, which are assumed to be the first intermediates in in vitro collagen fibrillogenesis. In this study, we confirmed that the 4D-staggered aggregates (containing various degrees of polymerization) are incorporated into native-type D-periodic fibrils under the physiological conditions. We intended to isolate the oligomers of the different polymericity by gel filtration and to assign the role of each oligomer in collagen fibrillogenesis. The trials were not yet successful.
2. Conditions for electron microscopic identification of the association form of the molecules (dimer) at the first step of collagen self-assembly were investigated and individual methods were optimized. We noticed the direct correlation between negatively stained banding patern of type I collagen molecular bundle (SLS) and the distribution of hydrophobic amino acids along the molecule. The correlation was confirmed with type I and type II collagens.
3. Non-helical parts of the collagen molecule (telopeptide) were revealed to be involved in the 4D-staggered association at pH 4.5.
4. Electron microscopic examination of the sample taken at an early stage of the in vitro fibrillogenesis showed the existance of D-periodic fibrils in addition to thin filaments (preliminaly obsevation).
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Report
(2 results)
Research Products
(16 results)
