| Project/Area Number |
08458255
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | SAITAMA MEDICAL SCHOOL |
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Principal Investigator |
KITAMURA Kunio Saitama Medical School, Physiology, Associate Professor, 医学部, 助教授 (70049857)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1997: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | peripheral nerve myelin / adhesion proteins / carbohydrate structure / sulfated glucurenic acid / HNK-1 / biosensor / 接着糖蛋白質 |
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| Research Abstract |
We have analyzed the oligosaccharides of the glycoproteins (PO and PAS-II/PMP-22) in peripheral nerve myelin from various mammalian species. The oligosaccharide moieties of both proteins contain sulfated glucuronic acid as a common constituent, suggesting that the sulfated glucuronic acid may be a key molecule in the adhesion functions of the glycoproteins. Since the PO protein is known to play a role in adhesion of myelin membranes by a homophilic manner, carbohydrate-carbohydrate interaction was analyzed by biosensor apparatus. However any interaction among oligosaccharides could not be observed. Then we have analyzed the interaction between oligosaccarides and polypeptides from PO protein by an affinity column. One peptide fragment which interacted specifically with sulfated glucuronic acid was obtained. By the sequence analysis of the peptide revealed that the peptide has a significant homology to the laminin G2 domain, which is known to be an essential site of sulfated glucuronic acid binding property of laminin. Therefore, the sulfated glucuronic acid is the requisite molecule for the homophilic adhesion property of the PO protein and eventually for myelination.
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