| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1990: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1989: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Research Abstract |
Amyloid P component (AP) is a glycoprotein in normal serum. AP deposits as a minor but a common component in amyloid tissues of systemic amyloidosis, familial amyloid polyneuropathy and other amyloidosis. In the previous study we have shown that human serum AP specifically and strongly binds to heparan sulfate and dermatan sulfate in a calcium-dependent manner and proposed that the ligand of AP in amyloid tissues be glycosaminoglycans (J. Biol. Chem. 262,1456-1460, 1987). It is supposed that AP serves as a 'protector' in amyloid deposits shielding the fibrils somehow from degration, whether by acting as a protease inhibitor or by masking the altered nature of the fibrils and thereby preventing them from stimulating or activating phagocytic cells. Therefore, the ligand for AP is expected to dissociate it from amyloid deposits and help degrading anyloid fibrils. In this project we examined several sulfated glycosaminoglycans and found that heparin and dextran sulfte were the most effective in dissociating polymerized AP (Biochim. Biophys. Acta 998, 231-235, 1989). The results suggest that heparin and dextran sulfate are candidates for a dissociating agent of amyloid fibrils. We also determined the structure of oligosaccharide attached to AP and demonstrated limited functions of the sugar unit in binding with ligands (Biochim. Biophys. Acta 1037, 435-438, 1990).
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