Role of Fibronectin on Thrombus Formation
| Project/Area Number |
06672299
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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 |
Laboratory medicine
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| Research Institution | Yokohama City University |
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Principal Investigator |
MOHRI Hiroshi Yokohama City Univ., First Dept. of Internal Med, Assistant Prof., 医学部, 講師 (80119271)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 1995: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1994: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | Fibronectin / Glycoprotein IIb / IIIa / Thrombosis / RGD / 合成ペプチド / 血小板 / GPIIb / RGD非依存性 |
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| Research Abstract |
Fibronectin has been shown to bind to glycoprotein (GP) IIb/IIIa in Arg-Gly-Asp (RGD) -dependent and-independent manners. RGD-independent binding sites are located in the N-terminal region of the cell-binding domain (residues from Ile^<1359> to Ser^<1436>) and in the C-terminal heparin-binding domain of fibronectin (residues from Ala^<1597> to Glu^<1963>). We provide here evidence that peptides (residues 1371-1382 and 1377-1388) in the cell-binding domain inhibited fibronectin binding to GPIIb/IIIa and a peptide (residues 1704-1718) inhibited 29kDa fragment of fibronectin to GPIIb/IIIa by interacting directly with this receptor. In addition, these peptides also inhibited ADP-induced platelet aggregation. Binding of 29kDa fragment of fibronectin to GPIIb/IIIa was not inhibited by RGDS peptide and the peptides in the cell-binding domain. It may suggest that binding site in the C-terminal heparin-binding domain may be different from those of RGDS and the peptides in the cell-binding domain. The idintification of minimal peptide ligands that participate in the recognition of GPIIb/IIIa may be the key to understand the mechanism of thrombus formation.
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Report
(3 results)
Research Products
(15 results)
