| Autor: |
Satoh T; Nippon Roche Research Center, Kanagawa, Japan., Kouns WC, Yamashita Y, Kamiyama T, Steiner B |
| Jazyk: |
angličtina |
| Zdroj: |
The Biochemical journal [Biochem J] 1994 Aug 01; Vol. 301 ( Pt 3), pp. 785-91. |
| DOI: |
10.1042/bj3010785 |
| Abstrakt: |
Arg-Gly-Asp (RGD) is an amino acid sequence in fibrinogen recognized by platelet glycoprotein (GP) IIb/IIIa. Recently, it was found that RGD peptide binding to GPIIb/IIIa leads to conformational changes in the complex that are associated with the acquisition of high-affinity fibrinogen-binding function. In this study, we found that tetrafibricin, a novel non-peptidic GPIIb/IIIa antagonist, induced similar conformational changes in GPIIb/IIIa as did RGD peptides. Tetrafibricin increased the binding of purified inactive GPIIb/IIIa to immobilized pl-80, a monoclonal antibody that preferentially recognizes ligand-occupied GPIIb/IIIa. Exposure of the pl-80 epitope by tetrafibricin was also observed on resting human platelets by flow cytometry. On intact platelets, the conformational changes transformed GPIIb/IIIa into a high-affinity receptor for fibrinogen and triggered subsequent platelet aggregation. Tetrafibricin is the first non-peptidic GPIIb/IIIa antagonist reported that has the capacity to induce conformational changes in GPIIb/IIIa. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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