Abstract
The fibrinogen receptor GPIIb-IIIa plays a crucial role in platelet aggregation. Here we show that the adenine nucleotide, 8-azido-ATP, inhibits ADP-induced conformational change of the platelet fibrinogen receptor GPIIb-IIIa (integrin αIIbβ3). Photoaffinity labeling of intact platelets with 8-azido[α-32P]ATP exclusively modifies two plasma-membrane glycoproteins which are identical with both subunits of GPIIb-IIIa. The presence of adenine-nucleotide-binding sites on GPIIb-IIIa implies that the platelet fibrinogen receptor is directly regulated by extracellular adenine nucleotides.
Original language | English (US) |
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Pages (from-to) | 77-81 |
Number of pages | 5 |
Journal | BBA - Molecular Cell Research |
Volume | 1137 |
Issue number | 1 |
DOIs | |
State | Published - Oct 6 1992 |
Externally published | Yes |
Keywords
- 8-azido-ATP
- GPIIb-IIIa
- Integrin α IIbβ3
- Nucleotide binding
- Photoaffinity labeling
- Platelet
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology