Abstract
Collagen is one of the most physiologically important agonists for platelet function. Two collagen-specific receptors, integrin α2β1 and glycoprotein (GP) VI, have been identified on the platelet surface from studying patient’s platelets deficient in one of these proteins (1,2). Integrin α2β1 was found to be the major receptor responsible for platelet adhesion to collagen (3,4). The other collagen receptor, GPVI, was indicated to contribute to platelet activation and aggregation by its involvement in collagen-induced signaling pathways (5,6).
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Notes
- 1.
1
Where no specific source is indicated, reagents can be obtained from any manufactuer.
- 2.
2
All these buffers should be divided into convenient aliquots, and stored at −20°C. They can be kept indefinitely in the deep freezer and then thawed out as needed.
- 3.
3These buffers contain MgCl2 and BSA or EDTA and BSA at 7 times the final concentrations in the binding mixtures. In the binding assay mixture (70 μL total volume), 10 μL of either binding buffer will be used, so the final concentrations of MgCl2 will be 2 mM and that of EDTA will be 5 mM, with 1% (w/v) BSA.
- 4.
3These buffers contain MgCl2 and BSA or EDTA and BSA at 7 times the final concentrations in the binding mixtures. In the binding assay mixture (70 μL total volume), 10 μL of either binding buffer will be used, so the final concentrations of MgCl2 will be 2 mM and that of EDTA will be 5 mM, with 1% (w/v) BSA.
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Jung, S.M., Moroi, M. (2004). Ligand-Binding Assays for Collagen. In: Gibbins, J.M., Mahaut-Smith, M.P. (eds) Platelets and Megakaryocytes. Methods in Molecular Biology™, vol 273. Humana Press. https://doi.org/10.1385/1-59259-783-1:105
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DOI: https://doi.org/10.1385/1-59259-783-1:105
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