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Blood, Vol. 110, Issue 7, 2466-2474, October 1, 2007 This Article Abstract Full Text Services Email this article to a friend Alert me to new issues of the journal Rights and Permissions Citing Articles Citing Articles via CrossRef Roles of the C-terminal tyrosine residues of LAT in GPVI-induced platelet activation: insights into the mechanism of PLC2 activation Blood Ragab et al. 110: 2466 Supplemental materials for: Ragab et al, Vol. 110, Issue 7, 2466-2474 Files in this Data Supplement: Figure S1. Comparable level of expression of LAT, PLCγ2 and GPVI in WT, Lat3YF and LatY136F platelets (PDF, 57.8 KB) - Same amounts of platelets from WT, Lat3YF and LatY136F mice were lysed in RIPA buffer, the proteins were separated by SDS-PAGE and transferred onto nitrocellulose, and LAT and PLC2 were detected by immunoblotting. GPVI was probed using biotinylated-Cvx as described.27 Figure S2. Mutations of the three C-terminal tyrosines or tyrosine 136 of LAT affect platelet aggregation in response to low concentrations of collagen (PDF, 135 KB) - Platelets from the different mice strains were stimulated with increasing concentrations of collagen and aggregation was assessed using a Chrono-log dual channel aggregometer under stirring at 900 rev/minutes (A and B). The aggregation induced by 0.2 IU/mL thrombin is shown (C and D). The profiles shown are representative of three independent experiments. This Article Abstract Full Text Services Email this article to a friend Alert me to new issues of the journal Rights and Permissions Citing Articles Citing Articles via CrossRef

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