Adhesion and spreading of human platelets on the FAS1 domain of TGFBIp. (A) Schematic representation of TGFBIp, which consists of 4 homologous internal repeat domains called Fasciclin 1 (FAS1), and various deletion constructs of TGFBIp for each FAS1 and other modifications. (B) Dose-dependent adhesion of the immobilized FAS1 domain of TGFBIp is shown. Washed platelets were allowed to adhere to the indicated FAS1 domain and are presented as platelet adhesion to each immobilized FAS1 domain of TGFBIp (1, 2, 5, and 10 μg/mL). Washed platelet adhesion (C) and spreading (D) on TGFBIp and each of the indicated FAS1 domains were detected. Platelet adhesion was detected by the acid phosphatase assay, spreading was detected by the use of the MetaMorph program. Results are expressed as a percent of TGFBIp adhesion. All results are shown as the means ± SD of 3 different experiments and ANOVA. *P < .05 compared with BSA.