Thrombin activates a Y box–binding protein (DNA-binding protein B) in endothelial cells
J. Clin. Invest. Olga I. Stenina, et al. 106:579 doi:10.1172/JCI9075 [Go to this article.]

Figure 2
Antibody directed to the COOH-terminus of dbpB recognized a 49-kDa protein in EC lysates as well as in vitro–translated dbpB. (a) In vitro–translated, full-length dbpB labeled with [³⁵S]methionine exhibited an apparent size of 49 kDa in SDS-PAGE (8% gel). The truncated dbpB had an apparent size of 30 kDa (the same size as active dbpB found in extracts from thrombin-stimulated ECs). (b) Western blot of cytosolic extracts of human ECs using an antibody directed to the COOH-terminus of dbpB. In the absence of stimulation, a 49-kDa protein was detected. Stimulation of ECs with thrombin (10 U/mL for 2 hours) resulted in the appearance of a new band of approximately 19 kDa, presumably the COOH-terminus of dbpB cleaved during the process of activation.