Moreover, BMP 2 was found to be able to induce osteogenic and chondrogenic phenotypes in WY 14643 adipocyte stem cells, which can be inhibited by the simultaneous TGFb1 treatment. However, in some other cell model systems, TGFb was identified as acting synergistically with BMP signaling. For example, TGFb can directly induce Smad1 phosphorylation in endothelial cells, by forming complexes between TbRII and ALK1, thus leading to stimulation of cell proliferation and migration. Besides, TGFb induced Smad1 phosphorylation was also identified in the C2C12 cells, keratinocytes, MEFs and HepG2 cells, suggesting that the synergetic effect of TGFb on BMP signaling may exist in many other tissues during tissue development and homeostasis.The event correlated to the endothermic peak was slower than that observed in the presence of PC liposomes. On the other hand, for PC:PE:SPM:Cho, the binding of wtEBO16 was less exothermic than the binding of EBO16-W8A, and the endothermic peak was sharper and the event correlated to it was faster . Thus, the data show that wtEBO16 and its mutant EBO16-W8A can interact with membranes of different lipid compositions but with a distinct energetic response. In addition, a more complex event was observed in the presence of lipid rafts. In general, the isothermal titration is performed by several injections, but after each one the heat flux tends to return to the equilibrium that is reflected in the return to the baseline level. In the case of DRMs, the return to the baseline level failed probably because of the presence of a very slow additional endothermic event. As shown in Fig. 5D and E, the Ebola fusion peptide was more efficient to induce aggregation of DRMs than vesicles of other lipid compositions. However, the energetic response for the interaction between EBO16-W8A and DRMs from BHK-21 cells showed a small endothermic and exothermic contribution. In contrast, wtEBO16 induced an exothermic curve with a positive slope increasing with time after its interaction with DRMs. It is a type II transmembrane glycoprotein with 756 amino acids, residing predominantly in the Golgi apparatus. Its N-terminal and C-terminal domains have sequence similarities to bacterial aglycosyltransferase and mammalian b-1,3-N-acetylglucosaminyltransferase, respectively. Despite the fact that glycosyltransferase activity of the LARGE gene has not been demonstrated, accumulating evidence suggested that LARGE plays a critical role in biosynthesis of the functional glycans of a-DG, which can be detected by immuno-staining with the IIH6 and VIA4 monoclonal antibodies and laminin binding assays.