On the passive and semiconducting behavior of severely deformed pure titanium in Ringer's physiological solution at 37°C: A trial of the point defect model.

The effects of sever plastic deformation through multi-pass accumulative roll bonding on the passive and semiconducting behavior of pure titanium is evaluated in Ringer's physiological solution at 37°C in the present paper. Produced results by polarization plots and electrochemical impedance spectroscopy measurements revealed a significant advance in the passive response of the nano-grained sample compared to that of the annealed pure titanium. Also, Mott-Schottky test results of the nano-grained pure titanium represented a lower donor density and reduced flat-band potential in the formed passive film in comparison with the annealed sample.

The role of grain refinement and film formation potential on the electrochemical behavior of commercial pure titanium in Hank's physiological solution.

In this study, the electrochemical behavior and semiconducting properties of the passive film formed on the nano-grained commercial pure titanium (CP-Ti), successfully made by seven-cycle accumulative roll bonding process, were compared to those for annealed CP-Ti in Hank's physiological solution at 37°C. Polarization plots and electrochemical impedance spectroscopy measurements revealed that the passive behavior of the nano-grained sample was significantly improved in comparison with that of annealed CP-Ti. Mott-Schottky analysis showed that the passive film formed on the nano-grained CP-Ti had a lower donor density and reduced flat-band potential than annealed sample.

Cell biology of Smad2/3 linker region phosphorylation in vascular smooth muscle.

The transforming growth factor (TGF)-β superfamily of ligands regulates a diverse set of cellular functions. Transforming growth factor-β induces its biological effects through Type I and Type II transmembrane receptors that have serine/threonine kinase activities and weak tyrosine kinase activity. In vascular smooth muscle, TGF-β binds to the TGF-β Type II receptor (TβRII) at the cell surface, recruiting the Type I receptor (TβRI) to form a heterocomplex.