Recently, the necessity of designing and applying tool materials that perform machining of difficult-to-cut materials in a cryogenic treatment where demand is increasing. The objective of this study is to evaluate the performance of cryogenically treated WC-5 wt% NbC hard materials fabricated by a pulsed current activated sintering process. The densely consolidated specimens are cryogenically exposed to liquid nitrogen for 6, 12, and 24 h. All cryogenically treated samples exhibit compressive stress in the sintered body compared with the untreated sample. Furthermore, a change in the lattice constant leads to compressive stress in the specimens, which improves their mechanical performance. The cryogenically treated samples exhibit significant improvement in mechanical properties, with a 10.5 % increase in Vickers hardness and a 60 % decrease in the rupture strength compared with the untreated samples. However, deep cryogenic treatment of over 24 h deteriorates the mechanical properties indicating that excessive treatment causes tensile stress in the specimens. Therefore, the cryogenic treatment time should be controlled precisely to obtain mechanically enhanced hard materials.

The neurotrophin plays an important role in the development, differentiation and survival of the nervous system in vertebrates. It exerts its cellular effects through two different receptors, the Trk receptor tyrosine kinase neurotrophin receptor and the p75 neurotrophin receptor, a member of the tumor necrosis factor receptor superfamily. Trk and p75 neurotrophin receptors utilize specific target proteins to transmit signals into the cell. An ankyrin-rich membrane spanning protein (ARMS) was identified as a new p75 interacting protein and serves as a novel downstream target of p75 neurotrophin receptor. We sought to delineate the interaction between p75 and ARMS by deletion constructs of p75 and green fluorescent protein (GFP)-tagged ARMS. We examined the interaction between these two proteins after overexpressing them in HEK-293 cells. Using both Western blot analysis and immunocytochemistry followed by confocal laser scanning microscopy, we found out that the intracellular domain of the p75 neurotrophin receptor was important for the interaction with ARMS. The results from this study suggest that ARMS may play an important role for mediating the signals from p75 neurotrophin receptor into the cell.