Discontinuous Precipitation and Phase Stability In Re- and Ru-Containing Nickel-Base Superalloys

The phase stability of nickel-base superalloys has been investigated using a new in-house-designed alloy series with stepwise increased additions of Re and Ru at otherwise fixed atomic fractions of alloying elements. Results presented in this study are focused on the lesser-known topologically closed packed (TCP) formation of columnar colonies or so-called discontinuous precipitation. A detailed investigation of these colonies allowed for identifying compositional changes during the growth process and for providing a three-dimensional (3-D) illustration of the TCP phases within these colonies. The results were used to compare the colony growth process with existing growth models. Furthermore, the influence of Re and Ru on the appearance of discontinuous precipitation has been investigated by means of colony width and the effect on creep properties. Larson-Miller plots are given to illustrate the creep strength of directionally solidified samples with and without TCP colonies compared with single crystalline samples free from TCP colonies.     

Specificity of the SH2 domains of SHP-1 in the interaction with the immunoreceptor tyrosine-based inhibitory motif-bearing receptor gp49B

Inhibitory receptors on hemopoietic cells critically regulate cellular function. Despite their expression on a variety of cell types, these inhibitory receptors signal through a common mechanism involving tyrosine phosphorylation of the immunoreceptor tyrosine-based inhibitory motif (ITIM), which engages Src homology 2 (SH2) domain-containing cytoplasmic tyrosine or inositol phosphatases. In this study, we have investigated the proximal signal-transduction pathway of an ITIM-bearing receptor, gp49B, a member of a newly described family of murine NK and mast cell receptors. We demonstrate that the tyrosine residues within the ITIMs are phosphorylated and serve for the association and activation of the cytoplasmic tyrosine phosphatase SHP-1. Furthermore, we demonstrate a physiologic association between gp49B and SHP-1 by coimmunoprecipitation studies from NK cells. To address the mechanism of binding between gp49B and SHP-1, binding studies involving glutathione S-transferase SHP-1 mutants were performed. Utilizing the tandem SH2 domains of SHP-1, we show that either SH2 domain can interact with phosphorylated gp49B. Full-length SHP-1, with an inactivated amino SH2 domain, also retained gp49B binding. However, binding to gp49B was disrupted by inactivation of the carboxyl SH2 domain of full-length SHP-1, suggesting that in the presence of the phosphatase domain, the carboxyl SH2 domain is required for the recruitment of phosphorylated gp49B. Thus, gp49B signaling involves SHP-1, and this association is dependent on tyrosine phosphorylation of the gp49B ITIMs, and an intact SHP-1 carboxyl SH2 domain.