Optimization of the Post-Process Heat Treatment Strategy for a Near-α Titanium Base Alloy Produced by Laser Powder Bed Fusion.

During the last decades, titanium alloys have been of great interest for lightweight applications due to their high strength in combination with a low material density. Current research activities focus on the investigation of near-α titanium alloys produced by laser powder bed fusion (LPBF). These alloys are known for their superior tensile strength and high creep resistance. This study focuses on the optimization of post-process heat treatments and the impact on tensile and creep strength of a LPBF produced Ti6242S alloy. Therefore, a variety of annealing steps were conducted to gain knowledge about the decomposition process of the non-equilibrium as-built microstructure and the arising influence on the mechanical properties. Components made of Ti6242S and produced by LPBF reveal an extraordinarily high ultimate tensile strength of about 1530 MPa at room temperature, but show a low elongation at fracture (A5 = 4.3%). Based on microstructure-property relationships, this study recommends precise heat treatments on how to improve the desired mechanical properties in terms of strength, ductility as well as creep resistance. Moreover, this study shows a triplex heat treatment, which enhances the elongation at fracture (A5) to 16.5%, while the ultimate tensile strength is still at 1100 MPa.

Microstructural evolution of a dual hardening steel during heat treatment.

Dual hardening steels combine precipitation of both secondary hardening carbides and intermetallic phases in a martensitic matrix. Due to this combination, the carbon content necessary to achieve high hardness levels can be reduced, resulting in a decreased amount of large and embrittling carbides. In this study, the influence of different heat treatments on microstructure evolution and secondary hardness is investigated. Different metallographic preparation methods were tested in order to visualize the microstructure. Carbides were characterized using spot-pattern electron backscatter diffraction. For light optical investigations, preparation with V2A-pickle lead to the best results. Preparation with colloidal silica suspension achieved the best results for investigations by scanning electron microscopy and for carbide characterization using electron backscatter diffraction. It was found that a homogenization treatment prior to austenitization was unable to increase the amount of dissolved carbides, and thus had no effect on secondary hardness. By increasing the austenitization temperature, the amount of carbides and secondary hardness could be increased significantly.

Recruitment of ikaros to pericentromeric heterochromatin is regulated by phosphorylation.

Ikaros encodes a zinc finger protein that is involved in heritable gene silencing. In hematopoietic cells, Ikaros localizes to pericentromeric heterochromatin (PC-HC) where it recruits its target genes, resulting in their activation or repression via chromatin remodeling. The function of Ikaros is controlled by post-translational modifications. CK2 kinase has been shown to phosphorylate Ikaros at its C terminus, affecting cell cycle progression. Using in vivo labeling of murine thymocytes followed by phosphopeptide mapping, we identified four novel Ikaros phosphorylation sites. Functional analysis of phosphomimetic mutants showed that the phosphorylation of individual amino acids determines the affinity of Ikaros toward probes derived from PC-HC. In vivo experiments demonstrated that targeting of Ikaros to PC-HC is regulated by phosphorylation. The ability of Ikaros to bind the upstream regulatory elements of its known target gene terminal deoxynucleotidyltransferase (TdT) was decreased by phosphorylation of two amino acids. In thymocytes, Ikaros acts as a repressor of the TdT gene. Induction of differentiation of thymocytes with phorbol 12-myristate 13-acetate plus ionomycin results in transcriptional repression of TdT expression. This process has been associated with increased binding of Ikaros to the upstream regulatory element of TdT. Phosphopeptide analysis of in vivo-labeled thymocytes revealed that Ikaros undergoes dephosphorylation during induction of thymocyte differentiation and that dephosphorylation is responsible for increased DNA binding affinity of Ikaros toward the TdT promoter. We propose a model whereby reversible phosphorylation of Ikaros at specific amino acids controls the subcellular localization of Ikaros as well as its ability to regulate TdT expression during thymocyte differentiation.

Tec kinases mediate sustained calcium influx via site-specific tyrosine phosphorylation of the phospholipase Cgamma Src homology 2-Src homology 3 linker.

Tyrosine phosphorylation of phospholipase Cgamma2 (PLCgamma2) is a crucial activation switch that initiates and maintains intracellular calcium mobilization in response to B cell antigen receptor (BCR) engagement. Although members from three distinct families of non-receptor tyrosine kinases can phosphorylate PLCgamma in vitro, the specific kinase(s) controlling BCR-dependent PLCgamma activation in vivo remains unknown. Bruton's tyrosine kinase (Btk)-deficient human B cells exhibit diminished inositol 1,4,5-trisphosphate production and calcium signaling despite a normal inducible level of total PLCgamma2 tyrosine phosphorylation. This suggested that Btk might modify a critical subset of residues essential for PLCgamma2 activity. To evaluate this hypothesis, we generated site-specific phosphotyrosine antibodies recognizing four putative regulatory residues within PLCgamma2. Whereas all four sites were rapidly modified in response to BCR engagement in normal B cells, Btk-deficient B cells exhibited a marked reduction in phosphorylation of the Src homology 2 (SH2)-SH3 linker region sites, Tyr(753) and Tyr(759). Phosphorylation of both sites was restored by expression of Tec, but not Syk, family kinases. In contrast, phosphorylation of the PLCgamma2 carboxyl-terminal sites, Tyr(1197) and Tyr(1217), was unaffected by the absence of functional Btk. Together, these data support a model whereby Btk/Tec kinases control sustained calcium signaling via site-specific phosphorylation of key residues within the PLCgamma2 SH2-SH3 linker.