Electrochemical Evaluation of Stress Corrosion Cracking Susceptibility of Ti-6Al-3Nb-2Zr-1Mo Alloy Welded Joint in Simulated Deep-Sea Environment.

Titanium alloys have high specific strength and excellent corrosion resistance and have been applied in deep-sea engineering fields. However, stress corrosion cracking may become one of the biggest threats to the service safety of a high-strength titanium alloy, as well as its weldment. In this work, stress corrosion cracking of a gas-tungsten-arc-welded Ti-6Al-3Nb-2Zr-1Mo (Ti6321) alloy influenced by the applied potentials in simulated deep-sea and shallow-sea environments was investigated by combining slow strain rate testing with electrochemical measurements. The results showed that the service environment and applied potential have a substantial effect on the stress corrosion cracking behavior of the Ti6321 welded joint. The Ti6321 welded joint exhibited higher stress corrosion susceptibility in a simulated deep-sea environment and at a strong polarization level owing to the diminishing protection of the passive film under passivation inhibition and the enhancement of the hydrogen effect. The fracture of a Ti6321 welded joint in the weld material could be attributed to the softening effect of the thick secondary α within the coarse-grained martensite. The electrochemical evaluation model of stress corrosion cracking susceptibility of a Ti6321 welded joint in a simulated marine environment was established by adding the criterion in the passivation region based on the literature model, and four potential regions corresponding to different stress corrosion cracking mechanisms were classified and discussed. Our study provides useful guidance for the deep-sea engineering applications of Ti6321 alloys and a rapid assessment method of stress corrosion risk.

An eIF3a gene mutation dysregulates myocardium growth with left ventricular noncompaction via the p-ERK1/2 pathway.

Left ventricular noncompaction (LVNC) is a heterogeneous disorder with unclear genetic causes and an unknown mechanism. eIF3a, an important member of the Eukaryotic translation initiation factor 3 (eIF3) family, is involved in multiple biological processes, including cell proliferation and migration during myocardial development, suggesting it could play a role in LVNC development. To investigate the association between a novel variant (c.1145 A- > G) in eIF3a and LVNC, and explore potential mechanisms that could lead to the development of LVNC. A novel eIF3a variant, c.1145 A- > G, was identified by whole-exome sequencing in a familial pedigree with LVNC. Adenovirus vectors containing wild-type eIF3a and the mutated version were constructed and co-infected into H9C2 cells. Cell proliferation, apoptosis, cell migration, and differentiation, as well as phosphorylation of ERK1/2 were studied and were measured by proliferation assays, flow cytometry, real-time PCR and Western blot, respectively. The eIF3a mutation inhibited the proliferation of H9C2 cells, induced apoptosis, promoted cell migration, and inhibited the differentiation of human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs). The effect of the eIF3a mutation may be attributed to a decrease in expression of p-ERK1/2. A novel eIF3a gene mutation disrupted the p-ERK1/2 pathway and caused decreased myocardium proliferation, differentiation, accelerated migration.This finding may provide some insight into the mechanism involved in LVNC development.

A de novo Mutation in the MTUS1 Gene Decreases the Risk of Non-compaction of Ventricular Myocardium via the Rac1/Cdc42 Pathway.

Background: The MTUS1 gene encodes a microtubule-associated protein involved in multiple processes including cell polarity and microtubule balance during myocardial development. Aims: To investigate the association between a de novo c. 2617A->C mutation in MTUS1 (NM_001001924.2) and non-compaction of ventricular myocardium (NVM) and explore the potential mechanisms. Methods: A de novo mutation in MTUS1 was identified for a familial pedigree with NVM. Lentiviral vectors containing MTUS1 wild type or the mutation MTUS1 were constructed and co-infected into HEK-293 cells. MTUS1, Rac1/Cdc42, α-tubulin, α/ß-tubulin, polarity protein (PAR6), and the morphology of daughter cells were measured by real-time PCR, Western blot, and immunofluorescence assays, respectively. Results: The lentiviral vectors were constructed successfully. Immunofluorescence assays revealed the fluorescence intensity of α-tubulin to be decreased and α/ß-tubulin to be increased in the mutation MTUS1 group. The fluorescence intensity of PAR6 was higher and morphology of the daughter cells in the mutation group was different from the wild type group. The phosphorylation of Rac1/Cdc42 in the mutation group was significantly lower than in the wild type group. Conclusions: A de novo mutation in MTUS1 decreased the stability of microtubules and increased cell polarity via the Rac1/Cdc42 pathway, which may partly elucidate the mechanism underlying cellular protection in NVM.