The Expression and Localization of N-Myc Downstream-Regulated Gene 1 in Human Trophoblasts

The protein N-Myc downstream-regulated gene 1 (NDRG1) is implicated in the regulation of cell proliferation, differentiation, and cellular stress response. NDRG1 is expressed in primary human trophoblasts, where it promotes cell viability and resistance to hypoxic injury. The mechanism of action of NDRG1 remains unknown. To gain further insight into the intracellular action of NDRG1, we analyzed the expression pattern and cellular localization of endogenous NDRG1 and transfected Myc-tagged NDRG1 in human trophoblasts exposed to diverse injuries. In standard conditions, NDRG1 was diffusely expressed in the cytoplasm at a low level. Hypoxia or the hypoxia mimetic cobalt chloride, but not serum deprivation, ultraviolet (UV) light, or ionizing radiation, induced the expression of NDRG1 in human trophoblasts and the redistribution of NDRG1 into the nucleus and cytoplasmic membranes associated with the endoplasmic reticulum (ER) and microtubules. Mutation of the phosphopantetheine attachment site (PPAS) within NDRG1 abrogated this pattern of redistribution. Our results shed new light on the impact of cell injury on NDRG1 expression patterns, and suggest that the PPAS domain plays a key role in NDRG1's subcellular distribution. © 2013 Shi et al

NAKANO_Biomaterials

Gene expression, PIV, Cell alignment dat

R_and_A_dataset_NAKANO

Mechanical property, BMD, Bone matrix micro-arrangement data of control and RA bones

NAKANO_Biomaterials

Gene expression, PIV, Cell alignment dat

R_and_A_dataset_NAKANO

Mechanical property, BMD, Bone matrix micro-arrangement data of control and RA bones.THIS DATASET IS ARCHIVED AT DANS/EASY, BUT NOT ACCESSIBLE HERE. TO VIEW A LIST OF FILES AND ACCESS THE FILES IN THIS DATASET CLICK ON THE DOI-LINK ABOV

Development of TiNbTaZrMo bio-high entropy alloy (BioHEA) super-solid solution by selective laser melting, and its improved mechanical property and biocompatibility

BioHEAs, specifically designed high entropy alloy (HEA) systems for biomedical applications, represent a new era for biometals. However, recent challenges are (1) the poor shape customizability, and (2) the inevitable severe segregation due to the intrinsic fact that HEA is an ultra-multicomponent alloy system. To achieve shape customization and suppression of elemental segregation simultaneously, we used an extremely high cooling rate (similar to 10(7) K/s) of the selective laser melting (SLM) process. We, for the first time, developed pre-alloyed Ti1.4Nb0.6Ta0.6Zr1.4Mo0.6 BioHEA powders and SLM-built parts with low porosity, customizable shape, excellent yield stress, and good biocompatibility. The SLM-built specimens showed drastically suppressed elemental segregation compared to the cast counterpart, representing realization of a super-solid solution. As a result, the 0.2% proof stress reached 1690 +/- 78 MPa, which is significantly higher than that of cast Ti1.4Nb0.6Ta0.6Zr1.4Mo0.6 (1140 MPa). The SLM-built Ti1.4Nb0.6Ta0.6Zr1.4Mo0.6 BioHEA is promising as a next-generation metallic material for biomedical applications. (C) 2020 Acta Materialia Inc. Published by Elsevier Ltd.11Nsciescopu

Improvement of Production and Isolation of Human Neuraminidase-1 in Cellulo Crystals

In cellulo crystallization is a developing technique to provide crystals for protein structure determination, particularly for proteins that are difficult to prepare by in vitro crystallization. This method has a key advantage: It requires neither a protein purification step nor a crystallization step. However, there is still no systematic strategy for improving the technique of in cellulo crystallization because the process occurs spontaneously. Here we report a protocol to produce and extract in cellulo crystals of human lysosomal neuraminidase-1 (NEU1) in human cultured cells. Overexpression of NEU1 protein by the retransfection of cells pretransfected with neu1-overexpressing plasmid improved the efficiency of NEU1 crystallization. Microscopic analysis revealed that NEU1 proteins were not crystallized in the lysosome but in the endoplasmic reticulum (ER). Screening of the buffer conditions used to extract crystals from cells further improved the crystal yield. The optimal pH was 7.0, which corresponds to the pH in the ER. Use of a high-yield flask with a large surface area also yielded more crystals. These optimizations enabled us to execute a serial femtosecond crystallography experiment with a sufficient number of crystals to generate a complete data set. Optimization of the in cellulo crystallization method was thus shown to be possible.Accepted Author ManuscriptBN/Arjen Jakobi La