Differential Regulation of Gene Expression of Alveolar Epithelial Cell Markers in Human Lung Adenocarcinoma-Derived A549 Clones

Stem cell therapy appears to be promising for restoring damaged or irreparable lung tissue. However, establishing a simple and reproducible protocol for preparing lung progenitor populations is difficult because the molecular basis for alveolar epithelial cell differentiation is not fully understood. We investigated an in vitro system to analyze the regulatory mechanisms of alveolus-specific gene expression using a human alveolar epithelial type II (ATII) cell line, A549. After cloning A549 subpopulations, each clone was classified into five groups according to cellmorphology andmarker gene expression. Two clones (B7 and H12)were further analyzed. Under serum-free culture conditions, surfactant protein C (SPC), an ATII marker, was upregulated in both H12 and B7. Aquaporin 5 (AQP5), an ATI marker, was upregulated in H12 and significantly induced in B7. When the RAS/MAPK pathway was inhibited, SPC and thyroid transcription factor-1 (TTF-1) expression levels were enhanced. After treatment with dexamethasone (DEX), 8-bromoadenosine 3’5’-cyclic monophosphate (8-Br-cAMP), 3-isobutyl-1-methylxanthine (IBMX), and keratinocyte growth factor (KGF), surfactant protein B and TTF-1 expression levels were enhanced. We found that A549-derived clones have plasticity in gene expression of alveolar epithelial differentiation markers and could be useful in studying ATII maintenance and differentiation

Nanoscale Texture and Microstructure in a NdFeAs(O,F)/IBAD-MgO Superconducting Thin Film with Superior Critical Current Properties

This paper reports the nanoscale texture and microstructure of a high-performance NdFeAs(O,F) superconducting thin film grown by molecular beam epitaxy on a textured MgO/Y2O3/Hastelloy substrate. The NdFeAs(O,F) film forms a highly textured columnar grain structure by epitaxial growth on the MgO template. Although the film contains stacking faults along the ab-plane as well as grain boundaries perpendicular to the ab-plane, good superconducting properties are measured: a critical temperature, T-c, of 46 K and a self-field critical current density, J(c), of 2 x 10(6) A/cm(2) at 4.2 K. Automated crystal orientation mapping by scanning precession electron diffraction in transmission electron microscope is employed to analyze the misorientation angles between adjacent grains in a large ensemble (247 grains), and 99% of the grain boundaries show in-plane misorientation angles (Delta gamma) less than the critical angle theta(c), which satisfies one of the necessary conditions for the high J(c). Comparing the columnar grain size distribution with the mean distance of the flux line lattice, the triple junctions of low-angle grain boundaries are found to be effective pinning centers, even at high temperatures (>= 35 K) and/or low magnetic fields

PITHD1 is essential for male fertilization

The proteasome is a protein-degrading molecular complex that is necessary for protein homeostasis and various biological functions, including cell cycle regulation, signal transduction, and immune response. Proteasome activity is finely regulated by a variety of proteasome-interacting molecules. PITHD1 is a recently described molecule that has a domain putatively capable of interacting with the proteasome. However, it is unknown as to whether PITHD1 can actually bind to proteasomes and what it does in vivo. Here we report that PITHD1 is detected specifically in the spermatids in the testis and the cortical thymic epithelium in the thymus. Interestingly, PITHD1 associates with immunoproteasomes in the testis, but not with thymoproteasomes in the thymus. Mice deficient in PITHD1 exhibit severe male infertility accompanied with morphological abnormalities and impaired motility of spermatozoa. Furthermore, PITHD1 deficiency reduces proteasome activity in the testis and alters the amount of proteins that are important for fertilization capability by the sperm. However, the PITHD1-deficient mice demonstrate no detectable defects in the thymus, including T cell development. Collectively, our results identify PITHD1 as a proteasome-interacting protein that plays a nonredundant role in the male reproductive system

PITHD1 is a proteasome-interacting protein essential for male fertilization

Hiroyuki Kondo, Takafumi Matsumura, Mari Kaneko, Kenichi Inoue, Hidetaka Kosako, Masahito Ikawa, Yousuke Takahama, Izumi Ohigashi, PITHD1 is a proteasome-interacting protein essential for male fertilization, Journal of Biological Chemistry, Volume 295, Issue 6, 2020, Pages 1658-1672, ISSN 0021-9258, https://doi.org/10.1074/jbc.RA119.011144

High Jc_{c} and low anisotropy of hydrogen doped NdFeAsO superconducting thin film

The recent realisations of hydrogen doped LnFeAsO (Ln = Nd and Sm) superconducting epitaxial thin films call for further investigation of their structural and electrical transport properties. Here, we report on the microstructure of a NdFeAs(O,H) epitaxial thin film and its temperature, field, and orientation dependencies of the resistivity and the critical current density J$_{c}$. The superconducting transition temperature T$_{c}$ is comparable to NdFeAs(O,F). Transmission electron microscopy investigation supported that hydrogen is homogenously substituted for oxygen. A high self-field J$_{c}$ of over 10 MA/cm$^{2}$ was recorded at 5 K, which is likely to be caused by a short London penetration depth. The anisotropic Ginzburg–Landau scaling for the angle dependence of J$_{c}$ yielded temperature-dependent scaling parameters γ$_{J}$ that decreased from 1.6 at 30 K to 1.3 at 5 K. This is opposite to the behaviour of NdFeAs(O,F). Additionally, γ$_{J}$ of NdFeAs(O,H) is smaller than that of NdFeAs(O,F). Our results indicate that heavily electron doping by means of hydrogen substitution for oxygen in LnFeAsO is highly beneficial for achieving high J$_{c}$ with low anisotropy without compromising T$_{c}$, which is favourable for high-field magnet applications

Establishment and Evaluation of a New Chemiluminescent Enzyme Immunoassay for Carcinoembryonic Antigen Adapted to the Fully Automated ACCESS® System

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