SUMMARY
Anchorage of tissue cells to their physical environment is an obligate requirement for survival which is lost in mature hematopoietic and in transformed epithelial cells. Here we find that a lymphocyte lineage-restricted transcription factor, Aiolos, is frequently expressed in lung cancers and predicts markedly reduced patient survival. Aiolos decreases expression of a large set of adhesion-related genes, disrupting cell-cell and cell-matrix interactions. Aiolos also reconfigures chromatin structure within the SHC1 gene, causing isoform-specific silencing of the anchorage reporter p66Shc and blocking anoikis in vitro and in vivo. In lung cancer tissues and single cells, p66Shc expression inversely correlates with that of Aiolos. Together, these findings suggest that Aiolos functions as an epigenetic driver of lymphocyte mimicry in metastatic epithelial cancers.
Reduced graphene oxide (rGO) aerogels were fabricated under mild conditions from an aqueous solution of graphene oxide (GO) using a one-step method which included the reduction of GO by mercaptoacetic acid and the self-assembling of rGO. The reduction of GO was confirmed with Fourier transform infrared spectroscopy, Raman spectroscopy, thermogravimetric analysis and X-ray diffraction analysis. The elemental compositions of the GO and rGO aerogels were determined with X-ray photoelectron spectroscopy. The effect of different mercapto compounds on the assembly of rGO was investigated and the results showed that rGO can also accomplish self-assembling in water when mercaptoacetic acid and mercaptoethanol were used. The porous structure of the rGO aerogels was observed with scanning electron microscopy and their porosities were in the range of 90-96% when mercaptoacetic acid was used as the reductant. The high porosity gives the rGO aerogels excellent absorption abilities for metal ions.
A simple
method to fabricate Bi nanoparticles by using redox reactions
between sodium borohydride and ammonium bismuth citrate in the presence
of soluble starch in water phase was developed. The results show that
soluble starch is better than PVP in stabilizing Bi nanoparticles.
The as-prepared Bi nanoparticles were characterized by Fourier transform
infrared spectroscopy, transmission electron microscopy, energy-dispersive
X-ray, and powder X-ray diffraction. The catalytic performance of
the Bi nanoparticles for the reduction of 4-nitrophenol (4-NP) to
4-aminophenol (4-AP) in the presence of sodium borohydride was studied.
The effects of sodium borohydride concentration, initial 4-NP concentration,
catalyst dose, and reduction temperature were also investigated.
Candida albicans RCH1 (regulator of Ca(2+) homoeostasis 1) encodes a protein of ten TM (transmembrane) domains, homologous with human SLC10A7 (solute carrier family 10 member 7), and Rch1p localizes in the plasma membrane. Deletion of RCH1 confers hypersensitivity to high concentrations of extracellular Ca(2+) and tolerance to azoles and Li(+), which phenocopies the deletion of CaPMC1 (C. albicans PMC1) encoding the vacuolar Ca(2+) pump. Additive to CaPMC1 mutation, lack of RCH1 alone shows an increase in Ca(2+) sensitivity, Ca(2+) uptake and cytosolic Ca(2+) level. The Ca(2+) hypersensitivity is abolished by cyclosporin A and magnesium. In addition, deletion of RCH1 elevates the expression of CaUTR2 (C. albicans UTR2), a downstream target of the Ca(2+)/calcineurin signalling. Mutational and functional analysis indicates that the Rch1p TM8 domain, but not the TM9 and TM10 domains, are required for its protein stability, cellular functions and subcellular localization. Therefore Rch1p is a novel regulator of cytosolic Ca(2+) homoeostasis, which expands the functional spectrum of the vertebrate SLC10 family.
The target of rapamycin complex 1 (TORC1) is the central controller of growth in eukaryotic cells. As one of the downstream targets of TORC1, the protein kinase ScSch9p plays multiple roles in stress resistance, longevity and nutrient sensing in Saccharomyces cerevisiae. In this study, we demonstrate that Candida albicans cells with CaSCH9 deleted have reduced cell sizes and show a delayed log-phase growth. In addition, deletion of CaSCH9 renders C. albicans cells sensitive to rapamycin, caffeine and sodium dodecyl sulfate. Similar to ScSCH9, deletion of CaSCH9 also causes C. albicans cells to become sensitive to cations, but does not lead to a defect in the utilization of galactose. Furthermore, deletion of CaSCH9 affects the filamentation of C. albicans cells and attenuates the virulence in a mouse mode of systemic candidiasis. Therefore, CaSch9p is an important regulator for the cell growth, filamentation and virulence of this human fungal pathogen.
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