The perception of life and death in patients with end-of-life stage cancer: A systematic review of qualitative research.

Purpose: This study aims to clarify the perceptions on life and death among patients with the end-of-life stage cancer through a systematic review.

Methods: The search strategy combined MeSH terminology with free text searches, and was applied to the PubMed, CINAHL, Embase, and ICHUSHI (Japan Medical Abstracts Society) databases covering from 2010 to 5/2022. To ensure the quality of the research included, the Critical Appraisal Skills Program Qualitative Studies Checklist was used.

Live birth by cesarean section after rupture of uterine cornua in simultaneous corneal and intrauterine pregnancies.

A patient became pregnant by in vitro fertilization and embryo transfer (IVF-ET). She had a history of laparoscopic bilateral salpingectomy and enucleation of a left ovarian tumor due to bilateral hydrosalpinx and left endometriotic cyst in primary infertility. She noticed abdominal pain and visited the nearby general hospital by ambulance (gestational age 6 weeks and 1 day).

Inducer-dependent nuclear localization of a Zn(II)(2)Cys(6) transcriptional activator, AmyR, in Aspergillus nidulans.

AmyR is a Zn(II)(2)Cys(6) transcriptional activator that regulates expression of the amylolytic genes in Aspergillus species. Subcellular localization studies of GFP-fused AmyR in A. nidulans revealed that the fusion protein preferentially localized to the nucleus in response to isomaltose, the physiological inducer of the amylolytic genes.

Novel promoter sequence required for inductive expression of the Aspergillus nidulans endoglucanase gene eglA.

Expression of the eglA gene, encoding for a major endoglucanse EG A in Aspergillus nidulans, is induced by cellulose and cellobiose, but not by xylose. This suggests that induction is independent of XlnR, a transcriptional activator of xylanolytic and cellulolytic genes in Aspergillus. Mutational analysis of the eglA promoter was performed to identify the novel cis-element responsible for XlnR-independent induction.

The region in a subunit of the Aspergillus CCAAT-binding protein similar to the HAP4p-recruiting domain of Saccharomyces cerevisiae Hap5p is not essential for transcriptional enhancement.

The CCAAT-binding complex in Aspergillus species, known as the Hap complex, consists of at least three subunits, HapB, HapC, and HapE. Each Hap subunit contains an evolutionarily conserved core domain. In this study, a series of the truncated gene, which encodes the HapE subunit of Aspergillus oryzae, was constructed to survey the regions essential for the transcriptional enhancement of fungal genes.

A second pectin lyase gene (pel2) from Aspergillus oryzae KBN616: its sequence analysis and overexpression, and characterization of the gene products.

A second pectin lyase gene, designated pel2, was isolated from a shoyu koji mold Aspergillus oryzae KBN616 and characterized. The structural gene comprised 1306 bp with three introns. The ORF encoded 375 amino acids with a signal peptide of 19 amino acids.

Isolation and transcriptional analysis of novel tetrachloroethene reductive dehalogenase gene from Desulfitobacterium sp. strain KBC1.

Strain KBC1, an anaerobic bacterium, that dechlorinates tetrachloroethene (PCE) to trichloroethene was isolated. This strain also dechlorinated high concentrations of PCE at a temperature range of 10 to 40 degrees C and showed high oxygen tolerance. Based on the 16S rRNA gene sequence analysis, this microorganism was identified as a species of the genus Desulfitobacterium.

Nuclear translocation of the heterotrimeric CCAAT binding factor of Aspergillus oryzae is dependent on two redundant localising signals in a single subunit.

The CCAAT-binding complex in the Aspergillus species, also known as the Hap complex, consists of at least three subunits, namely HapB, HapC and HapE. Each Hap subunit contains an evolutionary conserved core domain. Recently, we have found that the HapC and HapE subunits do not carry a nuclear localisation signal.

Discovery of glpC, an organic solvent tolerance-related gene in Escherichia coli, using gene expression profiles from DNA microarrays.

Gene expression profiles were collected from Escherichia coli strains (OST3410, TK33, and TK31) before and after exposure to organic solvents, and the six genes that showed higher gene expression were selected. Among these genes, glpC encoding the anaerobic glycerol-3-phosphate dehydrogenase subunit C remarkably increased the organic solvent tolerance.

Convenient and sensitive evaluation of a superoxide anion-generating reagent methyl viologen by Escherichia coli harboring a soxS'::gfp reporter plasmid.

We constructed a reporter system to detect a superoxide-generating methyl viologen using SoxRS of Escherichia coli and GFP of Aequorea victoria. E. coli carrying this plasmid exhibited strong fluorescence when grown in the presence of a superoxide-generating reagent methyl viologen.

Mode of AmyR binding to the CGGN8AGG sequence in the Aspergillus oryzae taaG2 promoter.

AmyR is a transcriptional activator in Aspergillus spp. necessary for induction of the amylolytic enzyme genes. It recognizes 5'-CGGN8CGG-3' conserved in a number of the amylolytic gene promoters, and in addition 5'-CGGAAATTTAA-3' in the A.

A single subunit of a heterotrimeric CCAAT-binding complex carries a nuclear localization signal: piggy back transport of the pre-assembled complex to the nucleus.

An unresolved question concerns the nuclear localization of the heterotrimeric CCAAT-binding complex, which is evolutionarily conserved in eukaryotic organisms including fungi, plants and mammals. All three subunits are necessary for DNA binding. In the filamentous fungus Aspergillus nidulans the corresponding complex was designated AnCF (A.

Transcriptional analysis of the ostA/imp gene involved in organic solvent sensitivity in Escherichia coli.

Transcriptional initiation sites of the ostA gene involved in organic solvent sensitivity in Escherichia coli were found by primer extension analysis. Two transcriptional initiation sites were newly identified at -133 and -48 nucleotides from the initiation codon of ostA, but the previously reported sigmaE-dependent one at -227 could not be detected. No heat-inducible expression of ostA was observed by Northern blotting analysis, indicating that the contribution of sigmaE-dependent transcription was very small if any.

Isolation of GnafC, a polysaccharide constituent of Gnaphalium affine, and synergistic effects of GnafC and ascorbate on the phenotypic expression of osteoblastic MC3T3-E1 cells.

After screening extensively factors in plant extracts that increase alkaline phosphatase activity, an osteoblastic differentiation marker protein in mouse calvarial osteoblast MC3T3-E1 cells, GnafC derived from Gnaphalium affine, was found to significantly enhance the alkaline phosphatase (ALPase) activity in a synergistic manner with ascorbate. GnafC was a polysaccharaide with an approximate molecular mass of 10,000 and comprised mannose, xylose, arabinose, galactose and glucose in a molar ratio of 1:2:4.3:2.

Functional roles of the tissue inhibitor of metalloproteinase 3 (TIMP-3) during ascorbate-induced differentiation of osteoblastic MC3T3-E1 cells.

The tissue inhibitor of the metalloproteinase-3 (TIMP-3) gene was isolated as a gene involved in the process of ascorbate-induced differentiation of mouse MC3T3-E1 cells by the differential display method. The functional roles of TIMP-3 were characterized by establishing stable cell lines, which constitutively expressed the TIMP-3 gene. The TIMP-3 transfectants produced type I collagen at the same level as that of normal cells in response to ascorbic acid 2-phosphate (AscP).

Upregulation of promoter activity of the Aspergillus oryzae xylanase gene by site-directed mutagenesis.

In Aspergillus oryzae, inductive expression of the xynF1 gene is mediated by a transcriptional activator, AoXlnR. Promoter activity of the xynF1 gene, monitored by beta-galactosidase activity, was successfully upregulated by mutating two non-canonical AoXlnR binding sequences to what is thought to be the strongest sequence. Transformants carrying three canonical binding sequences in the promoter region produced enzyme 2.

Structural features of the glycogen branching enzyme encoding genes from aspergilli.

A maltose binding protein, p78, was purified to homogeneity from Aspergillus nidulans by a single column chromatography step on cross-linked amylose. The partial amino acid sequence was highly homologous to the glycogen branching enzymes (GBEs) of human and yeast, and p78 did show branching enzyme activity. The genomic gene and its cDNA encoding GBE (p78) were isolated from the A.

Characterization of AnRP-mediated negative regulation of the xylanase gene, cgxA, from Chaetomium gracile in Aspergillus nidulans.

Aim: In vivo regulatory features of AnRP, a repressor for the cgxA gene, were characterized.

Methods And Results: Titration of AnRP by introducing multiple copies of its specific binding sequence 'TTGACAAAT' into an Aspergillus nidulans strain containing the Chaetomium gracile cgxA gene enhanced the cgxA gene expression. AnRP functions independently of and cooperatively with CreA to modulate the cgxA gene expression.

Regulation of the amylolytic and (hemi-)cellulolytic genes in aspergilli.

Filamentous fungi produce high levels of polysaccharide-degrading enzymes and are frequently used for the production of industrial enzymes. Because of the high secretory capacity for enzymes, filamentous fungi are effective hosts for the production of foreign proteins. Genetic studies with Aspergillus nidulans have shown pathway-specific regulatory systems that control a set of genes that must be expressed to catabolize particular substrates.

Isomaltose formed by alpha-glucosidases triggers amylase induction in Aspergillus nidulans.

Among various alpha-glucobioses examined, isomaltose was the most effective inducer for amylase synthesis in Aspergillus nidulans. Amylase induction by maltose was completely inhibited by addition of castanospermine or cycloheximide, while induction by isomaltose was not affected by the inhibitors, suggesting that amylase induction by maltose requires inducible alpha-glucosidases. Disruption of the alpha-glucosidase A gene ( agdA), the alpha-glucosidase B gene ( agdB), or both genes did not abolish maltose-dependent induction, although amylase production induced by maltose decreased about 2-fold in the agdA/ agdB double disruptant, compared with that in the agdB disruptant at all concentrations tested.

Transcriptional activator, AoXlnR, mediates cellulose-inductive expression of the xylanolytic and cellulolytic genes in Aspergillus oryzae.

AoXlnR was isolated as a transcriptional activator of the major xylanase gene, xynF1, in Aspergillus oryzae. To investigate the spectrum of genes under the control of AoXlnR, expression of the xylanolytic and cellulolytic genes in an A. oryzae wild type strain, an AoxlnR disruptant and an AoXlnR overexpressed strain was analyzed by Northern blotting.

Isolation of genes encoding novel transcription factors which interact with the Hap complex from Aspergillus species.

The Saccharomyces cerevisiae CCAAT-binding factor is composed of four subunits Hap2p, Hap3p, Hap4p and Hap5p. Three subunits, Hap2/3/5p, are required for DNA-binding and Hap4p is involved in transcriptional activation. Although homologues of Hap2/3/5p (in the case of Aspergillus nidulans; HapB/C/E, respectively) were found in many eukaryotes, no Hap4p homologues have been found except for the other yeast, Kluyveromyces lactis.

Upward shift of the pH optimum of Acremonium ascorbate oxidase.

A gene encoding a thermostable Acremonium ascorbate oxidase (ASOM) was randomly mutated to generate mutant enzymes with altered pH optima. One of the mutants, which exhibited a significantly higher activity in the pH range 4.5-7 compared to ASOM, had a Gln183Arg substitution in the region corresponding to SBR1, one of the substrate binding regions of the zucchini enzyme.

Novel alpha-glucosidase from Aspergillus nidulans with strong transglycosylation activity.

Aspergillus nidulans possessed an alpha-glucosidase with strong transglycosylation activity. The enzyme, designated alpha-glucosidase B (AgdB), was purified and characterized. AgdB was a heterodimeric protein comprising 74- and 55-kDa subunits and catalyzed hydrolysis of maltose along with formation of isomaltose and panose.

A quantity control mechanism regulating levels of the HapE subunit of the Hap complex in Aspergillus nidulans: no accumulation of HapE in hapC deletion mutants.

The Aspergillus nidulans CCAAT-binding complex (Hap complex) consists of at least three subunits, HapB, HapC and HapE. To investigate the quantity control mechanisms of the subunits during assembly of the Hap complex, reconstitution studies with the recombinant subunits and extracts prepared from the respective hap subunit deletion mutants were carried out. Furthermore, Western blot analysis of the Hap subunits and Northern blot analysis of the hap genes with the respective deletion mutants were also performed.