Placenta Percreta Progression to Resistance Against Uterine Artery Embolization and Penetration Into the Bladder.

A 31-year-old female sought termination of pregnancy due to a fetal body stalk anomaly diagnosed at 18 weeks of gestation. Despite an anterior placenta previa, successful vaginal delivery occurred. However, placental adhesion over a previous cesarean scar occurred, and part of the placenta could not be removed. Immediate postpartum bleeding prompted imaging studies, revealing extravasation from adherent placental remnants. Uterine artery embolization (UAE) provided initial hemostasis, but recurrent bleeding necessitated re-embolization. Although conservative treatment was initially pursued, significant hematuria prompted reevaluation, revealing extensive uterine wall and bladder penetration. Surgical intervention with total hysterectomy and partial bladder resection was performed, leading to the successful recovery of bladder function following surgical repair. While this case achieved a positive outcome, there is a potential for permanent urinary dysfunction if lesions are more extensive. While achieving a conservative cure is ideal, it is essential to assess the timing for opting for surgical intervention.

Lectin Bead Array in a Single Tip Facilitates Fully Automatic Glycoprotein Profiling.

A quantitative description of glyco-alteration/differences in diseases can lead to the development of a diagnostic agent for use in vitro to monitor the degree of change in target glycoproteins. Analytical systems have been developed along with the progress of omics-oriented technologies. For clinical implementation, their full automation is required with an apparatus that is simple to operate. Here, we report an automatic analysis system for quantitative characterization of glyco-alteration/differences that depends on the unique strategy of "bead arrays in a single tip." The alternative lectin array can obtain a minimum characterization of the glycan profile for nanogram quantities of an endogenous glycoprotein. A simple autopipetting robot produces the precise chemiluminescence detection of glycan-lectin interactions with a wide dynamic range that is superior to fluorescence-based lectin arrays. The tip-based array format enables automatic glycan profiling from sample pretreatment to detection with low variation and linear detection, which may facilitate the use of this lectin array in clinical practice.

A useful strategy to construct DNA polymerases with different properties by using genetic resources from environmental DNA.

DNA polymerases synthesize new DNA strands according to the template DNA, using deoxynucleotide triphosphates during DNA replication and repair, and are essential to maintain genome integrity in DNA metabolism. In addition, these enzymes are widely used for genetic engineering techniques, including dideoxy-sequencing, PCR, DNA labeling, mutagenesis, and other in vitro experiments. Thermostable DNA polymerases are especially useful for PCR and cycle-sequencing. We propose a powerful strategy using environmental DNA as a genetic resource to investigate the structure-function relationships of the family B DNA polymerases. The region corresponding to the active center of the DNA polymerizing reaction in the structural gene of P. furiosus DNA polymerase I (PolBI) was substituted by PCR fragments amplified from DNAs within soil samples from various locations in Japan. The chimeric pol genes were constructed within the PolBI expression plasmid. The chimeric enzymes thus produced revealed DNA polymerase activities with different properties.

Development of an automation system for single nucleotide polymorphisms genotyping using bio-strand, a new three-dimensional microarray.

Previously, we developed a novel three-dimensional microarray system called Bio-Strand, which may be used in various applications including single nucleotide polymorphisms genotyping. In Bio-Strand, samples for detection are immobilized on a one-dimensional thread, which is wound around a cylinder-shaped core to form a three-dimensional thread-and-core structure. The thread-and-core structure is then inserted into a plastic pipette tip, where hybridization and detection are performed. In this study, we have developed an automation system, NIAGALA Bio-Station SDx, which enables automated hybridization and detection during the genotyping procedure using Bio-Strand. Using this system, we have performed the single nucleotide polymorphism (SNP) genotyping of CYP2C, one of the important human cytochrome P450 genes and the results were completely consistent with the genotyping results determined by the TaqMan method.

Novel antimutagenic factors derived from the edible mushroom Agrocybe cylindracea.

Studies have shown that certain foods contain compounds with antigenotoxic activities. Here, we ask if dried powders and/or extracts from three edible mushrooms, Agrocybe cylindracea, Lentinula edodes and Pleurotus ostreatus, have a mitigating effect on genotoxicity. We used two in vivo assays: the Drosophila DNA repair test and the Drosophila wing spot test (also known as SMART) which measures somatic mutation and recombination. Eight carcinogens were tested with the mushroom powders: 2-AAF, aflatoxin B1, DMBA, IQ, MeIQx, MNU NDMA, and 4NQO. We found that A. cylindracea and P. ostreatus powders can suppress DNA damage induced by each of the mutagens we tested. In contrast, L. edodes has an inhibitory effect on DNA damage induced by only a sub-set of mutagens, namely aflatoxin B1, NDMA, MNU and 4NQO. In addition, A. cylindracea extracts were able to suppress somatic cell mutation induced by aflatoxin B1, MMC, MNU, NDMA, NMOR and 4NQO. These results suggest that Agrocybe genus mushrooms contain factors with antigenotoxic activity, including anti-recombinogenic activity. Furthermore, the antigenotoxic activity of A. cylindracea powder can be extracted in water but not in ethyl acetate or methanol, and is sensitive to heat treatment. The data suggest that there is a novel antigenotoxic factor(s) in A. cylindracea, possibly in the form of a peptide or protein.