鈍的腎損傷の画像診断

18名の鈍的腎損傷の患者における画像診断法の臨床的意義を検討した.患者は11名がminor injuryで, 7名がmajor injuryであった.このうち14名が保存的治療を, 4名が手術的治療を受けた.静脈性腎盂造影は健側腎の存在が把握できるために有用であるが, しばしば損傷の範囲が不確かなことが多く, これは過大評価が多く, 過小評価が稀な傾向を示した.CTエックス線検査は損傷の範囲, 腎周囲血腫および併発する後腹膜や腹部外傷が, 静脈性腎盂造影に比べ明らかに正確に診断された.血管造影は動脈性出血の部位を同定するのに有用であったRadiographic evaluation was performed on 18 patients with blunt renal trauma. Of 18 patients 11 had minor injury. Four of 11 patients with minor injury had a normal intravenous pyelogram (IVP), and other 7 were confirmed to have minor renal injury by computed tomographic (CT) scan. Seven patients had major injury. Six patients were diagnosed by both IVP and CT, and five by angiography. CT scan was reliable in major injury and had the high staging accuracy. Angiography was useful in specific patients. Therefore, we conclude that IVP or CT scan should be performed as the initial evaluation, and CT scan or angiography might be used as the second examination in selected patients

FIGNL1 AAA+ ATPase remodels RAD51 and DMC1 filaments in pre-meiotic DNA replication and meiotic recombination

Ito M., Furukohri A., Matsuzaki K., et al. FIGNL1 AAA+ ATPase remodels RAD51 and DMC1 filaments in pre-meiotic DNA replication and meiotic recombination. Nature Communications 14, 6857 (2023); https://doi.org/10.1038/s41467-023-42576-w.The formation of RAD51/DMC1 filaments on single-stranded (ss)DNAs essential for homology search and strand exchange in DNA double-strand break (DSB) repair is tightly regulated. FIGNL1 AAA+++ ATPase controls RAD51-mediated recombination in human cells. However, its role in gametogenesis remains unsolved. Here, we characterized a germ line-specific conditional knockout (cKO) mouse of FIGNL1. Fignl1 cKO male mice showed defective chromosome synapsis and impaired meiotic DSB repair with the accumulation of RAD51/DMC1 on meiotic chromosomes, supporting a positive role of FIGNL1 in homologous recombination at a post-assembly stage of RAD51/DMC1 filaments. Fignl1 cKO spermatocytes also accumulate RAD51/DMC1 on chromosomes in pre-meiotic S-phase. These RAD51/DMC1 assemblies are independent of meiotic DSB formation. We also showed that purified FIGNL1 dismantles RAD51 filament on double-stranded (ds)DNA as well as ssDNA. These results suggest an additional role of FIGNL1 in limiting the non-productive assembly of RAD51/DMC1 on native dsDNAs during pre-meiotic S-phase and meiotic prophase I

トクシマ シミン ビョウイン ダイキボ ビョウイン ニオケル ソシキテキ Safety Management

Numerous medical errors have been reported on mass media recently. It is a regret that people have become less confident in medicine and have a great deal of skepticism in medical service. Medical profession is now committing to do everything possible to remove their skepticism and restore the confidence in medicine. However, increasing complexity in medical technologies and diversified medical services have made it difficult to eradicate medical errors completely. Nevertheless, we must do everything possible to reduce medical mistakes to an acceptable level. This can be only achieved by the all-out effort of the entire hospital staffs, not by the vigilance of the individual doctor, nurse or technician. We have to face a challenge to improve patient safety and build safer system by the joint effort of all the members of the hospital staffs. We have just initiated the systematic safety programs for the patients, though there are still many problems remaining to be solved. We documented and discussed our concept of informed consent at Tokushima Municipal Hospital, how it is practiced in our daily medical service

Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy.

A detailed analysis of the NMR spectra of amyloid-β (Aβ) peptide revealed a decrease in signal intensity at higher temperature, due to a reversible conformational change of the molecule. Although peak intensity did not depend on peptide concentrations, the intensity in the region from D23 to A30 depended significantly on temperature. During the early stages of Aβ aggregation, each molecule might adopt transiently a turn conformation at around D23-A30, which converts mutually with a random coil. Stabilization of a turn by further conformational change and/or molecular association would lead to the formation of a "nucleus" for amyloid fibrils

Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement.

The most common isoforms of amyloid-β (Aβ) proteins are composed of 40 or 42 amino acid residues. While Aβ-(1-40) is the predominant species, Aβ-(1-42) is more fibrillogenic and neurotoxic, suggesting that Aβ-(1-42) plays a critical role in the initiation of amyloid fibril formation. We investigated the mechanisms by which soluble Aβ-(1-40) associates with preformed Aβ-(1-42) seeds. A paramagnetic relaxation enhancement analysis showed that the Aβ-(1-40) monomer and Aβ-(1-42) seed interact via their C-terminal region in a parallel fashion, and the N-terminal part does not to contribute to the interaction. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: A beta-(1-40) and A beta-(1-42)bind by fluorescence technology (View interaction) A beta-(1-42) and A beta-(1-40)bind by nuclear magnetic resonance (View interaction)