僻地で羊膜移植術を施行した再発翼状片の１例

京都府立医科大学附属北部医療センター眼科京都府立医科大学組織バンク/ アイバンクDepartment of ophthalmology, North Medical Center Kyoto Prefectural University of MedicineKyoto Prefectural University of Medicine, tissue bank / eye bank難治性眼表面疾患に対する羊膜移植の保険収載を受け、僻地の医療施設において羊膜移植を導入し、移植を行った再発翼状片の１例について報告する。症例は70 歳女性、7 年前に右翼状片切除術を受けたが、初回手術8 か月後に再発を認めた。羊膜移植施設認定を受け2018 年8 月に羊膜移植併用、右翼状片切除術を施行した。術後３か月において再発なく経過しており、僻地においても安全に問題なく羊膜移植を行うことが可能であった

Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit

N-methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors (iGluRs) that mediate the majority of fast excitatory synaptic transmission in the mammalian brain. One of the hallmarks for the function of NMDA receptors is that their ion channel activity is allosterically regulated by binding of modulator compounds to the extracellular amino-terminal domain (ATD) distinct from the L-glutamate-binding domain. The molecular basis for the ATD-mediated allosteric regulation has been enigmatic because of a complete lack of structural information on NMDA receptor ATDs. Here, we report the crystal structures of ATD from the NR2B NMDA receptor subunit in the zinc-free and zinc-bound states. The structures reveal the overall clamshell-like architecture distinct from the non-NMDA receptor ATDs and molecular determinants for the zinc-binding site, ion-binding sites, and the architecture of the putative phenylethanolamine-binding site

Prevalence of HR-HPV infection, and univariate and multivariate logistic regression analyses of the association between potential predictors and HR-HPV infection in sexually active respondents (n = 770).

<p>CT = Chlamydia trachomatis; STD = sexually transmitted disease; AOR = Adjusted odds ratio</p><p>*Wilcoxon rank-sum test (for trend)</p><p>†Chi-square test</p><p>Prevalence of HR-HPV infection, and univariate and multivariate logistic regression analyses of the association between potential predictors and HR-HPV infection in sexually active respondents (n = 770).</p

ロウジン ビョウイン カンジャ ノ ニュウイン マエ カイゴ ジョウキョウ ノ ケイネンテキ ヘンカ

1998年から1995年の8年間に老人病院に新規に入院した患者の家族を対象として、質問紙法を用いて、入院前の患者の状態と介護状況の調査をした。入院前の患者の状態及び介護者のプロフィールには明らかな変化はみられなかったが、在宅介護を行う家族は減少していた。 ホームヘルパー、デイサービス、ショートステイの周知度と利用率は上昇したが、周知度の高さに比べ利用率は低かった。在宅福祉サービスの利用率が増加した近年に介護負担感とサービス利用の有無に関連がみられるようになり、患者の移動に対する介護負担感は、各サービス共、利用した介護者が利用しなかったものより高かった。痴呆の介護負担感についてはデイサービス、ショートステイを利用した介護者の方が高かったが、ホームヘルパーについては利用した介護者の方が低かった。在宅介護期間についてはデイサービス、ショートステイを利用した方が長かった

Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors

Since it was discovered that the anti-hypertensive agent ifenprodil has neuroprotective activity through its effects on NMDA (N-methyl-D-aspartate) receptors, a determined effort has been made to understand the mechanism of action and to develop improved therapeutic compounds on the basis of this knowledge. Neurotransmission mediated by NMDA receptors is essential for basic brain development and function. These receptors form heteromeric ion channels and become activated after concurrent binding of glycine and glutamate to the GluN1 and GluN2 subunits, respectively. A functional hallmark of NMDA receptors is that their ion-channel activity is allosterically regulated by binding of small compounds to the amino-terminal domain (ATD) in a subtype-specific manner. Ifenprodil and related phenylethanolamine compounds, which specifically inhibit GluN1 and GluN2B NMDA receptors, have been intensely studied for their potential use in the treatment of various neurological disorders and diseases, including depression, Alzheimer's disease and Parkinson's disease. Despite considerable enthusiasm, mechanisms underlying the recognition of phenylethanolamines and ATD-mediated allosteric inhibition remain limited owing to a lack of structural information. Here we report that the GluN1 and GluN2B ATDs form a heterodimer and that phenylethanolamine binds at the interface between GluN1 and GluN2B, rather than within the GluN2B cleft. The crystal structure of the heterodimer formed between the GluN1b ATD from Xenopus laevis and the GluN2B ATD from Rattus norvegicus shows a highly distinct pattern of subunit arrangement that is different from the arrangements observed in homodimeric non-NMDA receptors and reveals the molecular determinants for phenylethanolamine binding. Restriction of domain movement in the bi-lobed structure of the GluN2B ATD, by engineering of an inter-subunit disulphide bond, markedly decreases sensitivity to ifenprodil, indicating that conformational freedom in the GluN2B ATD is essential for ifenprodil-mediated allosteric inhibition of NMDA receptors. These findings pave the way for improving the design of subtype-specific compounds with therapeutic value for neurological disorders and diseases