ユーモア ヒョウシュツ ガ ソーシャル サポート オヨビ ヒョウシュツシャ ノ セイシンテキ ケンコウ ニ アタエル エイキョウ : ユーモア ノ ケイタイ ニ チャクモク シテ

The purpose of this research was to examine the effect of humor on mental health and social support, focusing on the type of humor. The result of this study indicated that there was a significant difference between men and women only in offensive humor expression. Moreover, the high social support group indicated higher humor expression of all the forms than the low social support group. This result suggests that humor expression of all forms are useful to obtain social support. The low social support group had higher uneasiness and lower well-being than the high social support group. Therefore, social support is useful to promote the both of positive and negative mental health. It was indicated that three kinds of humor expressions affect social support in path analysis. Furthermore, social support affects happiness and uneasiness. In this research, it was shown that the influence process of humor on mental health was different according to the form of humor expression

Four-electron reduction of dioxygen by a multicopper oxidase, CueO, and roles of Asp112 and Glu506 located adjacent to the trinuclear copper center

金沢大学理工研究域物質化学系The mechanism of the four-electron reduction of dioxygen by a multicopper oxidase, CueO, was studied based on reactions of single and double mutants with Cys500, a type I copper ligand, and the noncoordinating Asp112 and Glu506, which form hydrogen bonds with the trinuclear copper center directly and indirectly via a water molecule. The reaction of C500S containing a vacant type I copper center produced intermediate I in an EPR-silent peroxide-bound form. The formation of intermediate I from C500S/D112N was restricted due to a reduction in the affinity of the trinuclear copper center for dioxygen. The state of intermediate I was realized to be the resting form of C500S/E506Q and C500S of the truncated mutant Δα5-7CueO, in which the 50 amino acids covering the substrate-binding site were removed. Reactions of the recombinant CueO and E506Q afforded intermediate II, a fully oxidized form different from the resting one, with a very broad EPR signal, g < 2, detectable only at cryogenic temperatures and unsaturated with high power microwaves. The lifetime of intermediate II was prolonged by the mutation at Glu506 involved in the donation of protons. The structure of intermediates I and II and the mechanism of the four-electron reduction of dioxygen driven by Asp112 and Glu506 are discussed. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc

Across-axis transition of hydrothermal vent fauna in southern Mariana Trough

http://www.godac.jamstec.go.jp/darwin/cruise/yokosuka/yk10-11/

A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration

Hyperphosphorylation of the microtubule associated protein tau is detected in the brains of individuals with a range of neurodegenerative diseases including Alzheimer's disease (AD). An imbalance in phosphorylation and/or dephosphorylation of tau at disease-related sites has been suggested to initiate the abnormal metabolism and toxicity of tau in disease pathogenesis. However, the mechanisms underlying abnormal phosphorylation of tau in AD are not fully understood. Here, we show that the DNA damage-activated Checkpoint kinase 2 (Chk2) is a novel tau kinase and enhances tau toxicity in a transgenic Drosophila model. Overexpression of Drosophila Chk2 increases tau phosphorylation at Ser262 and enhances tau-induced neurodegeneration in transgenic flies expressing human tau. The non-phosphorylatable Ser262Ala mutation abolishes Chk2-induced enhancement of tau toxicity, suggesting that the Ser262 phosphorylation site is involved in the enhancement of tau toxicity by Chk2. In vitro kinase assays revealed that human Chk2 and a closely related checkpoint kinase 1 (Chk1) directly phosphorylate human tau at Ser262. We also demonstrate that Drosophila Chk2 does not modulate the activity of the fly homolog of microtubule affinity regulating kinase, which has been shown to be a physiological tau Ser262 kinase. Since accumulation of DNA damage has been detected in the brains of AD patients, our results suggest that the DNA damage-activated kinases Chk1 and Chk2 may be involved in tau phosphorylation and toxicity in the pathogenesis of AD