[Expectations toward the care service and the medical service for elderly in Japan].

Aim: With the purpose of gathering basic data in order to prompte various research toward the realization of a vibrant aging society, we performed a nationwide 'Survey on life' intended for citizens over 60 years old who engage in independent living, preserving their state of health even after retirement.

Methods: We created a survey form consisting of 14 question items. Processing 4,000 persons surveyed from 100 locations chosen nationwide, we obtained a total of 2,370 answers from both male and female subjects, with an effective recovery rate of 59.

Anticancer activity of phenoxazines produced by bovine erythrocytes on colon cancer cells.

The present study investigated the anticancer activity of 2-aminophenoxazine-3-one (Phx-3) and 2-amino-4,4 alpha-dihydro-4 alpha,7-dimethyl-3H-phenoxazine-3-one (Phx-1), which were obtained by improved preparation methods using bovine erythrocyte suspension, on colon cancer cell lines COLO201, DLD1 and PMCO1 in vitro. The preparation methods for Phx-1 and Phx-3 had the advantages of extensively shortening reaction time and reducing sample volumes up to one-seventh during treatment, compared with the conventional method using bovine hemoglobin solution, resulting in extensive reduction of handling time. Phx-1 and Phx-3 thus obtained were identified as pure by the absorption spectra and NMR spectra.

Is the periaqueductal gray an essential relay center for the micturition reflex pathway in the cat?

The periaqueductal gray (PAG), especially in a region between the levels the oculomotor nucleus and the trochlear nucleus, was suggested to be the essential relay center that conveys information of bladder fullness to the pontine micturition center (Barrington's nucleus). The present study examined this hypothesis by transecting the brainstem in anesthetized cats. In eight cases of the midbrain transection, all (n=3) or most (n=5) of the PAG between the levels the oculomotor nucleus and the trochlear nucleus was separated from the intact side of the brain.

Mitochondrial depolarization and apoptosis associated with sustained activation of c-jun-N-terminal kinasein the human multiple myeloma cell line U266 induced by 2-aminophenoxazine-3-one.

We investigated the involvement of c-jun-N-terminal kinase (JNK) in mitochondrial depolarization and apoptosis in a human multiple myeloma cell line, U266, treated with 2-aminophenoxazine (Phx-3). It was found that, with Phx-3 administration to U266 cells, JNK was phosphorylated 2 and 7.5-fold at 6 and 24 h, respectively, compared to the Phx-3-free control.

[A patient with early Alzheimer's disease who showed improvement of cognitive function and cerebral perfusion by combined therapy of nilvadipine and PPAR gamma agonists].

A 76-year-old man was referred to our hospital because of memory impairment. He was diagnosed as having early Alzheimer's disease, in addition to hypertension and type II diabetes mellitus. Nilvadipine (a Ca-channel blocker), telmisartan (an angiotension II receptor blocker), and pioglitazone (an insulin sensitizer) were administered for the control of the hypertension and diabetes.

Apoptosis induction preceded by mitochondrial depolarization in multiple myeloma cell line U266 by 2-aminophenoxazine-3-one.

The aim of the present study was to investigate the mechanism of apoptosis in human multiple myeloma cell line, U266, caused by 2-aminophenoxazine-3-one (Phx-3). Flow-cytometrical and morphological analyses showed that Phx-3 increased the population of annexin V-positive cells including early stage apoptotic cells and late stage apoptotic cells and induced DNA fragmentation or apoptotic body formation in U266 cells, indicating that Phx-3 induced the apoptosis of U266 cells. Activity of caspase-3 was extensively increased in U266 cells treated with Phx-3 time-dependently within 24 h, but this Phx-3-stimulated activity of the enzyme in the cells was completely cancelled by the addition of N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (z-VAD-fmk), a pan-caspase inhibitor.