Usefulness of a simulated experience method for transfer assistance for hemiplegia or limited range of motion in multiple joints.

[Purpose] To further the understanding of dysfunctions to which a simulated experience method could be applied, we clarified whether a simulated experience method can promote caregivers to utilize the abilities of care recipients with pseudo-hemiplegia or pseudo-limited range of motion (ROM) in multiple joints. [Participants and Methods] We studied transfer assistance in 60 nursing assistants from nursing home settings: 30 were assigned to the pseudo-hemiplegia (26 females, 4 males) and limited ROM in multiple joints (27 females, 3 males) groups. One healthy person was fitted with orthotic braces to mimic hemiplegia or limited ROM in multiple joints, each making it difficult to stand-up. Participants were randomized to either a simulated experience group (involving interventional help from a physical therapist between the first and second measurements) or a control group. The load difference on the lower limbs of the care recipient between two rounds of transfer assistance was examined. [Results] The difference between the second and first measurements was -5.9 ± 74.5 N for the control group and 107.9 ± 123.6 N for the simulated experience method in the pseudo-hemiplegia study, and -14.7 ± 64.7 N and 149.1 ± 132.4 N, respectively, for the pseudo-limited ROM-in-multiple-joints study. [Conclusion] The simulated experience method promoted transfer assistance of a care recipient with pseudo-hemiplegia or pseudo-limited ROM in multiple joints. These results suggest that hemiplegia and limited ROM in multiple joints are added as dysfunctions that can be applied to a simulated experience method in transfer assistance.

Usefulness of simulation method to improve efficiency of chair-to-wheelchair transfer of patients performed by caregivers.

[Purpose] We aimed to clarify whether demonstration and simulated experience help the ability of care-receivers to get transferred, such as from the bed to the commode. [Participants and Methods] Participants included 28 nurses and 17 caregivers (34 females and 11 males). We developed a total floor reaction force measurement device to quantify the total loading level of care-receivers and caregivers and force shoes to quantify the loading level of the caregivers. Using these instruments, we constructed a system to measure the load on the lower limbs of the care-receivers during partial assistance. We divided the participants into the control, demonstration, and simulated experience method groups. We examined the differences in the load on the lower limbs before and after the intervention. [Results] The loads on the lower limbs of care-receivers when their buttocks were lifted from the chair were 11.7 ± 69.6, 61.8 ± 79.4, and 101.0 ± 104.0 N in the control, demonstration, and simulated experience groups. [Conclusion] These data suggest that the simulated experience method could help make use of the ability of the care-receiver to get transferred. Even care workers for the sanatorium-type sickbeds could learn to utilize the physical ability of the care-receivers using simulated experience.

Effect of Chlorella Ingestion on Oxidative Stress and Fatigue Symptoms in Healthy Men.

OBJECTIVE: We examined the effects of dietary chlorella ingestion on oxidative stress and fatigue symptoms in healthy men under resting and fatigue conditions. METHOD: We conducted a double-blind, parallel-arm controlled study. Twenty-seven healthy male volunteers (mean age, 35.4±10.4 years) were randomly divided into the chlorella and placebo groups, and received chlorella (6 g/day) and lactose as placebo (7.2 g/day), respectively, for 4 weeks. To simulate mild fatigue, subjects underwent exercise (40% of the heart rate reserve) for 30 minutes. Fatigue was measured using the visual analog scale of fatigue (F-VAS) pre- and post-exercise. Serum antioxidant capacity (AC), malondialdehyde levels, and other indices of oxidative stress were measured pre- and post-exercise. All measurements were repeated after the intervention period and the results were compared with baseline measurements. RESULTS: Under resting conditions, AC significantly increased after the intervention period in the chlorella group, but not in the placebo group. Malondialdehyde levels after the intervention period were significantly lower in the chlorella group than in the placebo group. There were no significant differences in any of the oxidative-stress indices measured pre- and post-exercise, either before or after intervention, in either group. F-VAS significantly increased after exercise at all measurement time-points in both groups, except after the intervention period in the chlorella group. Under fatigue conditions, there were no significant differences in oxidative stress indices between the groups. CONCLUSIONS: Our results suggest that chlorella ingestion has the potential to relieve oxidative stress and enhance tolerance for fatigue under resting conditions.

The regulation mechanisms of AhR by molecular chaperone complex.

The AhR, so called the dioxin receptor, is a member of the nuclear receptor superfamily. The ligand-free AhR forms a cytosolic protein complex with the molecular chaperone HSP90, co-chaperone p23, and XAP2 in the cytoplasm. Following ligand binding like 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin (TCDD), the AhR translocates into the nucleus. Although it has been reported that HSP90 regulates the translocation of the AhR to the nucleus, the precise activation mechanisms of the AhR have not yet been fully understood. AhR consists of the N-terminal bHLH domain containing NLS and NES, the middle PAS domain and the C-terminal transactivation domain. The PAS domain is familiar as a ligand and HSP90 binding domain. In this study, we focused on the bHLH domain that was thought to be a HSP90 binding domain. We investigated the binding properties of bHLH to HSP90. We analyzed the direct interaction of bHLH with HSP90, p23 and XAP2 using purified proteins. We found that not only the PAS domain but also the bHLH domain bound to HSP90. The bHLH domain forms complex with HSP90, p23 and XAP2. We also determined the bHLH binding domain was HSP90 N-domain. The bHLH domain makes a complex with HSP90, p23 and XAP2 via the HSP90 N-domain. Although the NLS is closed in the absence of a ligand, the structure of AhR will be changed in the presence of a ligand, which leads to NLS open, result in the nuclear translocation of AhR.

The activation mechanism of the aryl hydrocarbon receptor (AhR) by molecular chaperone HSP90.

The aryl hydrocarbon receptor is a member of the nuclear receptor superfamily that associates with the molecular chaperone HSP90 in the cytoplasm. The activation mechanism of the AhR is not yet fully understood. It has been proposed that after binding of ligands such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), 3methylcholanthrene (3-MC), or ß-naphthoflavone (ß-NF), the AhR dissociates from HSP90 and translocates to the nucleus. It has also been hypothesized that the AhR translocates to the nucleus and forms a complex with HSP90 and other co-chaperones. There are a few reports about the direct association or dissociation of AhR and HSP90 due to difficulties in purifying AhR. We constructed and purified the PAS domain from AhR. Binding of the AhR-PAS domain to ß-NF affinity resin suggested that it possesses ligand-binding affinity. We demonstrated that the AhR-PAS domain binds to HSP90 and the association is not affected by ligand binding. The ligand 17-DMAG inhibited binding of HSP90 to GST-PAS. In an immunoprecipitation assay, HSP90 was co-immunoprecipitated with AhR both in the presence or absence of ligand. Endogenous AhR decreased in the cytoplasm and increased in the nucleus of HeLa cells 15 min after treatment with ligand. These results suggested that the ligand-bound AhR is translocated to nucleus while in complex with HSP90. We used an in situ proximity ligation assay to confirm whether AhR was translocated to the nucleus alone or together with HSP90. HSP90 was co-localized with AhR after the nuclear translocation. It has been suggested that the ligand-bound AhR was translocated to the nucleus with HSP90. Activated AhR acts as a transcription factor, as shown by the transcription induction of the gene CYP1A1 8 h after treatment with ß-NF.

Influences of weight loss on monocytes and T-cell subpopulations in male judo athletes.

The purpose of this study was to examine weight loss effects on immune function in judo athletes. Six elite male Japanese judo athletes (20.3 ± 0.4 years) were enrolled in this study. They completed usual weight loss programs during 2 weeks preceding an actual competition. Subjects noted the appearance of upper-respiratory tract infection (URTI) symptoms during the study period. Blood samples were obtained at 40 (baseline period: BL) and 3 (weight loss period: WL) days before and 1 day after the competition (AC). The CD3, CD4, CD8, CD56CD3, CD28CD4, CD28CD8, and Toll-like-receptor-4 (TLR-4) CD14 cells were counted by using flow cytometer analysis. The 6 subjects reported 1 headache, 3 runny nose conditions, and 1 coughing instance during the WL. The CD3, CD4, CD8, and CD28CD4 cell counts were significantly lower at WL than at BL (p ≤ 0.05); they reverted to the baseline value at AC. The TLR-4CD14 cells were significantly fewer at WL (p ≤ 0.05); they remained fewer than they had been at BL, even at AC. These results suggest that 2 weeks of weight loss before a competition can impair cell-mediated immune function and induce high susceptibility to URTI in judo athletes. Coaches, support staff, and athletes should monitor athletes' weight loss, hydration status, appearance of URTI symptoms, and immunocompetence such as lymphocytes and monocytes to prevent the physical condition from becoming worse.

Increased expression of co-chaperone HOP with HSP90 and HSC70 and complex formation in human colonic carcinoma.

Co-chaperone HOP (also called stress-inducible protein 1) is a co-chaperone that interacts with the cytosolic 70-kDa heat shock protein (HSP70) and 90-kDa heat shock protein (HSP90) families using different tetratricopeptide repeat domains. HOP plays crucial roles in the productive folding of substrate proteins by controlling the chaperone activities of HSP70 and HSP90. Here, we examined the levels of HOP, HSC70 (cognate of HSP70, also called HSP73), and HSP90 in the tumor tissues from colon cancer patients, in comparison with the non-tumor tissues from the same patients. Expression level of HOP was significantly increased in the tumor tissues (68% of patients, n = 19). Levels of HSC70 and HSP90 were also increased in the tumor tissues (95% and 74% of patients, respectively), and the HOP level was highly correlated with those of HSP90 (r = 0.77, p < 0.001) and HSC70 (r = 0.68, p < 0.01). Immunoprecipitation experiments indicated that HOP complexes with HSC70 or HSP90 in the tumor tissues. These data are consistent with increased formation of co-chaperone complexes in colon tumor specimens compared to adjacent normal tissue and could reflect a role for HOP in this process.