Japan passed a law that eliminated discrimination against persons with disabilities in 2016. Health care providers must comply with this law and are required to deepen their understanding of disabilities and take action to eliminate discrimination based on a higher level of awareness. Pharmacists need to better understand hearing disabilities to effectively communicate and provide medication education to deaf and hard of hearing (HH). This study examined the understanding about deaf and HH communities and the effects of learning through a lecture and hearing loss simulation experiences on 151 students in Daiichi University of Pharmacy to improve their understanding deaf and HH communities and ability to communicate effectively with deaf and HH patients in providing medication education in April 2018. Before the learning, 125 students indicated a lack of confidence in their ability to communicate medication education due to a lack of understanding. However, 26 students responded that they could communicate with deaf and HH patients despite their misunderstandings about deaf and HH communities and the features of such communication. After the learning 132 students indicated they had the confidence to interact with deaf and HH patients in communication for medication education. This study suggests that students need to learn about deaf and HH communities and develop communication skills to interact with them for medication education. Taking these steps may contribute to creating an educational program to facilitate communication and improve medication education for deaf and HH through effective communication by pharmacists.
The canonical Wnt/β-catenin pathway plays crucial roles in various aspects of lung morphogenesis and regeneration/repair. Here, we examined the lung phenotype and function in mice lacking the Wnt/β-catenin antagonist Chibby (Cby). In support of its inhibitory role in canonical Wnt signaling, expression of β-catenin target genes is elevated in the Cby−/− lung. Notably, Cby protein is prominently associated with the centrosome/basal body microtubule structures in embryonic lung epithelial progenitor cells, and later enriches as discrete foci at the base of motile cilia in airway ciliated cells. At birth, Cby−/− lungs are grossly normal but spontaneously develop alveolar airspace enlargement with reduced proliferation and abnormal differentiation of lung epithelial cells, resulting in altered pulmonary function. Consistent with the Cby expression pattern, airway ciliated cells exhibit a marked paucity of motile cilia with apparent failure of basal body docking. Moreover, we demonstrate that Cby is a direct downstream target for the master ciliogenesis transcription factor Foxj1. Collectively, our results demonstrate that Cby facilitates proper postnatal lung development and function.
Abstract: Using autophosphorylated Ca 2+ /calmodulin‐dependent protein kinase II (CaM kinase II) as substrate, we now find that long‐term potentian (LTP) induction and maintenance are also associated with a significant decrease in calyculin A‐sensitive protein phosphatase (protein phosphatase 2A) activity, without changes in Mg 2+ ‐dependent protein phosphatase (protein phosphatase 2C) activity. This decrease in protein phosphatase 2A activity was prevented when LTP induction was inhibited by treatment with calmidazolium or D‐2‐amino‐5‐phosphonopentanoic acid. In addition, the application of high‐frequency stimulation to 32 P‐labeled hippocampal slices resulted in increases in the phosphorylation of a 55‐kDa protein immunoprecipitated with anti‐phosphatase 2A antibodies. Use of a specific antibody revealed that the 55‐kDa protein is the B′α subunit of protein phosphatase 2A. Following purification of brain protein phosphatase 2A, the B′α subunit was phosphorylated by CaM kinase II, an event that led to the reduction of protein phosphatase 2A activity. These results suggest that the decreased activity in protein phosphatase 2A following LTP induction contributes to the maintenance of constitutively active CaM kinase II and to the long‐lasting increase in phosphorylation of synaptic components implicated in LTP.
In order to improve efficiency in the preparation of TAXOTERE® injection for alcohol hypersensitive patients,we investigated its dissolution in warmed saline or 5% glucose solution.Solutions were heated to 3 different temperatures : 25°C,55 °C and 70°C.At 55°C and 70°C,for both warmed saline and 5% glucose,uniform TAXOTERE® premix solutions were obtained within 1 minute,while 10 minutes or more was required at 25°C.Further,to obtain uniform TAXOTERE® premix solutions at 55°C and 70°C only gentle mixing was necessary.There was no need for vigorous shaking.We then investigated the stability of docetaxel hydrate in warmed TAXOTERE® premix solutions using HPLC.No peak for docetaxel hydrate was observed in the case of heating at 25°C for 24 hours or for heating at 55°C heating for 3 hours,for both warmed saline and 5% glucose.At 70°C,peaks assumed to be those of catabolites of docetaxel hydrate were apparent after 60 minutes.In conclusion,we consider that the use of warmed saline or 5% glucose solution at 55°C in the preparation of TAXOTERE® injection for alcohol hypersensitive patients can shorten the preparation time,and greatly raise efficiency in preparation.
In a previous study, we found that human neural stem cells (HNSCs) exposed to high concentrations of secreted amyloid-precursor protein (sAPP) in vitro differentiated into mainly astrocytes, suggesting that pathological alterations in APP processing during neurodegenerative conditions such as Alzheimer's disease (AD) may prevent neuronal differentiation of HNSCs. Thus, successful neuroplacement therapy for AD may require regulating APP expression to favorable levels to enhance neuronal differentiation of HNSCs. Phenserine, a recently developed cholinesterase inhibitor (ChEI), has been reported to reduce APP levels in vitro and in vivo. In this study, we found reductions of APP and glial fibrillary acidic protein (GFAP) levels in the hippocampus of APP23 mice after 14 days treatment with (+)-phenserine (25 mg/kg) lacking ChEI activity. No significant change in APP gene expression was detected, suggesting that (+)-phenserine decreases APP levels and reactive astrocytes by posttranscription regulation. HNSCs transplanted into (+)-phenserine-treated APP23 mice followed by an additional 7 days of treatment with (+)-phenserine migrated and differentiated into neurons in the hippocampus and cortex after 6 weeks. Moreover, (+)-phenserine significantly increased neuronal differentiation of implanted HNSCs in hippocampal and cortical regions of APP23 mice and in the CA1 region of control mice. These results indicate that (+)-phenserine reduces APP protein in vivo and increases neuronal differentiation of HNSCs. Combination use of HNSC transplantation and treatment with drugs such as (+)-phenserine that modulate APP levels in the brain may be a useful tool for understanding mechanisms regulating stem cell migration and differentiation during neurodegenerative conditions in AD.
