Development, validity, and reliability of the Japanese version of the 7C of vaccination readiness scale.

BACKGROUND: The 7C of the vaccination readiness scale measures the 7 psychological components that structure people's vaccination readiness. We aimed to develop the Japanese version of this scale (7C scale Japanese version) and to assess its validity and reliability. METHODS: The full and short versions of 7C scale Japanese were developed based on translation guidelines provided by the ISPOR Task Force. An Internet survey, including 709 participants, was performed to assess the scale's validity and reliability within a confirmatory factor analysis (CFA) framework (men: 38.8%, age range: 20-92 years). Invariance analysis using multiple-group CFA was conducted to test cross-cultural validity between participants in this study and those in the 7C original version study. McDonald's omega and intraclass correlation coefficient were calculated to evaluate internal consistency and test-retest reliability, respectively. To clarify the criterion validity, regression analysis, with previous COVID-19 vaccination status as the dependent variable, was performed to calculate pseudo R2. RESULTS: The 7C scale Japanese version exhibited good content validity, structural validity, configural invariance, and criterion validity. The results showed good internal consistency, and test-retest reliability, except for the "calculation" component. CONCLUSIONS: 7C scale Japanese version exhibited acceptable reliability and validity; however, "calculation" may be a less reliable subscale.

Arginine is a disease modifier for polyQ disease models that stabilizes polyQ protein conformation.

The polyglutamine (polyQ) diseases are a group of inherited neurodegenerative diseases that include Huntington's disease, various spinocerebellar ataxias, spinal and bulbar muscular atrophy, and dentatorubral pallidoluysian atrophy. They are caused by the abnormal expansion of a CAG repeat coding for the polyQ stretch in the causative gene of each disease. The expanded polyQ stretches trigger abnormal ß-sheet conformational transition and oligomerization followed by aggregation of the polyQ proteins in the affected neurons, leading to neuronal toxicity and neurodegeneration. Disease-modifying therapies that attenuate both symptoms and molecular pathogenesis of polyQ diseases remain an unmet clinical need. Here we identified arginine, a chemical chaperone that facilitates proper protein folding, as a novel compound that targets the upstream processes of polyQ protein aggregation by stabilizing the polyQ protein conformation. We first screened representative chemical chaperones using an in vitro polyQ aggregation assay, and identified arginine as a potent polyQ aggregation inhibitor. Our in vitro and cellular assays revealed that arginine exerts its anti-aggregation property by inhibiting the toxic ß-sheet conformational transition and oligomerization of polyQ proteins before the formation of insoluble aggregates. Arginine exhibited therapeutic effects on neurological symptoms and protein aggregation pathology in Caenorhabditis elegans, Drosophila, and two different mouse models of polyQ diseases. Arginine was also effective in a polyQ mouse model when administered after symptom onset. As arginine has been safely used for urea cycle defects and for mitochondrial myopathy, encephalopathy, lactic acid and stroke syndrome patients, and efficiently crosses the blood-brain barrier, a drug-repositioning approach for arginine would enable prompt clinical application as a promising disease-modifier drug for the polyQ diseases.