Sleep problems are known to be risk factors for subsequent emotional and behavioral difficulties in childhood and adolescence. To date, there has been no study investigating the relationships between sleep habits and behavioral problems in a large nonclinical sample of preschool age children. The aim of this study was to examine these relationships and factors associated with the sleep habits of preschool age (2 to 5 year old) children. Their mothers (n = 1,746) completed a multiple-choice questionnaire about the sleep habits and behavior problems of their children, as well as their own sleep habits and working hours at Tokyo metropolitan public nursery schools. The short sleep duration group showed significantly higher aggressive scores than the long sleep duration group among 2-to 3-year-old children, and the irregular bedtime group showed significantly higher aggressive and attention problem scores than the regular bedtime group among 4-to 5-year-old children. Univariate and multivariate logistic regression analyses revealed that children's late bedtime was associated with their mother's late waking-up time, and late schedule of both the mother's leaving and returning home. This study recognized an association between behavioral problems and poor sleep habits among preschool-age children. It is important for children to sleep regularly and adequately in order to decrease their behavior problems. In conclusion, appropriate management of children's sleep by their mothers is necessary for promoting sleep-related health of children.
Applications of the GFP-fusion technique have greatly facilitated evaluations of the amounts and qualities of sample proteins used for structural analyses. In this study, we applied the GFP-based sample evaluation to secreted protein expression by insect cells. We verified that a GFP variant, GFPuv, retains proper folding and monodispersity within all expression spaces in Sf9 cells, such as the cytosol, organelles, and even the extracellular space after secretion, and thus can serve as a proper folding reporter for recombinant proteins. We then applied the GFPuv-based system to the extracellular domains of class C G-protein coupled receptors (GPCRs) and examined their localization, folding, and oligomerization upon insect cell expression. The extracellular domain of metabotropic glutamate receptor 1 (mGluR1) exhibited good secreted expression by Sf9 cells, and the secreted proteins formed dimer with a monodisperse hydrodynamic state favorable for crystallization, consistent with the results from previous successful structural analyses. In contrast, the extracellular domains of sweet/umami taste receptors (T1R) almost completely remained in the cell. Notably, the T1R and mGluR1 subfractions that remained in the cellular space showed polydisperse hydrodynamic states with large aggregated fractions, without forming dimers. These results indicated that the proper folding and oligomerization of the extracellular domains of the class C GPCR are achieved through the secretory pathway.
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