13 research outputs found

    THE CURRENT SITUATION OF MASTICATORY BEHAVIOR OF FIRST GRADER AT ELEMENTARY SCHOOL: A RELATIONSHIP BETWEEN MASTICATORY ABILITY AND STUDENTSā€™ LIKES AND DISLIKES

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    Twenty percent of first-graders of a public elementary school in Kanagawa Prefecture were unable to masticate school lunch properly. Teachers encouraged masticate training at school, but it showed no improvement. The purpose of this research was to investigate the characteristics of mastication to find possible methods and more specific mastication education. The subjects were 100 first graders(6ļ½ž7years old) at public elementary school where school lunch was served with an individual tray. The survey was conducted during school lunchtime by recording the bread crust eating situation. Every student was provided with 8g of bread crust cut into three equal parts. Within one month, on the days when kibinago (herring-like forage fish), cabbage, potatoes, curry rice, bonito, and komatsuna (Japanese Spinach) were served, the subjects were asked about their ā€œLikes or Dislikesā€ and the food was ā€œEasy to Masticate or Hard to Masticateā€.The average of masticatory time during eating bread crust was 76 seconds, the maximum was 151 seconds, and the minimum was 19 seconds. The average of masticatory frequency was 72 times, the maximum was 155 times and the minimum was 27 times. The average masticatory speed was 58 beats per minute (bpm), the fastest was 113 bpm and the slowest was 29 bpm. The most favorite dish was curry rice (99%) and the least favorite dishes were kibinago and bonito (13%, respectively). The highest percentage (27%) of the subjects answered bonito dish as ā€œHard to Masticateā€ and the lowest percentage (1%) was curry rice. ā€œDislikeā€ was significantly associated with ā€œHard to Masticateā€ in cabbage (p<0.01) and bonito (p<0.01). The first graders had individual differences in masticatory behavior. It was suggested that ā€œLikes and Dislikesā€ are related to masticatory ability. If the children practice the mastication of solid foods before entering school, the children might eat more smoothly

    Diagonistic Apraxia: A Unique Case of Corpus Callosal Disconnection Syndrome and Neuromyelitis Optica Spectrum Disorder

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    Diagonistic apraxia is a corpus callosal disconnection syndrome. Callosal lesions in Neuromyelitis optica spectrum disorder (NMOSD) have been reported, but callosal disconnection syndrome are rare. A 48-year-old woman was treated for fever and a cough before hospitalization. Her fever abated immediately, but she had balance problems in walking and standing. She also had slurred speech. On neurological examination, she had diagonistic apraxia. Her left hand moved in an uncoordinated way when she moved her right hand: changing her clothes for example or using a knife and fork. She had to instruct her left hand to stop. She had dysarthria and her gait was wide-based. She also had many callosal disconnection syndrome symptoms such as alexia of left visual field, left ear extinction, crossed optic ataxia. Using FLAIR and DWI MRI, a mixture of low and high signals, a so-called ā€œmarbled pattern,ā€ was seen in the corpus callosum. Since the patient was positive for anti-aquaporin-4 antibody, she was diagnosed with NMOSD. After two courses of steroid pulse therapy, the symptoms improved. Here we report diagonistic apraxia and other symptoms of callosal disconnection syndrome in anti-AQP4-positive NMOSD

    Herpesvirus protein ICP27 switches PML isoform by altering mRNA splicing

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    Viruses use alternative splicing to produce a broad series of proteins from small genomes by utilizing the cellular splicing machinery. Since viruses use cellular RNA binding proteins for viral RNA processing, it is presumable that the splicing of cellular pre-mRNAs is affected by viral infection. Here, we showed that herpes simplex virus type 2 (HSV-2) modifies the expression of promyelocytic leukemia (PML) isoforms by altering pre-mRNA splicing. Using a newly developed virus-sensitive splicing reporter, we identified the viral protein ICP27 as an alternative splicing regulator of PML isoforms. ICP27 was found to bind preferentially to PML pre-mRNA and directly inhibit the removal of PML intron 7a in vitro. Moreover, we demonstrated that ICP27 functions as a splicing silencer at the 3ā€² splice site of the PML intron 7a. The switching of PML isoform from PML-II to PML-V as induced by ICP27 affected HSV-2 replication, suggesting that the viral protein modulates the splicing code of cellular pre-mRNA(s) governing virus propagation

    RNA binding activity of HSV-2 ICP27 protein: DOI: 10.14800/rd.1165

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    Herpes Simplex virus (HSV) protein ICP27 is a multifunctional gene expression regulator, which assumes various roles during the course of the viral infection. Previously we identified ICP27 switches RNA isoforms expression of particular genes such as PML (promyelocytic leukemia). Although ICP27 protein contains several RNA binding domains, it remains unclear what domain of ICP27 protein is critically important for RNA binding activity to both host and viral transcripts. Here we characterized the RNA binding activity of ICP27 protein in vitro. We found that R2 domain and three KH domains in the C terminal region of ICP27 protein bound to PML pre-mRNA and also suppressed retention of PML intron 7a, indicating that the C-terminal region contributes to such alternative splicing regulation of host gene. Notably C-terminal region of ICP27 protein efficiently binds to poly G, poly U and poly C, although the N-terminal region preferentially binds to poly G. In addition, the mutant proteins that lack either R2 or KH domains decreases RNA binding activity to poly U. We also employed Cross-Linking and Immuno-Precipitation (CLIP)-PCR approach in HSV-2 infected cells and identified 39 RNA binding targets of ICP27 protein in the viral genome that is G-rich. Finally, we showed that loss of either the N or C terminal regions of ICP27 significantly impaired RNA binding to such viral RNAs. Overall our results suggest that combination of ICP27 protein domains determines specificity of RNA binding to host and HSV-2 RNAs
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