Effect of masseter muscle activity during wakefulness and sleep on tooth wear.

PURPOSE: To investigate the effect of masseter muscle activity during wakefulness and sleep on tooth wear. METHODS: Sixteen participants with no or mild tooth wear (NMTW group) and sixteen participants with moderate-to-severe tooth wear (MSTW group) were enrolled. The severity of tooth wear was evaluated using the occlusal and incisal indices of the tooth wear index. Surface electromyography was performed to record the electrical activity of the left masseter muscle during wakefulness and sleep. Electromyographic activity was detected using an electromyographic threshold of 5% and 20% of maximal voluntary clenching (MVC). The total duration of electromyographic activity and bruxism episodes were calculated. RESULTS: The mean ages of the NMTW and MSTW groups were 71.75 ± 7.61 years and 71.69 ± 7.49 years, respectively. The mean cumulative duration of electromyographic activity during wakefulness using a threshold of >5% MVC was 6.44 ± 4.52 min/h and 13.62 ± 10.08 min/h for the NMTW and MSTW groups, respectively (p=0.048). The mean total durations of electromyographic activity during wakefulness and sleep using a threshold of >20% MVC were 1.08 ± 1.70 min/h and 1.05 ± 3.02 min/h, respectively, in the NMTW group and 4.78 ± 6.37 min/h and 1.61 ± 1.79 min/h, respectively, in the MSTW group (p=0.048 and p=0.003, respectively). CONCLUSION: These results suggest that masseter electromyographic activity during wakefulness and sleep may be related to the severity of tooth wear.

Coordination of surface electromyography activity in the posterior tongue region during mastication of differently textured foods.

BACKGROUND: Masticatory movement occurs complicatedly and bilaterally. Although the tongue plays an important role in mastication, bilateral tongue function during mastication has not been clarified yet. OBJECTIVE: To investigate the effect of food properties on posterior tongue activity and coordination of muscles bilaterally by electromyography (EMG). METHODS: Twenty healthy adults (10 males and 10 females; mean age 28 years; range: 22-33 years) participated in this study. Three test foods, gummy jelly (hard food), sponge cake (soft food requiring crushing), and mashed potatoes (soft food not requiring crushing), were used. Bilateral masseter N-EMG (surface electromyography for measuring the muscle activity of posterior tongue) and submental EMG were carried out while the participants chewed three test foods. The participants were instructed to masticate three test foods only on the right side and only on the left side unilaterally. RESULTS: In the case of gummy jelly, N-EMG activity on the mastication side was significantly larger than that on the non-mastication side (P < .01). Regarding temporal relationship between the masseter and N-EMG activity, in the case of gummy jelly, the percentage of cases where the N-EMG peak was observed during masseter muscle EMG bursts was significantly higher than those for sponge cake and mashed potatoes (P < .01). CONCLUSION: N-EMG activity on the mastication side was significantly larger than that on the non-mastication side in the mastication of hard foods. Tongue showed activity pattern changes and coordinated with the masseter muscle depending on food texture.

An evaluation tool for FKBP12-dependent and -independent mTOR inhibitors using a combination of FKBP-mTOR fusion protein, DSC and NMR.

Mammalian target of rapamycin (mTOR), a large multidomain protein kinase, regulates cell growth and metabolism in response to environmental signals. The FKBP rapamycin-binding (FRB) domain of mTOR is a validated therapeutic target for the development of immunosuppressant and anticancer drugs but is labile and insoluble. Here we designed a fusion protein between FKBP12 and the FRB domain of mTOR. The fusion protein was successfully expressed in Escherichia coli as a soluble form, and was purified by a simple two-step chromatographic procedure. The fusion protein exhibited increased solubility and stability compared with the isolated FRB domain, and facilitated the analysis of rapamycin and FK506 binding using differential scanning calorimetry (DSC) and solution nuclear magnetic resonance (NMR). DSC enabled the rapid observation of protein-drug interactions at the domain level, while NMR gave insights into the protein-drug interactions at the residue level. The use of the FKBP12-FRB fusion protein combined with DSC and NMR provides a useful tool for the efficient screening of FKBP12-dependent as well as -independent inhibitors of the mTOR FRB domain.

Identification and relative quantitation of an orphan G-protein coupled receptor SREB2 (GPR85) protein in tissue using a linear ion trap mass spectrometer.

SREB2 (GPR85) is an orphan G-protein coupled receptor (GPCR) whose function is unknown. We previously prepared a SREB2-overexpressing transgenic mouse for functional analysis but were unable to confirm SREB2 protein expression level by immunochemical or biochemical methods. In this article, we report mass spectrometric identification and relative quantitative analysis of SREB2 in the forebrains of transgenic and wild type mice using nanoliquid chromatography coupled with a linear ion-trap mass spectrometer. By analyzing Chinese hamster ovary (CHO) cells overexpressing the SREB2 gene, we identified a proteotypic SREB2 peptide, GPTPPTLLGIR. Using a stable isotope-labeled analog as an authentic peptide for protein identification and as an internal control for relative quantitation, SREB2 was directly identified from the membrane fraction of forebrains from wild type and SREB2 transgenic mice. SREB2 protein expression level in the transgenic mouse was estimated to be 3-fold higher than that in the wild type littermate.

STAT3 and Oct-3/4 control histone modification through induction of Eed in embryonic stem cells.

Mouse embryonic stem (ES) cells can self-renew in the presence of leukemia inhibitory factor (LIF). Several essential transcription factors have been identified for the self-renewal of mouse ES cells, including STAT3, Oct-3/4, and Nanog. The molecular mechanism of ES cell self-renewal, however, is not fully understood. In the present study, we identified Eed, a core component of Polycomb repressive complex 2, as a downstream molecule of STAT3 and Oct-3/4. Artificial activation of STAT3 resulted in increased expression of Eed, whereas expression of a dominant negative mutant of STAT3 or suppression of Oct-3/4 expression led to down-regulation of Eed. Reporter, chromatin immunoprecipitation, and electrophoretic mobility shift assays revealed that STAT3 and Oct-3/4 directly bind to the promoter region of Eed, suggesting that Eed is a common target molecule of STAT3 and Oct-3/4. We also found that suppression of STAT3, Oct-3/4, or Eed causes induction of differentiation-associated genes as well as loss of Lys(27)-trimethylated histone H3 at the promoter regions of the differentiation-associated genes. Suppression of STAT3 and Oct-3/4 also resulted in the absence of Eed at the promoter regions. These results suggest that STAT3 and Oct-3/4 maintain silencing of differentiation-associated genes through up-regulation of Eed in self-renewing ES cells.