BackgroundBrain-derived neurotrophic factor (BDNF) protein or mRNA levels may be involved in the pathophysiology of bipolar disorder. However, the results were inconsistent. We aimed to simultaneously investigate the relationship of BDNF protein and mRNA levels in peripheral blood of patients with bipolar mania.MethodsPatients with bipolar mania (n = 30) and healthy controls (n = 30) were recruited during our one-year study. Psychiatric diagnoses were made according to Diagnostic and Statistical Manual of Mental Disorders, 4th Edition criteria. The scores of the Young Mania Rating Scale (YMRS) of patients with bipolar mania were greater than 26. All participants had peripheral blood drawn to analyze the serum BDNF protein and mRNA levels.ResultsUsing t-test, patients with bipolar mania had a lower BDNF protein and mRNA levels than did the healthy controls (p < 0.001 and 0.049, respectively), however, the statistical significances were lost after analysis of co-variance adjusted for age and body mass index. Twenty seven out of 30 patients with bipolar mania remained in the study after the 4 weeks of mood stabilizer treatment. Patients' BDNF protein and mRNA levels did not change significantly after 4-week treatment.ConclusionsOur study found that serum BDNF protein and mRNA levels in patients with bipolar mania were lower than healthy controls, but a larger sample size will be needed to confirm this finding.

The gradual emergence of social commerce is enhancing the development of businesses. The opinions exchanged and information shared by each consumer in the community affects consumers’ purchasing decisions and participation behaviors. This study established a consumer information sharing model in social commerce based on the theories of social exchange and communication ecology. Data were collected from 204 respondents and PLS technique was used to analyze the data. The results indicated that reciprocity and community participation exhibited a significantly positive effect on information sharing. Reciprocity and community participation also had partial mediation effects on the consumer–community and consumer–platform relationships.

The current study proposes a computer-assisted instruction (CAI) system built on game design, which aims to increase students' enjoyment, motivation, and immersion. Its main objective is to evaluate the effects of CAI with different interactive interfaces in a learning environment. The authors developed an educational game with a vision-based interface and a keyboard/mouse to compare the differences in children's learning experiences when using different input interfaces. The evaluation of the proposed system was based on the questionnaire findings; the participants are 60 third-and fourthgrade students in Taiwan. The authors addressed the issue of the participants' experience in gender and personal preferences for computer games. Through the questionnaire and data analysis, this study found that a vision-based interface not only attracts the interest of children, but also stimulates their learning motivation. The findings have highlighted the value of the present CAI system with a vision-based interface and confirmed an improvement in learning motivation. Classroom observation indicates that the introduction of a CAI system with a novel interface can be a useful tool for enhancing classroom learning activities.

tRNAHis guanylyltransferase (Thg1) catalyzes the 3′-5′ incorporation of guanosine into position -1 (G-1) of tRNAHis. G-1 is unique to tRNAHis and is crucial for recognition by histidyl-tRNA synthetase (HisRS). Yeast Thg1 requires ATP for G-1 addition to tRNAHis opposite A73, whereas archaeal Thg1 requires either ATP or GTP for G-1 addition to tRNAHis opposite C73. Paradoxically, human Thg1 (HsThg1) can add G-1 to tRNAsHis with A73 (cytoplasmic) and C73 (mitochondrial). As N73 is immediately followed by a CCA end (positions 74–76), how HsThg1 prevents successive 3′-5′ incorporation of G-1/G-2/G-3 into mitochondrial tRNAHis (tRNAmHis) through a template-dependent mechanism remains a puzzle. We showed herein that mature native human tRNAmHis indeed contains only G-1. ATP was absolutely required for G-1 addition to tRNAmHis by HsThg1. Although HsThg1 could incorporate more than one GTP into tRNAmHisin vitro, a single-GTP incorporation prevailed when the relative GTP level was low. Surprisingly, HsThg1 possessed a tRNA-inducible GTPase activity, which could be inhibited by ATP. Similar activity was found in other high-eukaryotic dual-functional Thg1 enzymes, but not in yeast Thg1. This study suggests that HsThg1 may downregulate the level of GTP through its GTPase activity to prevent multiple-GTP incorporation into tRNAmHis.