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Objective:To explore the association between left-behind status, screen time (ST) and behavior of autism in rural preschool children.Methods:Cross section study was used in this study.A sample of 3 636 rural preschool children aged from 3 to 6 years old in 26 kindergartens were selected from four counties in Anhui province of China.The contents of the questionnaire include: basic information questionnaire, self-made left behind status questionnaire, self-made screen time questionnaire, Clancy autism behavior scale.EpiData 3.2 and SPSS 23.0 software were used for data entry and statistical analysis.Chi-square test was used to analyze the difference of positive rate of autism behavior.Logistic regression analysis was used to further explore the relationship between left-behind status, screen time and autism behavior of rural preschool children.Results:Compared with non-left-behind children (NLBC), the risk of autism behavior for left-behind children (LBC) increased 36%.The risk of autism behavior increased by 40% for 1 h/d <ST≤ 2 h/d and 85% for ST>2 h/d when compared with ST ≤ 1 h/d.While comparing to NLBC with ST ≤ 1 h/d, the risk of autism behavior increased by 97% in LBC with 1 h/d <ST ≤2 h/d and 159% in LBC with ST>2 h/d.Conclusions:There is an additive effect on the risk of autism behavior when left-behind experience and excessive ST combined together.The daily ST should be strictly controlled within 2 h/d for NLBC, and within 1 h/d for LBC in order to reduce the risk of autism behavior in preschool children of rural areas.
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Objective To establish a joint wavelength switching HPLC gradient elution method for simultaneous determination of darutoside, kirenol, darutigenol, fangchinoline and d-tetrandrine in Xixian Fengshi Wan. Methods A Kromasil C18 column (4. 6 mm × 250 mm, 5 μm) was used with a mobile phase A; acetonitrile-methano (2: 1) and mobile phase B: 0. 05% acetic acid solution with gradient elution. The flow rate was 1. 0 mL/min; the injection volume was 20 μL; darutoside, kirenol and darutigenol were detected at 215 nm, and fangchinoline and d-tetrandrine were detected at 280 nm. Results In the given concentration range, the linearity ranges of darutoside, kirenol, darutigenol, fangchinoline and d-tetrandrine were 6. 45-129. 00 μg/mL (r=0. 999 5), 5. 61-112. 20 μg/mL (r=0. 999 9), 4. 25-85. 00 μg/mL (r=0. 999 3), 9. 19-183. 80 μg/mL (r =0.999 8), and 11. 05-221. 00 μg/mL (r=0. 999 7), respectively; and their average recoveries and RSD were 98. 73% (1. 43%), 97. 63% (1. 28%), 99. 44% (1. 29%), 98. 33% (1. 38%), and 97. 36% (1. 37%), respectively. Conclusion The established joint wavelength switching HPLC gradient elution method is simple, accurate and reproducible; it can simultaneously determine the contents of darutoside, kirenol, darutigenol, fangchinoline and d-tetrandrine in Xixian Fengshi Wnn and can be used for quality control of Xixinn Fengshi Wan.
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Objectives To investigate the mutational characteristics of MSX1 and PAX9 genes in a family affected by non-syndromic oligodonti so as to study the pathogenesis of oligodontia from a molecular prospective. Methods A family with oligodontia, but of different descent and unrelated healthy controls were enrolled in our study. Genomic DNA was isolated from the blood samples. Mutation analyses were performed by amplifying MSX1 and PAX9 exons and sequencing the products. Results DNA sequencing revealed a novel missense mutation c.348C>T in a highly conserved homeobox sequence of MSX1 and a known polymorphisms c. 469+35- c.469+45del in exon 1 and in intron in the two patients and in two unrelated healthy controls. But we did not detect any mutation in PAX9. Conclusion Our finding suggests the samesense mutation (c.348C>T) and the polymorphisms (c.469+35- c.469+45del) may be responsible for oligodontia phenotype in this Chinese family.
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<p><b>OBJECTIVE</b>This study aimed to investigate the effects of hirudin on the expression of transforming growth factor (TGF-β1) and basic fibroblast growth factor (bFGF) in human gingival fibroblasts (HGFs) in vitro, as well to explore its func- tion in the mechanism of gingival remodeling.</p><p><b>METHODS</b>After culturing was performed with classic tissue-explant method, HGFs were derived from normal gingival and gingival hyperplasia tissues followed by orthodontic treatments with different concentrations of hirudin. The mRNA and protein expression levels of TGF-β1 and bFGF were respectively detected by real time quantity polymerase chain reaction and immunocytochemistry.</p><p><b>RESULTS</b>Compared with normal HGFs, TGF-β1 expression promoted collagen synthesis of fibroblasts, whereas bFGF collagen synthesis was decreased in hyperplasia HGFs without hirudin (P < 0.05). Hirudin significantly upregulated the expression levels of bFGF but downregulated TGF-β1 in hyperplasia HGFs (P < 0.05).</p><p><b>CONCLUSION</b>Orthodontic force may influence the balance of collagen synthesis and degradation in HGFs. Hirudin may modulate the balance of HGF collagen metabolism, thereby promoting gingival remodeling.</p>
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Humans , Fibroblast Growth Factor 2 , Fibroblasts , Gingiva , Hirudins , RNA, Messenger , Transforming Growth Factor beta , Transforming Growth Factor beta1ABSTRACT
<p><b>OBJECTIVE</b>To examine the expression of molar root patterning gene 1 (Mrp1) and predict the Mrp1 structure by bioinformatics analysis.</p><p><b>METHODS</b>A pair of Mrp1-specific PCR primers were designed, and RT-PCR method was used to study the mRNA's expression pattern in rat molar root and other organs. Gene positioning and other protein sequence prediction were carried out by chromosome analysis and other bioinformatics analysis.</p><p><b>RESULTS</b>Mrp1 was expressed not only in the molar but also in the developing pancreas, liver, lung and kidney tissues. Mrp1 was located in the 18q12.3 chromosome of the rats and the Mrp1 amino acids sequence had about 37% homology with a known protein Uroplakin IIIb (p35) which was an urothelial differentiation membrane molecular marker. A trans-membrane structure, 5 PKC phosphorylation sites and 4 CKII phosphorylation sites in Mrp1 were found.</p><p><b>CONCLUSIONS</b>Mrp1 has a broad expression in different developing organs, and it may have a important function in the rat tooth root development.</p>
Subject(s)
Animals , Rats , Computational Biology , Gene Expression Regulation, Developmental , Genes , Molar , Molecular Sequence Data , Protein Sorting Signals , Genetics , Proteins , Genetics , Metabolism , Rats, Sprague-Dawley , Reverse Transcriptase Polymerase Chain Reaction , Tooth RootABSTRACT
Objective:To evaluate the physiological roles of bmp3,bmp4 and bmp7 during the formation of permanent tooth roots in dog. Methods:The expression of bmp3,bmp4 and bmp7 mRNA at different stages of the development of permanent tooth roots was examined by in situ hybridization in 3 dogs aged 12-18 weeks. Results:bmp3 was found in dental sac surrounding the germs at the early stage of tooth root development, and in cementoblasts and periodontal cells at the later stage. bmp4 was found in odontoblasts, dental papilla and osteoblasts. bmp7 positive signals was found only in epithelial cells of root sheath around cervical circulus at early stage, then located in cementoblasts and odontoblasts at later stage. Conclusion:The spatiotemporal expressions of bmp3,bmp4 and bmp7 are widely diverse, indicating that they participate in the regulation of tooth root development.
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Objective:To observe the temporal and spatial expression and function of mcpr1 gene during murine tooth germ development.Methods:The expression of MCPR1 at different stages of mouse tooth germ were detected by immunohistochemical staining.Results:MCPR1 expression was detected at all stages of tooth germ, but the distribution patterns at various stages were different. It indicated that the temporal and spatial expression pattern of MCPR1 during murine tooth germ development was specific.Conclusion:mcpr1 might play an important role in modulating the differentiation and mature of enamel organ.
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Objective: To construct mcpr1prokaryoti c expression vector and to express MCPR1 protein.Methods:PCR was used to obtain coding region of mcpr1. Construction of a high-level fusion protein expression vector pGEX-4T-mcpr1 was conducted by inserting the fra gment of coding region of mcpr1into a fusion protein expression vector pGEX -4T-1. Then the recombinant plasmid was transferred into E. colito prepar e the MCPR1/GST fusion protein. DNA sequencing and endonucleases digesting were used to check the coding region. Results:pGEX-4T- mcpr1 wa s constructed successfully and the coding region was inserted into the vector co rrectly. A new protein band of 36 000 was observed by SDS-PAGE analysis after i nduction by IPTG. The 36 000 protein amounted to 39 percent of the total prote in and existed mostly in precipitation of broken bacteria. Conclusion: MCPR1 protein can be expressed in E. coliexpression system and purif ied initially.