7 research outputs found
Reliability of Frontal Sinus Morphology with Cervical Vertebral Maturation for the Assessment of Skeletal Maturity
No full textINTRODUCTION:
Growth, an expository variable aids the orthodontist in precise diagnosis and treatment planning. Variations in developmental pattern led to the evolution of malocclusion and dentofacial deformities. Developmental status of a patient can be evaluated by several methods but most of them failed to give a reliable estimate of skeletal maturity.
AIM OF THE STUDY:
To evaluate the correlation of frontal sinus morphology with cervical vertebrae stages as a skeletal maturity indicator.
MATERIALS AND METHODS:
A total of 180 lateral cephalograms of subjects aged between 8 and 16 years were included in the study. Based on the cervical maturation stages, the subjects were divided into 6 groups with 1:1 male to female ratio. The frontal sinus index and the cervical stages were evaluated on the same radiograph. Frontal sinus index was compared with different cervical stages by Kruskal-Wallis test and frontal sinus index values between adjacent cervical stages were compared for each sex by post hoc Dunnett T3 test. The correlation between the cervical stages and the sinus index were assessed by Kendall tau-b values.
RESULTS:
There was a significant linear increase and a good statistical correlation of the frontal sinus height and width at each cervical vertebral maturation stages. The index of frontal sinus increases statistically with the cervical vertebral maturation but had a weak correlation with the maturation stage. There was no significant relationship and no significant correlation of frontal sinus height, width and index with gender.
CONCLUSION:
Frontal sinus morphology cannot be used as a reliable sole indicator for the appraisal of skeletal maturity in patients
Canine retraction and anchorage loss using self-ligating and conventional brackets with sliding mechanics: A split-mouth clinical study
No full textOBJECTIVE: Appliance biocompatibility, orthodontic treatment efficiency and patient convenience are the major issues confronting contemporary orthodontic practice. Very few studies have been published till date regarding the efficiency of self-ligating brackets as against conventional brackets. Hence, the present study was planned to compare the rate of canine retraction between self-ligating and conventional brackets and to determine the amount of anchorage loss during canine retraction.
METHODS: The present clinical study was designed as a prospective, observational study comprising of 25 patients requiring first premolar extraction as a part of orthodontic treatment. Self-ligating and conventional brackets were bonded using a split-mouth study design randomly. Retraction of canines was done with 150 grams of force using Dontrix gauge with E-chains. The study was conducted in relation to upper arch only, while the rate of retraction was evaluated every 4 weeks for 3 months. Average rates of retraction in 3 months were calculated. For anchorage loss, an acrylic guide plug was used in mid-treatment cast (T0) and after 3 months of retraction (T3). The statistical analysis was done using Statistical Package for Social Sciences (SPSS) version 17.0 (SPSS Inc., Chicago, IL, USA). Independent t-test was used to compare the means of the two variables studied, while Pearson's correlation coefficient was used to evaluate the correlation between the variables studied in the groups included. P < .05 was considered statistically significant.
RESULTS: The correlation coefficient between the average rate of canine retraction with self-ligating brackets vs. conventional brackets over a period of 3 months came out to be 0.6434, while on comparing the data in terms of anchorage loss over a period of 3 months, the respective correlation coefficient value was found to be 0.6659 with the results being statistically highly significant in either case (P < .001).
CONCLUSIONS: Self-ligating brackets showed double the amount of displacement compared to conventional brackets in some of the cases. Also, chair side time was significantly reduced with self-ligating brackets as against conventional brackets
Phosphotyrosine profiling of curcumin-induced signaling
No full textBackground: Curcumin, derived from the rhizome Curcuma longa, is a natural anti-cancer agent and has been shown to inhibit proliferation and survival of tumor cells. Although the anti-cancer effects of curcumin are well established, detailed understanding of the signaling pathways altered by curcumin is still lacking. In this study, we carried out SILAC-based quantitative proteomic analysis of a HNSCC cell line (CAL 27) to investigate tyrosine signaling in response to curcumin. Results: Using high resolution Orbitrap Fusion Tribrid Fourier transform mass spectrometer, we identified 627 phosphotyrosine sites mapping to 359 proteins. We observed alterations in the level of phosphorylation of 304 sites corresponding to 197 proteins upon curcumin treatment. We report here for the first time, curcumin-induced alterations in the phosphorylation of several kinases including TNK2, FRK, AXL, MAPK12 and phosphatases such as PTPN6, PTPRK, and INPPL1 among others. Pathway analysis revealed that the proteins differentially phosphorylated in response to curcumin are known to be involved in focal adhesion kinase signaling and actin cytoskeleton reorganization. Conclusions: The study indicates that curcumin may regulate cellular processes such as proliferation and migration through perturbation of the focal adhesion kinase pathway. This is the first quantitative phosphoproteomics-based study demonstrating the signaling events that are altered in response to curcumin. Considering the importance of curcumin as an anti-cancer agent, this study will significantly improve the current knowledge of curcumin-mediated signaling in cancer.</p
MOESM3 of Phosphotyrosine profiling of curcumin-induced signaling
No full textAdditional file 3: Table S2. A list of phosphopeptides quantitated by SILAC
MOESM1 of Phosphotyrosine profiling of curcumin-induced signaling
No full textAdditional file 1: Figure 1. (A) Cell viability of CAL 27 with indicated concentrations of curcumin. Classification of differentially phosphorylated proteins based on (B) Localization (C) Biological process (D) Molecular function
Integrating transcriptomic and proteomic data for accurate assembly and annotation of genomes
No full textComplementing genome sequence with deep transcriptome and proteome data could enable more accurate assembly and annotation of newly sequenced genomes. Here, we provide a proof-of-concept of an integrated approach for analysis of the genome and proteome of Anopheles stephensi, which is one of the most important vectors of the malaria parasite. To achieve broad coverage of genes, we carried out transcriptome sequencing and deep proteome profiling of multiple anatomically distinct sites. Based on transcriptomic data alone, we identified and corrected 535 events of incomplete genome assembly involving 1196 scaffolds and 868 protein-coding gene models. This proteogenomic approach enabled us to add 365 genes that were missed during genome annotation and identify 917 gene correction events through discovery of 151 novel exons, 297 protein extensions, 231 exon extensions, 192 novel protein start sites, 19 novel translational frames, 28 events of joining of exons, and 76 events of joining of adjacent genes as a single gene. Incorporation of proteomic evidence allowed us to change the designation of more than 87 predicted "noncoding RNAs" to conventional mRNAs coded by protein-coding genes. Importantly, extension of the newly corrected genome assemblies and gene models to 15 other newly assembled Anopheline genomes led to the discovery of a large number of apparent discrepancies in assembly and annotation of these genomes. Our data provide a framework for how future genome sequencing efforts should incorporate transcriptomic and proteomic analysis in combination with simultaneous manual curation to achieve near complete assembly and accurate annotation of genomes.</p
A draft map of the human proteome
No full textThe availability of human genome sequence has transformed biomedical research over the past decade. However, an equivalent map for the human proteome with direct measurements of proteins and peptides does not exist yet. Here we present a draft map of the human proteome using high-resolution Fourier-transform mass spectrometry. In-depth proteomic profiling of 30 histologically normal human samples, including 17 adult tissues, 7 fetal tissues and 6 purified primary haematopoietic cells, resulted in identification of proteins encoded by 17,294 genes accounting for approximately 84% of the total annotated protein-coding genes in humans. A unique and comprehensive strategy for proteogenomic analysis enabled us to discover a number of novel protein-coding regions, which includes translated pseudogenes, non-coding RNAs and upstream open reading frames. This large human proteome catalogue (available as an interactive web-based resource at http://www.humanproteomemap.org) will complement available human genome and transcriptome data to accelerate biomedical research in health and disease.</p
