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1.
J Clin Exp Dent ; 11(3): e269-e274, 2019 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-31001398

RESUMO

BACKGROUND: The biological responses involved during retention phase have been studied for many years but little is known about the effect of saliva proteome during retention phase of post-orthodontic treatment. This study aims to identify the protein profiles during retention phase in relation to biological processes involved by Liquid Chromatography Mass Spectrometry (LC-MS) approach. MATERIAL AND METHODS: A total of 5 ml of unstimulated saliva was collected from each subject (10 non-orthodontic patients and 15 post-orthodontic patients with 6-months retention phase). Samples were then subjected to LC-MS analysis. The expressed proteins were identified and compared between groups. Incisor irregularity for both maxilla and mandible were determined with Little's Irregularity Index at 6-months retention phase. RESULTS: 146 proteins and 135 proteins were expressed in control and 6-months retention phase group respectively. 15 proteins were identified to be co-expressed between groups. Immune system process was only detected in 6-months retention phase group. Detected protein in immune system process was identified as Tyrosine-protein kinase Tec. Statistical significant of incisor irregularity was only found in mandible at 6-months retention phase. CONCLUSIONS: Our study suggests that immune system process protein which is Tyrosine-protein kinase Tec could be used as biomarker for prediction of stability during retention phase of post-orthodontic treatment. Key words:Orthodontics, proteomics, retention, LC-MS, saliva.

2.
Electrophoresis ; 29(12): 2645-50, 2008 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-18494030

RESUMO

A 35 kDa glycoprotein whose abundance was previously demonstrated to be enhanced in sera of patients with endometrial adenocarcinoma (n = 12), was isolated from pooled sera of three of the cancer patients using champedak galactose-binding lectin affinity chromatography in the present study. Subjecting it to 2-DE and MS/MS, the glycoprotein was identified as the O-glycosylated fragment of inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4). When compared to control sera (n = 17), expression of the 35 kDa ITIH4 cleavage fragment was demonstrated to be significantly enhanced in sera of patients with breast carcinoma (n = 10), epithelial ovarian carcinoma (n = 10), and germ cell ovarian carcinoma (n = 10) but not in patients with nasopharyngeal carcinoma (n = 13) and osteosarcoma (n = 7). The lectin-based electrophoretic bioanalytical method adopted in the present study may be used to assess the physiological relevance of ITIH4 fragmentation and its correlation with different malignancies, their stages and progression.


Assuntos
alfa-Globulinas/biossíntese , Biomarcadores Tumorais/biossíntese , Galectinas , Lectinas de Plantas , Adolescente , Adulto , Idoso , Biomarcadores Tumorais/sangue , Neoplasias Ósseas/metabolismo , Neoplasias da Mama/metabolismo , Eletroforese em Gel Bidimensional , Feminino , Glicosilação , Humanos , Masculino , Pessoa de Meia-Idade , Neoplasias Nasofaríngeas/metabolismo , Neoplasias Embrionárias de Células Germinativas/metabolismo , Neoplasias Epiteliais e Glandulares/metabolismo , Osteossarcoma/metabolismo , Neoplasias Ovarianas/metabolismo , Espectrometria de Massas em Tandem
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