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Yang J.,Xian Jiaotong University | Zhu J.,Shaanxi Provincial Tumor Hospital | He K.,Xian Jiaotong University | Zhao L.-Y.,Xian Jiaotong University | And 3 more authors.
Journal of Clinical Laboratory Analysis | Year: 2015

Aim: To reveal the serum proteomic profiling of intraductal carcinoma (IDC) patients in China, establish a serum proteome fractionation technique for choosing magnetic beads for proteomic analysis in breast cancer research; and identify differentially expressed peptides (m/z; P < 0.0001) as potential biomarkers of early IDCs. Methods: We used two different kinds of magnetic beads (magnetic bead-based weak cation exchange chromatography (MB-WCX) and immobilized metal ion affinity chromatography (MB-IMAC-Cu)) to analyze 32 patients with early stage (stages I-II) IDC and 32 healthy control serum samples for proteomic profiling by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) analysis. The mass spectra, analyzed using ClinProTools software, distinguished between IDC patients and healthy individuals based on k-nearest neighbor genetic algorithm. Results: The serum samples purified in the MB-WCX group provided better proteomic patterns than the MB-IMAC-Cu group. The samples purified by MB-WCX had better average peak numbers, higher peak intensities, and better capturing ability of low abundance proteins or peptides in serum samples. In addition, the MB-WCX and MB-IMAC-Cu purification methods, followed MALDI-TOF MS identification and use of ClinProTools software accurately distinguished patients with early stage IDC from healthy individuals. Conclusion: Serum proteomic profiling by MALDI-TOF MS is a novel potential tool for the clinical diagnosis of patients with IDC in China. © 2014 Wiley Periodicals, Inc. Source


Liu Y.,Shaanxi Provincial Tumor Hospital | Li H.,Xian XD Group Hospital | Zhang R.,Xian Mental Health Center | Dang H.,Xian Jiaotong University | And 5 more authors.
Gene | Year: 2016

BRCA1-interacting protein 1 (BRIP1), a DNA-dependent ATPase and a DNA helicase, is critical for BRCA-associated DNA damage repair functions and may be associated with the tumourigenesis and aggressiveness of various cancers. Here, we constructed a BRIP1 recombinant plasmid, overexpressed it in a cervical cancer cell line (HeLa) and found that ectopic expression of BRIP1 could remarkably enhance the antitumor activity of cisplatin, as demonstrated by decreased cell viability, colony formation and tumour xenografts' weight. Moreover, BRIP1 promoted cisplatin-mediated cell apoptosis and suppressed tumour angiogenesis. We also found that the synergistic inhibition effect of BRIP1 might be partially attributed to attenuation of Rac1 GTPase activation and that Rac1 GTPase re-activation could reverse the sensitizing effect induced by BRIP1. Our study suggested that up-regulation of BRIP1 could enhance chemosensitivity of HeLa cells to cisplatin through inhibiting Rac1 GTPase activation, and it provides a new insight into the essential role of BRIP1 in cervical cancer chemotherapy. © 2015 Elsevier B.V. Source


Yang J.,Xian Jiaotong University | Xiong X.,Xian Jiaotong University | Liu S.,Xian Jiaotong University | Zhu J.,Shaanxi Provincial Tumor Hospital | And 6 more authors.
Proteomics | Year: 2016

This study aimed to identify novel serum peptides biomarkers for female breast cancer (BC) patients. We analyzed the serum proteomic profiling of 247 serum samples from 96 BC patients, 48 additional paired pre- and postoperative BC patients, 39 fibroadenoma patients as benign disease controls, and 64 healthy controls, using magnetic-bead-based separation followed by MALDI-TOF MS. ClinProTools software identified 78 m/z peaks that differed among all analyzed groups, ten peaks were significantly different (P < 0.0001), with Peaks 1-6 upregulated and Peaks 7-10 downregulated in BC. Moreover, three peaks of ten (Peak 1, m/z: 2660.11; Peak 2, m/z: 1061.09; Peak 10, m/z: 1041.25) showed a tendency to return to healthy control values after surgery. And these three peptide biomarkers were identified as FGA605-629, ITIH4 347-356, and APOA2 43-52. Methods used in this study could generate serum peptidome profiles of BC, and provide a new approach to identify potential biomarkers for diagnosis as well as prognosis of this malignancy. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Source


Yuan Y.,Xian Jiaotong University | Zheng P.-S.,Xian Jiaotong University | Zhou M.,Xian Jiaotong University | Yao A.-M.,Shaanxi Provincial Tumor Hospital | Wang J.,Shaanxi Provincial Tumor Hospital
Journal of Xi'an Jiaotong University (Medical Sciences) | Year: 2014

Objective: To investigate the effects of transcription factor (Sp2) on the proliferation of cervical cancer Hela cells and the molecular mechanisms.Methods: The expression of Sp2 in cervical cancer tissues and effects of Sp2 siRNA on the expressions of Sp2 and Cyclin D1 RNA and protein were analyzed by Real-time PCR and Western Blot, respectively. MTT assay was used to analyze the effects of Sp2 on the proliferation of cervical cancer Hela cells. The effects of Sp2 on cell cycle and apoptosis of cervical cancer Hela cells were analyzed with flow cytometer.Results: Sp2 expression level was higher in human cervical cancer tissues than in normal cervical tissues. Sp2 siRNA inhibited the proliferation of cervical cancer Hela cells. The number of S and G2/M phase cells significantly decreased in Sp2 siRNA group compared with the control group (P<0.01). Meanwhile, the number of G1/G0 phase cells increased remarkably (P<0.01). It was found that Sp2 and Cyclin D1 expressions at the mRNA and protein levels downregulated significantly in Sp2 siRNA group compared with the control group (P<0.01).Conclusion: Sp2 promotes the proliferation of cervical cancer Hela cells through up-regulating Cyclin D1 expression. Source


Zhao W.-H.,Xian Jiaotong University | Chen J.,Shaanxi Provincial Tumor Hospital | Jing G.-X.,Xian Jiaotong University | Liu J.,Xian Jiaotong University | Dang X.-D.,Shaanxi Provincial Tumor Hospital
Journal of Xi'an Jiaotong University (Medical Sciences) | Year: 2014

Objective: To investigate the effects of propofol on the changes in myocardial Toll-like receptor 4 (TLR-4) and TNF-α and NF-κb protein expressions in ischemia-reperfusion injury (I/R). Methods: Thirty healthy male SD rats weighing 250-320 g were randomly divided into 3 groups (n=10 for each): Group A, sham operation; Group B, I/R; and Group C, propofol + I/R. In Groups B and C myocardial I/R was induced by occlusion of the left anterior descending artery (LAD) for 30 min, followed by 120 min reperfusion. In Group C propofol was given intravenously 10 min before myocardial ischemia, followed by continuous infusion of propofol at 5 mg/(kg·h) until the end of 120 min reperfusion. In Groups A and B normal saline instead of propofol was given. The myocardial tissues were taken at the end of 120 min; ultrastructural changes of myocardial cells were observed under X-ray electron microscope and the expressions of TLR-4 mRNA as well as TNF-α and NF-κb protein were determined. Results: Ultrastructural observation under electron microscope showed significantly worsened damage in myocardial tissue structure and mitochondria in Groups B and C compared with Group A. The myocardial expressions of TLR-4 and TNF-α and NF-κb protein were significantly higher in Groups B and C than in control Group A. The myocardial expressions of TLR-4 and TNF-α and NF-κb protein were down-regulated in Group C compared with Group B. Conclusion: Intravenous injection of propofol can protect against myocardial damage. Propofol can suppress the increase in myocardial TLR-4 and TNF-α and NF-κb protein expressions induced by I/R. Source

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