Publications (6)7.87 Total impact
-
Article: Prognostic value of matrix metalloproteinase-1/ proteinase-activated receptor-1 signaling axis in hepatocellular carcinoma.
[show abstract] [hide abstract]
ABSTRACT: Matrix metalloproteinase-1 (MMP-1) is proposed to be involved in both tumor cell invasion and metastasis. MMP-1 proteolytically activates protease activated receptor-1 (PAR-1), which also plays an important role in tumor development and progression. However, it is currently unknown whether MMP-1 activation of PAR-1 has relevance to the progression of hepatocellular carcinoma (HCC). To address this problem, we investigate the clinicopathological and prognostic value of MMP-1/PAR-1 signaling axis in HCC. Immunohistochemistry assay was used to determine the expression of MMP-1 and PAR-1 proteins in normal and HCC tissues. The correlations of MMP-1 and PAR-1 expression with clinicopathological parameters were assessed by Chi-squared test. Patient survival and their differences were determined by Kaplan-Meier method and log-rank test. Cox regression was adopted for multivariate analysis of prognostic factors. MMP-1 and PAR-1 immunoreactivities were negative or low in normal liver tissues, but high in HCC tissues. PAR-1 expression was significantly correlated with that of MMP-1 (r = 0.896, p < 0.0001). The overexpression of MMP-1 and PAR-1 was significantly associated with recurrence, TNM staging and portal vein invasion of HCC. Patients with high MMP-1 and PAR-1 expression had significantly poorer overall survival (OS) (both P < 0.001) and disease-free survival (DFS) (both P < 0.001) when compared with patients with the low expression of MMP-1 and PAR-1. On multivariate analysis, MMP-1 and PAR-1 expression patterns were found to be independent prognostic factors for OS (both P < 0.001) and DFS (both P < 0.001). Our results suggest for the first time that the MMP-1/PAR-1 signaling axis might be applied as a novel marker for the prediction of recurrence and metastasis potency and a significant indicator of poor prognosis for patients with HCC.Pathology & Oncology Research 09/2011; 18(2):397-403. · 1.37 Impact Factor -
Article: [Expression of HSP70/HSP27 protein in residual lesion after NPC radiotherapy].
[show abstract] [hide abstract]
ABSTRACT: To analyze HSP70/HSP27 protein expression in the nasopharyngeal carcinoma (NPC) primary tissues and the residual lesion, and to explore its predictive value. Immunohistochemical experiment was performed to detect the expression of HSP70 and HSP27 in 58 NPC primary tissues: 28 were in the experimental group with the local residual lesion and 30 in the control group without recurring and metastasis within 5 years by conventional radiotherapy. The positive expression of HSP70 and HSP27 in the experimental group was 92.9%(26/28) and 53.6%(15/28), while that in the control group was 53.3%(16/30) and 53.3%(16/30),respectively. There was significant difference in the 2 groups. The common positive expression of HSP70 and HSP27 between the 2 groups had significant difference, 50.0% (14/28) in the experimental group and 16.7% (5/30) in the control group, respectively. There was no significant difference in the negative ratio of HSP70 and HSP27 common expression between the 2 groups, 3.6% (1/28) in the experimental group and 10.0% (3/30) in the control group, respectively. HSP70 may have an important role in the radioresistance of NPC, and may predict the residual lesion after radiotherapy.Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences 11/2009; 34(11):1091-5. -
Article: A reference map of human nasopharyngeal squamous carcinoma proteome.
[show abstract] [hide abstract]
ABSTRACT: In order to conduct a comparative proteomics study of human nasopharyngeal carcinoma (NPC) to understand the molecular mechanisms that participate in the formation of NPC, the two-dimensional gel electrophoresis (2-DE) reference map of human NPC tissue proteome was described. To provide a high level of reproducibility between gels and accurately array each protein expressed in NPC tissue proteome, the two-dimensional polyacrylamide gel electrophoresis system, modified colloidal Coomassie Brilliant Blue staining method and ImageMaster 2D Platinum image analysis software were used. The NPC 2-DE maps show that high quality and good reproducibility of the 2-DE gel pattern was attained. An average total of 1,100 protein spots were separated by 2-DE, visualized by a modified colloidal Coomassie Brilliant Blue staining method. A synthesized 2-DE reference gel was acquired after detailed analysis of the NPC 2-DE gel maps, and 216 medium to high abundant spots were identified as landmark spots of NPC 2-DE gel, which expressed on >75% of gels. To provide an unambiguous identification of the landmark spots in gels, MALDI-TOF, ESI-Q-TOF mass spectrometry and database search were used to identify the proteins expressed in NPC tissue proteome. Between the 216 landmark spots, all proteins were identified with MALDI-TOF at first, 41 of which were identified with both MALDI-TOF and ESI-Q-TOF. All identified proteins were classified in terms of their subcellular localization and physiological function with information from SWISS-PROT and NCBI websites. According to our knowledge this is the first 2-DE reference map of human NPC. This reference map will serve as a basis for further studies of human NPC and the reference map data will be used to expand the proteome database of human NPC, which can be accessed in our website (http://www.xyproteomics.org/).International Journal of Oncology 05/2007; 30(5):1077-88. · 2.40 Impact Factor -
Article: Differential analysis of two-dimension gel electrophoresis profiles from the normal-metaplasia-dysplasia-carcinoma tissue of human bronchial epithelium.
[show abstract] [hide abstract]
ABSTRACT: Processes involved in malignant transformation of the lung from preneoplasia are poorly understood. To better understand this process, two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) profiles of proteins from the normal, metaplasia, dysplasia and carcinoma tissues of human bronchial epithelia were examined by differential proteomic analysis. The selected differential protein-spots were identified by peptide mass fingerprint based on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and database searching. The average spots for normal epithelium, metaplasia, dysplasia and invasive carcinoma were 1189.50 +/- 39.89, 1227.00 +/- 37.90, 1273.00 +/- 43.31 and 1326.00 +/- 66.63, respectively. Well-resolved, reproducible 2-D PAGE patterns of the normal-metaplasia-dysplasia-carcinoma tissues of bronchial epithelia were obtained. After matching, the number of spots of differential proteins between normal tissue and metaplasia, metaplasia and dysplasia, and dysplasia and invasive cancer tissues were 31.50 +/- 7.67, 41.00 +/- 9.07 and 56.00 +/- 8.96, respectively. In total, 35 differential proteins, expressed only at the later stage of a two-stage comparison, were identified, some of which are known to be involved in regulating the processes of proliferation, differentiation and signal transduction. Current data in this study, for the first time, provide the basis for identification of potential tumor markers of human lung squamous carcinoma and their involvement in the progression of malignant transformation of bronchial epithelium.Pathology International 11/2004; 54(10):765-73. · 1.62 Impact Factor -
Article: Comparative proteomics analysis of human lung squamous carcinoma.
[show abstract] [hide abstract]
ABSTRACT: Two-dimensional polyacrylamide gel electrophoresis (2-DE) profiles of human lung squamous carcinoma tissue and paired surrounding normal bronchial epithelial tissue were compared. Selected differential protein-spots were identified with peptide mass fingerprinting based on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and database searching. Well-resolved and reproducible 2-DE patterns of both the tumor and the normal tissues were acquired. The average deviations of spot position were 0.873+/-0.125mm in IEF direction and 1.025+/-0.213mm in SDS-PAGE direction, respectively. For the tumor tissues, a total of 1349+/-67 spots were detected and 1235+/-48 spots were matched with an average matching rate of 91.5%. For the corresponding normal tissues, a total of 1297+/-73 spots were detected and 1183+/-56 spots were matched with an average matching rate of 91.2%. A total of 1069+/-45 spots were matched between the tumor and the normal tissues. Forty differential proteins between tumor and normal tissues were characterized. Some proteins were the products of oncogenes and others were involved in the regulation of cell cycle and signal transduction. These data are valuable for mass identification of differentially expressed proteins involved in lung carcinogenesis, establishing human lung cancer proteome database and screening molecular marker to further study human lung squamous carcinoma.Biochemical and Biophysical Research Communications 10/2003; 309(1):253-60. · 2.48 Impact Factor -
Article: Proteomic comparison of two-dimensional gel electrophoresis profiles from human lung squamous carcinoma and normal bronchial epithelial tissues.
[show abstract] [hide abstract]
ABSTRACT: Differential proteome profiles of human lung squamous carcinoma tissue compared to paired tumor-adjacent normal bronchial epithelial tissue were established and analyzed by means of immobilized pH gradient-based two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS). The results showed that well-resolved, reproducible 2-DE patterns of human lung squamous carcinoma and adjacent normal bronchial epithelial tissues were obtained under the condition of 0.75-mg protein-load. The average deviation of spot position was 0.733+/-0.101 mm in IEF direction, and 0.925+/-0.207 mm in SDS-PAGE direction. For tumor tissue, a total of 1241+/-88 spots were detected, 987+/-65 spots were matched with an average matching rate of 79.5%. For control, a total of 1190+/-72 spots were detected, and 875+/-48 spots were matched with an average matching rate of 73.5%. A total of 864+/-34 spots were matched between tumors and controls. Forty-three differential proteins were characterized: some proteins were related to oncogenes, and others involved in the regulation of cell cycle and signal transduction. It is suggested that the differential proteomic approach is valuable for mass identification of differentially expressed proteins involved in lung carcinogenesis. These data will be used to establish human lung cancer proteome database to further study human lung squamous carcinoma.Genomics Proteomics & Bioinformatics 03/2003; 1(1):58-67.
Top Journals
Institutions
-
2009
-
Central South University
Changsha, Hunan, China
-