Objective: To investigate the expression of cortactin in colorectal cancer and its correlation with clinicopathological parameters and prognosis. Methods: The expressions of cortactin in normal colorectal mucosal tissue and colorectal cancer tissue in paraffin-embedded tissue microarray from 319 patients who were diagnosed as colorectal cancer and treated in Cancer Hospital of Chinese Academy of Medical Sciences from 2006 to 2009 was detected by immunohistochemistry. Kaplan-Meier method and Log rank test were used for survival analysis, and Cox proportional risk regression model was used for multivariate analysis. Results: The positive expression rates of cortactin in colorectal cancer tissue and normal colorectal mucosal tissue were 61.1% (195/319) and 5.6% (18/319, P<0.001), respectively. T-stage, N-stage, American Joint Committee on Cancer (AJCC) stage, degree of tumor differentiation, neural invasion and preoperative carcinoembryonic antigen (CEA) levels were associated with the expression of cortactin (P<0.05). The positive expression of cortactin was associated with poorer disease-free survival (P=0.036) and overall survival (P=0.043), and the effect was more significant in patients with stage Ⅱ to Ⅲ. For patients with stage Ⅱ-Ⅲ colorectal cancer, postoperative adjuvant therapy was associated with disease-free survival (P=0.007) and overall survival (P=0.015). The vascular tumor embolus, pathological type, preoperative CEA level and cortactin expression were independent influencing factors for disease-free survival (P<0.05). The age, AJCC stage, preoperative CEA level and cortactin expression were independent influencing factors for overall survival (P<0.05). Preoperative CEA level and cortactin expression were independent influencing factors for disease-free survival and overall survival (P<0.05). Conclusion: Cortactin is expressed in colorectal cancer and in stage Ⅱ-Ⅲ patients, it is a potential predictor of colorectal cancer prognosis.
Biomarkers, Tumor/metabolism* ; Carcinoembryonic Antigen/metabolism* ; Colorectal Neoplasms/pathology* ; Cortactin/metabolism* ; Humans ; Prognosis ; Retrospective Studies

OBJECTIVE: To investigate the expression of EMS1 in laryngeal carcinoma and its clinical significance. METHOD: The expression of EMS1 protein was measured in 40 samples of, 40 samples of para carcinoma tissues (which were near to cutting margin of laryngeal carcinoma tissue over 0.5 cm), and 20 samples of normal laryngeal mucosa as controls by Flow Cytometer (Epics-XL II). RESULT: The quantity and percentage of EMS1 protein expression in laryngeal carcinoma tissues was significantly higher than those in para carcinoma and in normal laryngeal mucosa tissues respectively (P<0.05). There was no significant expression difference between the para carcinoma tissues and normal laryngeal mucosa tissues. There were positive correlation between the expressions of EMS1 protein and metastasis, pathological grade and clinical stage in laryngeal carcinoma. But there were not relationship with patients' clinical classification, tumor size, smoking history, age and sex. CONCLUSION The high expression of EMS1 may contribute to the carcinogenesis and development of laryngeal carcinoma. The expression of EMS1 protein is an important index of judging differentiation, infiltration, metastasis and staging of laryngeal carcinoma.
Adult ; Aged ; Carcinoma, Squamous Cell ; metabolism ; pathology ; Cortactin ; metabolism ; Female ; Humans ; Laryngeal Mucosa ; metabolism ; pathology ; Laryngeal Neoplasms ; metabolism ; pathology ; Male ; Middle Aged ; Neoplasm Staging

OBJECTIVE: To investigate the expression of EMS1 and DcR3 in laryngeal carcinoma and analyze the relation of EMS1 and DcR3. METHOD: The expression of EMS1 and DcR3 protein in 41 laryngeal carcinoma fresh samples and 41 para-carcinoma tissues (to cutting margin > 0.5 cm) were measured by flow cytometry, and 15 normal laryngeal mucosa samples were also studied as controls. RESULT: (1) The quantitative and qualitative expression of EMS1 and DcR3 protein in laryngeal carcinoma tissues was obviously higher than those in para-carcinoma and in normal laryngeal mucosa tissues respectively (P < 0.05). There was no significant difference between the expression of para-carcinoma and normal laryngeal mucosa tissues. (2) In laryngeal carcinoma, the expression of EMS1 and DcR3 protein was independent of patients' clinical classification, tumor size, smoking history, patients' age and sex but associated with tumor metastasis, pathological grade and clinical stage. (3) In laryngeal carcinoma, the expression of EMS1 was positively correlated with that of DcR3. CONCLUSION EMS1 was positively related to DcR3, which might play an important role in the carcinogenesis and development of laryngeal carcinoma by synergic effect.
Adult ; Aged ; Cortactin ; metabolism ; Female ; Flow Cytometry ; Humans ; Laryngeal Neoplasms ; metabolism ; pathology ; Male ; Middle Aged ; Neoplasm Staging ; Receptors, Tumor Necrosis Factor, Member 6b ; metabolism

Objective: To investigate the effect of adenovirus-mediated shRNA down-regulating phosphatase and tensin homolog deleted on chromosome 10 (PTEN) expression on vinculin, filamin A, and cortactin in activated hepatic stellate cells (HSCs). Methods: Activated rats hepatic stellate cell line (HSC-T6) was cultured in vitro. Recombinant adenovirus Ad-shRNA/PTEN carrying PTEN targeted RNA interference sequence [short hairpin RNA (shRNA)] and empty control virus Ad-GFP were transfected into HSCs. The PTEN mRNA and protein expression of HSCs in each group were detected by real-time fluorescence quantitative PCR and Western blot. The expressional change of vinculin, filamin A and cortactin in HSCs of each group were detected by confocal laser scanning immunofluorescence microscope. Image-pro plus 6.0 software was used for image analysis and processing. The integrated optical density (IOD) of the fluorescence protein expression was measured. The experiment was divided into three groups: control group (DMEM instead of adenovirus solution in the adenovirus transfection step), Ad-GFP group (transfected with empty virus Ad-GFP only expressing green fluorescent protein), and Ad-shRNA/PTEN group (recombinant adenovirus Ad-shRNA/PTEN carrying shRNA targeting PTEN and expressing green fluorescent protein). One-way analysis of variance was used for comparison of mean value among the three groups, and LSD-test was used for comparison between the groups. Results: shRNA targeted PTEN was successfully transfected and the expression of PTEN mRNA and protein in HSC (P < 0.05) was significantly down-regulated. HSCs vinculin was mainly expressed in the cytoplasm. HSCs vinculin fluorescence IOD in the Ad-shRNA/PTEN group (19 758.83 ± 1 520.60) was higher than control (7 737.16 ± 279.93) and Ad-GFP group (7 725.50 ± 373.03) (P < 0.05), but there was no statistically significant difference between control group and Ad-GFP group (P > 0.05). There was no statistically significant difference in the fluorescence IOD of Filamin A among the three groups (P > 0.05), but the subcellular distribution of Filamin A among the three groups were changed. Filamin A in the Ad-shrNA /PTEN HSC group was mainly distributed in the cytoplasm. Filamin A HSC was mainly located in the nucleus.The filamin A HSC in the control group and Ad-GFP group was mainly located in the nucleus. The nucleocytoplasmic ratio of Filamin A in the AD-shrNA /PTEN group (0.60 ± 0.15) was significantly lower than control group (1.20 ± 0.15) and Ad-GFP group (1.08 ± 0.23), P < 0.05. but there was no statistically significant difference in filamin A nucleocytoplasmic ratio of HSC between the control group and the Ad-GFP group (P > 0.05). Cortactin HSCs in the three groups was mainly distributed in the cytoplasm. The cortactin fluorescence IOD of HSCs in the Ad-shRNA/PTEN group was significantly higher than control group (22 959.94 ± 1 710.42) and the Ad-GFP group (22 547.11 ± 1 588.72 ) (P < 0.05), while there was no statistically significant difference in the IOD of cortactin fluorescence in HSCs between the control group and the Ad-GFP group (P > 0.05). Conclusion: The down-regulation of PTEN expression raises the expression of microfilament-binding protein vinculin and cortactin, and changes the subcellular distribution of another microfilament binding protein filamin A, that is, translocation from nucleus to the cytoplasm in activated HSC in vitro.
Adenoviridae/metabolism* ; Animals ; Carrier Proteins ; Cell Proliferation ; Cortactin ; Filamins/genetics* ; Hepatic Stellate Cells/metabolism* ; PTEN Phosphohydrolase/metabolism* ; RNA, Small Interfering/genetics* ; Rats ; Vinculin/genetics*