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1.
Chinese Journal of Oncology ; (12): 547-549, 2011.
Article in Chinese | WPRIM | ID: wpr-320174

ABSTRACT

<p><b>OBJECTIVE</b>To summarize the experience in diagnosis and treatment of primary tracheal tumors, and to improve the life quality of patients.</p><p><b>METHODS</b>Sixty-three patients with primary tracheal tumors treated in the First Affiliated Hospital of China Medical University during the past 40 years were included in this study, among them, there were 42 cases of malignant tumors and 21 cases of benign tumors. The 61 patients underwent surgery including tracheal sleeve resection (22), carinal resection and reconstruction (6), semi-carinal resection and reconstruction (6), tracheal resection for tracheal tumors (17); tracheostomy (4), tracheal resection, partial resection of the thyroid (goiter) and esophagomyotomy (1), tracheal tumor resection and vertical hemilaryngectomy with reconstruction of laryngeal ventricle and trachea by sternocleidomastoid flap (2), cervical trachea and laryngeal resection (1), and carinal scrape (2).</p><p><b>RESULTS</b>Fifty-five patients had an uneventful recovery. Eight patients suffered from postoperative complications, among them 3 patients died postoperatively.</p><p><b>CONCLUSIONS</b>Primary tracheal tumors often present atypical symptoms, are easily misdiagnosed and with poor prognosis. The main aim of treatment remains to remove the airway obstruction.</p>


Subject(s)
Adolescent , Adult , Aged , Aged, 80 and over , Female , Humans , Male , Middle Aged , Young Adult , Carcinoma, Adenoid Cystic , Diagnosis , General Surgery , Carcinoma, Squamous Cell , Diagnosis , General Surgery , Chondroma , Diagnosis , General Surgery , Follow-Up Studies , Neoplasm Recurrence, Local , Papilloma , Diagnosis , General Surgery , Postoperative Complications , Plastic Surgery Procedures , Methods , Survival Rate , Tracheal Neoplasms , Diagnosis , General Surgery , Tracheotomy , Methods
2.
Journal of Southern Medical University ; (12): 166-168, 2008.
Article in Chinese | WPRIM | ID: wpr-293426

ABSTRACT

<p><b>OBJECTIVE</b>To express human platelet-derived growth factor (hPDGF) B chain mature peptide gene in a prokaryotic expression system and detect the bioactivity of the expressed protein.</p><p><b>METHODS</b>hPDGF B chain mature peptide gene was amplified and expressed in E. coli, and the recombinant protein, rhPDGF-BB, was purified and renatured in GSSG/GSS system. The bioactivity of rhPDGF-BB in vitro was evaluated with SD rat osteoblasts.</p><p><b>RESULTS</b>The full-length PDGF-B mature peptide gene was obtained and verified, and successfully expressed in E. coli. Bioactivity detection results showed that the expressed rhPDGF-BB obviously promoted the proliferation and DNA replication of SD rat osteoblasts in vitro (P<0.01).</p><p><b>CONCLUSION</b>he PDGF-B chain mature peptide cDNA has been successfully cloned and the PDGF-B precursor highly expressed in E. coli, and renatured rhPDGF-BB displays high bioactivity as shown by MTT assay and flow cytometry. This success provides the basis for production of functional PDGF-BB and facilitates further studies of its role in fracture healing and trauma reconstruction.</p>


Subject(s)
Animals , Humans , Rats , Cell Proliferation , Cells, Cultured , DNA Replication , Escherichia coli , Genetics , Genetic Vectors , Osteoblasts , Metabolism , Proto-Oncogene Proteins c-sis , Genetics , Rats, Sprague-Dawley , Recombinant Proteins , Genetics
3.
Journal of Southern Medical University ; (12): 1838-1840, 2007.
Article in Chinese | WPRIM | ID: wpr-281527

ABSTRACT

<p><b>OBJECTIVE</b>To provide insights into the mechanisms and pathways of osteogensis by observing the effects of water-soluble matrix of nacre (WSM) on bone morphogenetic protein-2 (BMP-2) and Cbfa1 gene expressions in rabbit marrow mesenchymal stem cells (BMSCs).</p><p><b>METHODS</b>New Zealand rabbit BMSCs cultured in vitro were stimulated with different concentrations of WSM extracted at low temperature, and the activity of AKP in the cells was evaluated with the dose-effect curve generated. BMP-2 and Cbfa1 gene expressions in rabbit BMSCs exposed to WSM were assayed with one-step RT-PCR.</p><p><b>RESULTS</b>The activity of AKP in rabbit BMSCs increased after stimulation with different concentrations of WSM, and the effects were the most obvious with the WSM concentration ranging from 150 to 200 microg/ml. BMP-2 gene expression in the BMSCs increased after WSM exposure, but which did not result in obvious changes in Cbfa1 gene expression.</p><p><b>CONCLUSION</b>WSM induces differentiation of rabbit BMSCs towards osteoblasts by increasing BMP-2 gene expression, in which process Cbfa1 gene does not seem to play a significant role.</p>


Subject(s)
Animals , Rabbits , Biological Factors , Pharmacology , Bone Marrow Cells , Metabolism , Bone Morphogenetic Protein 2 , Metabolism , Calcium Carbonate , Pharmacology , Cell Differentiation , Cells, Cultured , Core Binding Factor Alpha 1 Subunit , Metabolism , Mesenchymal Stem Cells , Metabolism , Reverse Transcriptase Polymerase Chain Reaction
4.
Chinese Journal of Oncology ; (12): 289-292, 2007.
Article in Chinese | WPRIM | ID: wpr-255662

ABSTRACT

<p><b>OBJECTIVE</b>To investigate the characteristics of SKP2 protein expression in lung carcinoma tissues and its implication for prognosis.</p><p><b>METHODS</b>The expression of SKP2 protein was detected in 89 NSCLC, 13 SCLC, 5 benign lung neoplasms, 5 normal bronchus and lung tissues by tissue chip and immunohistochemical techniques.</p><p><b>RESULTS</b>The positive rate of SKP2 staining was (23.52 +/-13.57)% in NSCLC tissues and (53.85 +/- 12.26)% in SCLC tissues, significantly higher than (2.91 +/- 1.27)% in benign lung neoplasms and normal bronchus and lung tissues. Its expression was highest in SCLC tissues and lowest in benign lung tissues, with a significant difference between them (P <0.01). The expressive level of SKP2 protein in lung carcinoma tissues was closely related to cell differentiation and lymph node metastasis, but not to age, sex, smoking history, tumor site and size, and TNM staging, etc. The survival analysis revealed that the 5-year survival rate of lung carcinoma patients was much lower in SKP2 protein positive expression group than that in negative expression group (P < 0.01).</p><p><b>CONCLUSION</b>The positive expression of SKP2 protein is higher in lung carcinoma than in benign or normal lung tissues, in particular, much higher in SCLC tissue. Moreover, it may be an independent factor to exert negative influence on prognosis of patients with lung carcinoma.</p>


Subject(s)
Adolescent , Adult , Aged , Female , Humans , Male , Middle Aged , Bronchi , Chemistry , Pathology , Carcinoma, Non-Small-Cell Lung , Metabolism , Pathology , Carcinoma, Small Cell , Metabolism , Pathology , Immunohistochemistry , Lung , Chemistry , Pathology , Lung Neoplasms , Metabolism , Pathology , Lymphatic Metastasis , Neoplasm Staging , Prognosis , S-Phase Kinase-Associated Proteins , Metabolism , Survival Analysis
5.
Chinese Journal of Surgery ; (12): 1170-1173, 2004.
Article in Chinese | WPRIM | ID: wpr-345106

ABSTRACT

<p><b>OBJECTIVE</b>To acquire sufficient PDGF-BB protein and provide the basis for the further studies of its role on the fracture healing and trauma reconstruction and its clinical applications.</p><p><b>METHODS</b>Constructed the prokaryotic expression vector pQE-PDGF-B with the gene rearrangement technique, and the monomeric form of recombinant PDGF-B expressed in E. coli M15.</p><p><b>RESULTS</b>PDGF-B mature peptide gene was inserted into prokaryotic expression vector pQE30, which was confirmed by PCR, enzyme digestion and sequencing identification; the expressed products of pQE-PDGF-B in E. coli showed a single protein on SDS-PAGE, and their expression level was about 15% of the total bacterial protein. The molecular weight of the purified PDGF-B protein was about 15 KDs on SDS-PAGE.</p><p><b>CONCLUSIONS</b>The construction of recombinant plasmid and preparation of the monomeric protein of PDGF-B provides a solid foundation for further studying the function of PDGF-BB and producing biologically PDGF-BB protein.</p>


Subject(s)
Humans , Cloning, Molecular , Escherichia coli , Genetics , Metabolism , Genetic Vectors , In Vitro Techniques , Platelet-Derived Growth Factor , Genetics , Proto-Oncogene Proteins c-sis , Genetics , Recombinant Proteins , Genetics , Transfection
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