[Expressions and clinical significance of caveolin-1 gene and protein in tongue squamous cell carcinoma].

PURPOSE: To investigate the changes and the significance of caveolin-1 gene and protein in tongue squamous cell carcinoma(TSCC). METHODS: Immunohistochemical staining and in situ hybridization were used to detect the changes of caveolin-1 gene and the protein in 92 TSCCs and their adjacent normal tissues. The data were analyzed with SPSS10.0 software package. RESULTS: The expressions of caveolin-1 gene(24.6+/-1.8) and its protein(471.2+/-68.1) in TSCC were lower than those of the control group(167.2+/-20.5, 964.5+/-77.2), respectively. The difference was significant(P<0.01). The expression of caveolin-1 protein in well-differentiated TSCC(5.6+/-1.4) was higher than that in moderately and poorly differentiated TSCC(1.3+/-0.8); The expression of caveolin-1 protein in stage I-II patients(6.1+/-2.0) was higher than that in stage III-IV patients(2.4+/-0.7), and the difference was significant(P<0.01). There was no significant relationship between the expression of caveolin-1 protein and cervical lymph node metastasis(P>0.05). CONCLUSIONS: The level of caveolin-1 gene and the expression of the protein decrease in TSCC and the level of protein has a significant relationship with the clinical stage and the pathological grade, rather than the cervical lymph node metastasis.

[Cell apoptosis and the change of Fas/FasL gene in experimental pulmonary fibrosis].

OBJECTIVE: To investigate the changes and significance of cell apoptosis and Fas/FasL gene in pulmonary fibrosis. METHODS: Forty mice were divided into two groups randomly, each group contained twenty mice. TUNEL, immunohistochemistry and in situ hybridization were used to detect the change of cell apoptosis, Fas/FasL mRNA and protein in mice with pulmonary fibrosis caused by bleomycin. RESULTS: The apoptosis index of lung cells in the pulmonary fibrosis group (55.3 +/- 12.2) was higher than that of control group (4.7 +/- 1.0, t = 13.06, < 0.01). The expression of Fas/FasL mRNA (175.8 +/- 21.6, 5.2 +/- 1.6) and protein (956 +/- 96, 285 +/- 76) in the pulmonary fibrosis group was higher than that of control group (mRNA: 26.6 +/- 1.9, 0.5 +/- 0.4, t = 21.7, 8.79, all < 0.01; protein: 491 +/- 96, 100 +/- 18, t = 5.03, 12.81, < 0.01). CONCLUSION: The apoptosis index of lung cells, Fas/FasL genes and protein were up-regulated in lung tissue of pulmonary fibrosis, which may play an important role in the development of disease.

[Change of prostaglandin E2 and interleukin-12, interleukin-13 in the bronchoalveolar lavage fluid and the serum of the patients with idiopathic pulmonary fibrosis].

OBJECTIVE: To detect the levels of prostaglandin E2 (PGE2) and interleukin-12 (IL-12), IL-13 in the bronchoalveolar lavage fluid (BALF) and the serum of patients with idiopathic pulmonary fibrosis (IPF) and to investigate the significance of their change in the pathogenesis of IPF. METHODS: Radioimmunoassay (RIA) and enzyme-linked immunoadsorbent assay (ELISA) were used to detect the levels of PGE2 and IL-12, IL-13 in the BALF and the serum of patients with IPF. RESULTS: In the BALF of patients with IPF, the levels of PGE2 (591 +/- 88) ng/L and IL-13 (38 +/- 5) ng/L were higher than that of the control group (P < 0.01), and the level of IL-12 (1.34 +/- 0.25) ng/L was lower than that of control group. In the patients with IPF, the change of IL-13 in the serum was consistent with the change in the BALF. But the levels of PGE2 (235 +/- 13) ng/L and IL-12 (2.35 +/- 0.14) ng/L in the serum showed no significant difference between the patients with IPF and the control group. CONCLUSIONS: In the patients with IPF the increase of PGE2 may be correlated with the increase of IL-13 and the decrease of IL-12. It suggests that disequilibrium of Th1/Th2 plays an important role in the development of IPF. The increase of PGE2 in IPF is a local event rather than a systemic effect.

[Inhibitory effect of p53 with deletion of c-terminal 356 - 393 amino acids on malignant phenotype of human lung cancer cell line].

OBJECTIVE: To study the effect of extraneous p53 gene with deletion of c-terminal 356 - 393 amino acids on inhibition of malignant phenotype of human lung cancer cell line. METHODS: Recombinant plasmid pEGFP-p53 (del) with codon deletion of c-terminal 37 amino acids from 393 to 356 region and pEGFP-p53 (wild type) were constructed. The human lung cancer cell line 801D served as a receipt cell had p53 deletion and mutation at 248 codon. 801D cells, having been transfected by pEGFP-p53 (wild type), pEGFP-p53 (del) or pEGFP, were selected by G418. Growing transfected cells were cloned respectively by method of dilution. Presence of extraneous gene was detected by PCR, their expression in cells was examined by fluorescence microscopy. Cloning efficiency was in vitro tested to examine the cellular proliferating ability. The xenograft in nude mice was performed and xenograft tumors were weighed one month later. Expression of GFP in tumor and transplanted cellular mass were detected by blot slices. RESULTS: pEGFP-p53 (del)-801D, pEGFP-p53-801D and pEGFP-801D were established. Extraneous p53 gene and expression of GFP were found in pEGFP-p53 (del)-801D and pEGFP-p53-801D. Inhibitory rate of colony was 99.6% for pEGFP-p53 (del)-801D and 81.0% for pEGFP-p53-801D. Inhibition of malignant proliferation of extraneous p53 (del) was higher than that of p53 (wild type) (P < 0.01). Even when inhibition of malignant proliferation extraneous pEGFP-p53 (del) was obvious, 0.2% colonies were formed, extraneous p53 and expression of GFP were observed. Animal test showed that tumor on the nude mice was positive (4/4, 4/4) in the control group (801D and pEGFP-801D), but negative (0/4, 0/4) in the experiment group [pEGFP-p53 (del) 801D and pEGFP-p53 (wild type) 801D]. Expression of GFP in the cells of cellular mass transplanted by pEGFP-p53 (del) 801D or pEGFP-p53 (wild type) 801D was observed. CONCLUSION: In vitro inhibitory effect of extraneous p53 gene with deletion of C-terminal 356 - 393 amino acids on malignant growth of lung cancer cell with p53 mutation or deletion at 248 codon is marked. Inhibitory action of p53 on malignant proliferation of cancer cells is heterogeneous.