[Management of chylous leakage after radical operation of gastric cancer].

OBJECTIVE: To investigate the management of chylous leakage after radical operation of gastric carcinoma. METHODS: 161 patients with gastric carcinoma underwent D2-D4 dissection. A double catheterization cannula was employed in each patient around the abdominal aorta above the celiac trunk and crus of diaphragm. Postoperatively, the chylous fluid from the drainage tube was observed, smeared and cultured; infection of chylous fluid was treated. The development of chylous leakage was observed and the optimal time to remove the drainage tube was determined. RESULTS: Chylous leakage occurred in 19 patients. The volume of chylous leakage was less than 250 ml/24 h in 8 patients, 250 - 500 ml/24 h in 7, and 500 - 1500 ml/24 h in 4. Candida albicans was founded in the fluid of chylous leakage in 8 patients, and bacterial infection was found simultaneously in 5 of them. The patients with chylous leakage were healed within 10 - 90 postoperative days. The drainage tube was removed when there was no fluid in the tube and no hydrops in peritoneal cavity by B ultrasound, and the patient were in good condition without signs and symptoms of infections. CONCLUSION: Chylous leakage after D2 - D4 dissection for gastric carcinoma can be cured by immediate diagnosis, thorough drainage, and anti-infectious treatment with regional and continuative washout when the chylous fluid is infected by Candida or bacteria.

[Construction of the eukaryotic expression vector of bioactive fragment of human bactericidal/permeability-increasing protein and its expression in CHO cells].

AIM: To construct the eukaryotic expression vector of the cDNA sequence encoding bioactive N-terminal fragment of human bactericidal/permeability-increasing protein (BPI) and express it in CHO cells. METHODS: Total RNA was extracted from human polymorphonuclear leukocytes (PMN) and subjected to reverse transcription, then the human BPI cDNA gene was amplified by nested PCR. The PCR product was cloned into pUC19 plasmid and confirmed by restriction enzyme digestion and DNA sequencing. Then the specific BPI encoding fragment was subcloned into pcDNA3 plasmid to form pcDNA-BPI(N) eukaryotic expression vector. CHO cells were transfected with the recombinant plasmid and the stable clones were selected by G418. The expression of BPI was identified by immunofluorescent assay. RESULTS: Restriction enzyme digestion and DNA sequence analysis revealed that the sequence encoding signal peptide and bioactive N-terminal fragment of BPI had six nucleotide substitutions, compared with that of the established human BPI sequence. The expression products of the selected CHO positive cell clones were detected by anti-BPI monoclonal antibody. CONCLUSION: The construction of the eukaryotic expression vector of bioactive fragment of human BPI and its successful expression in CHO cells are helpful to further study of the role of BPI.