[Application of superselective lingual artery embolization in treatment of severe hemorrhange in patients with carcinoma of tongue].

To explore the clinical value of superselective lingual artery embolization in treating the severe hemorrhage in patients with advanced carcinoma of tongue. Four patients with advanced tongue cancer hemorrhage from March 2014 to February 2016 were enrolled in this study. T3N2M0 (2 cases) and T4N1M0 (2 cases) were diagnosed preoperatively. Two cases of advanced tongue carcinoma tumors had severe bleeding and the other 2 cases of hemorrhage were after radiotherapy. All cases including 3 squamous cell carcinoma and 1 adenocarcinoma were firstly demonstrated by arterigraphy under seldinger technique with digtial subtraction angiogarphy to ensure the rupture site and then all cases were followed by superselective artery embolization. The efficacy and complications of interventional embolizationg were observed. There was no serious complication of central nervous system injury such as hemorrhage and hemiplegia during follow-up. Superselective lingual artery embolization can accurately locate the responsibility of blood vessels, and the injury is small, significant effect, fewer complications.

Circulating SHIP2 mRNA as a novel biomarker in the diagnosis and prognosis of gastric cancer.

OBJECTIVE: Previous studies showed the aberrant expression of Src homology 2-containing inositol 5-phosphatase 2 (SHIP2) in GC tissue. However, the exact role of circulating SHIP2 in GC remains unclear. The aim of this manuscript was to analyze potential diagnostic and prognostic value of circulating SHIP2 levels in GC. PATIENTS AND METHODS: Circulating SHIP2 expression was detected in the plasma of 156 GC patients and 60 healthy controls by qRT-PCR. The receiver operating characteristic (ROC) curves were plotted to explore the reliability of circulating SHIP2 in detecting GC. Survival curves were estimated using the Kaplan-Meier method, and differences between them were evaluated by the log-rank test. The influence of each variable on survival was examined by the Cox multivariate regression analysis. RESULTS: Our research showed that the expression levels of circulating SHIP2 in plasma of GC patients were lower than in healthy controls (p < 0.05). Decreased circulating SHIP2 mRNA expression was negatively correlated with clinical stage (p = 0.004), lymph node metastasis (p= 0.003) and distant metastasis (p = 0.025). ROC curve analysis showed that circulating SHIP2 may be a useful marker for discriminating cases from healthy controls. In addition, patients with low circulating SHIP2 mRNA level had poorer overall survival than those with high circulating SHIP2 mRNA level (p = 0.006). Moreover, multivariate analysis indicated that the level of circulating SHIP2 mRNA expression was an independent prognostic indicator (p = 0.005) for the survival of patients with GC. CONCLUSIONS: The present study indicated that decreased plasma SHIP2 mRNA level might be a novel diagnostic and prognostic biomarker for GC patients. This conclusion should be further assessed in randomized clinical trials.

Comparative evaluation of 2.3 mm locking plate system vs conventional 2.0 mm non locking plate system for mandibular condyle fracture fixation: a seven year retrospective study.

OBJECTIVE: This retrospective study evaluated the efficacy of a 2.3 mm locking plate/screw system compared with a 2.0-mm non-locking plate/screw system in fixation of isolated non comminuted mandibular condyle fractures. PATIENTS AND METHODS: Surgical records of 101 patients who received either a 2.3 mm locking plate (group A, n = 51) or 2.0 mm non locking plate (group B, n = 50) were analyzed. All patients were followed up to a minimum of 6 months postoperatively and evaluated for hardware related complications, occlusal stability, need for and duration of MMF and mandibular functional results. RESULTS: Four complications occurred in the locking group and eighteen in the non locking group with complication rates equalling 8% and 36% respectively. When comparing the overall results according to plates used, the χ2 test showed a statistically significant difference between the locking and non locking plates (p < 0.001). Fewer patients required postoperative MMF in group A. CONCLUSIONS: Mandibular condyle fractures treated with a 2.3 mm locking plate exhibited stable osteosynthesis, were associated with minimal complications and resulted in acceptable mandibular range of motion compared with a 2.0 mm non locking plate.

Clinical effectiveness of 125I-seed implantation in combination with nimotuzumab therapy for the advanced oral carcinoma: preliminary results.

OBJECTIVE: This study determines the short-term efficacy and toxicity of combined 125I-seed implantation and nimotuzumab in treating the advanced oral carcinoma. 125I-seed implantation is safe and has shown good short-term efficacy in clinical practice. Nimotuzumab is a useful biological agent for targeted therapy. Effect of 125I-seed implantation with nimotuzumab in treating oral carcinomas remains unclear. PATIENTS AND METHODS: From November 2011 to December 2012, 11 patients with advanced oral carcinoma (pathologic types: 7 cases of squamous cell carcinoma and 4 cases of poorly differentiated adenocarcinoma) were enrolled in our hospital. The patients did not receive surgery due to systemic disease or locally advanced cancer. All of them underwent 125I-seed implantation with the matched peripheral doses (MPD) ranging from 90-100 Gy. The apparent activity per seed ranged from 0.6 mCi (2.22 MBq) to 0.7 mCi (2.59 MBq). Later, all patients were given nimotuzumab (200 mg, intravenous drip, weekly, for 6 weeks). The patients were then followed up and the response rate, acute/chronic radiation-induced injury, and safety of the induction treatment were analyzed. RESULTS: Three patients achieved complete while 6 patients had partial response; yielding a response rate of 81.8%. Major adverse events included radiation-induced oral mucositis, local hemorrhage, bone marrow suppression, nausea/vomiting, and alopecia. Adverse reaction was not significantly different between the group of patients under 65 years of age and over 65 years of age (p > 0.05). Nimotuzumab enhanced the tumor sensitivity to brachytherapy without increasing AEs and improved the patients' life quality. CONCLUSIONS: 125I-seed implantation combined with nimotuzumab is effective and safe for patients with unresectable oral carcinoma.

TPS-guided interstitial Iodine-125 implantation in patients with oral cavity and maxillofacial carcinomas.

OBJECTIVE: To investigate the efficacy as well as the complications involved in the use of interstitial Iodine-125 implantation for the treatment of oral cavity and maxillofacial carcinomas. PATIENTS AND METHODS: Fifteen patients with oral cavity and maxillofacial carcinomas received treatment planning system (TPS)-guided interstitial Iodine-125 implantation. The apparent activity per particle ranged from 0.6 mCi (2.22MBq) to 0.7 mCi (2.59MBq). The matched peripheral dose delivered by radioactive seeds ranged from 90 to 120 Gy. The efficacy of the treatment and the postoperative complications were evaluated during follow-up. RESULTS: The seeds were implanted successfully in all 15 patients and median number of seeds implanted was 36.53. CT scans were performed in all patients at 1-6 months postoperatively. During follow-up at 6-27 months, seed migration occurred and a good local tumor control was achieved with an overall response of 86.7%. No severe side effects were observed. CONCLUSIONS: TPS-guided interstitial Iodine-125 implantation is an effective and safe procedure with minimal invasiveness for the treatment of oral cavity and maxillofacial carcinomas, and it effectively prevents the recurrence of cancer and short-term lymphatic metastasis.

Digital subtraction angiography (DSA) guided sequential sclerotherapy for maxillofacial vein malformation.

OBJECTIVES: Venous malformations commonly occur in the head and neck and affect the patient's appearance and also cause pain, ulcers, and bleeding. Current treatment options have many limitations and it is necessary to explore alternate methods to address these malformations. This work was aimed to explore the best method for treating patients with maxillofacial vein malformation. PATIENTS AND METHODS: Guided by digital subtraction angiography, 43 patients with maxillofacial vein malformation were treated with sequential sclerotherapy intervention. RESULTS: Patients were followed up for 7 months to 3 years. Lesions completely recessed in 7 cases. Recession rates were greater than 50% in 28 cases, 25-50% in 5 cases, and less than 25% in 3 cases. No severe complications occurred. CONCLUSIONS: Sclerotherapy with ethanol and pingyangmycin is a safe and effective method of treating maxillofacial vein malformation.

Selenoprotein W gene regulation by selenium in L8 cells.

The effects of selenium on selenoprotein W gene expression were examined in cultured L8 rat skeletal muscle cells. Selenoprotein W contains selenium as selenocysteine in the primary protein structure and levels of this selenoprotein are affected by selenium. Northern blots indicated that there were no significant changes (P < 0.05) in selenoprotein W mRNA levels during cell proliferation and differentiation. Reduction of selenium concentration in the medium decreased the selenoprotein W mRNA levels. Nuclear run-on experiments with isolated L8 nuclei showed the same rate of selenoprotein W mRNA synthesis in cells cultured in either low selenium or selenium supplemented medium, suggesting that the transcription rate of the selenoprotein W gene is independent of selenium. Measurement of the selenoprotein W mRNA half-life in myoblasts treated with the transcription inhibitor, alpha-amanitin, showed that selenoprotein W mRNA levels decreased over time with an estimated half-life of 57 h for cells grown in low selenium medium. Selenium treatment increased the selenoprotein W mRNA half-life 2-fold. These data suggest that selenium stabilizes selenoprotein W mRNA but has no effect on transcription.

Selenoprotein W in overexpressed and underexpressed rat glial cells in culture.

Selenium deficiency results in undetectable levels of selenoprotein W (SeW) in muscle but has very little effect upon its content in the brain and thus rat glial cells were studied. Previous work showed that glutathione (GSH) is bound to SeW and this study was undertaken to elucidate its possible antioxidant functions. Full length cDNA of SeW was cloned to inducible LacSwitch expression vector and stably transfected in C6 rat glial cells. After induction, SeW and its mRNA were expressed 22- and 11-fold higher respectively than control. The cDNA coding region of SeW was cloned to the vector in the antisense direction and stably transfected in C6 cells for underexpression of the protein. After induction, SeW expression was reduced to 20% of the control cells. Glutathione peroxidase activity and GSH levels were not significantly different between induced and control cells. There was a greater survival rate of overexpressed than control cells when incubated with 2,2'-Azobis (2-amidinopropane) dihydrochloride (AAPH), suggesting SeW possibly has an antioxidant function.

Selenoprotein W accumulates primarily in primate skeletal muscle, heart, brain and tongue.

The human selenoprotein W coding region with the selenocysteine codon (TGA) changed to a cysteine codon (TGT) was fused to six histidine codons (at its 3' end), cloned into a prokaryotic expression vector (pTrc99a), and the corresponding mutated selenoprotein W was expressed in bacteria. The protein was purified by Ni-NTA agarose column and reverse phase HPLC. Polyclonal antibodies raised against this protein were used in Western blots to determine tissue distribution of selenoprotein W from rhesus monkeys fed a commercial chow. Selenoprotein W was found in several tissues with highest amounts in skeletal muscle and heart (muscle 6 fold greater than liver) and lowest levels in liver, but selenium concentrations were highest in kidneys (10 fold greater than muscle) and lowest in skeletal muscle. Northern blots using a human selenoprotein W cDNA probe indicated that mRNA levels were highest in monkey skeletal muscle and heart (2-2.5 fold greater than in liver), which is similar to the pattern found with a human multiple tissue Northern blot. However, as in the monkey, selenium concentrations were highest in human kidney and lowest in skeletal muscle and heart. Thus, selenoprotein W protein levels correlated with selenoprotein W mRNA levels but not with tissue selenium concentrations.

Purification, characterization, and glutathione binding to selenoprotein W from monkey muscle.

Selenoprotein W was purified from monkey skeletal muscle to investigate its binding of glutathione. The purification was accomplished by concentration of the cytosol with an Amicon cell, gel filtration using Sephadex G-50, cation-exchange chromatography with CM-Sephadex, and reverse-phase high-pressure liquid chromatography using a C-18 Vydac column. Selenoprotein W was monitored during purification by slot blots. These steps resulted in an electrophoretically pure selenoprotein W preparation that was estimated by gel filtration to have molecular weight of about 10 kDa. N-terminal amino acid sequencing was used to confirm that the pure proteins were selenoprotein W. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI) revealed that the proteins existed in three masses of 9635 +/- 7, 9371 +/- 11, and 9330 +/- 5 Da. The theoretical mass of the protein predicted from the cDNA sequence is 9330 Da. The 9635-Da form of the protein was shown to contain bound glutathione (306 Da), which could be released by reduction with dithiothreitol at 50 degreesC. The form with a mass of 9371 Da is assumed to result from binding of an unidentified 41-Da moiety to the 9330-Da form of the protein. MALDI peptide mapping with endoproteinase Glu-C suggested that glutathione is bound to the 36th amino acid (cysteine) of selenoprotein W.

Distribution of selenium between plasma fractions in guinea pigs and humans with various intakes of dietary selenium.

The distribution of selenium between the plasma fractions was investigated in guinea pigs fed various levels (basal, 0.5, 1.0, 2.0, 4.0, 6.0 and 8.0 mg Se/kg) of dietary selenomethionine (Semet) and in humans living in different areas of China with different selenium status. There was a corresponding increase of selenium concentration in liver, kidney, brain, testis, spleen, heart and muscle with each increase of dietary selenium, but there were no increases of glutathione peroxidase (GPX) activity in liver, brain, testis, heart or muscle in pigs fed any of the selenium levels as compared to controls fed a basal commercial diet. On a percentage distribution basis, the selenium in selenoprotein P decreased and that in the albumin fraction increased with increased dietary intakes of selenium as Semet. The ratios of selenium to albumin in either the plasma or the albumin fractions increased with each increase in dietary selenium. The greatest percentage of selenium was in the albumin fraction of Chinese living in the high selenium areas whereas the greatest amount was in the selenoprotein P fraction in subjects living in deficient and adequate areas of China. Increases in the ratios of selenium to albumin in either the plasma or the albumin fraction also occurred with increases of selenium intake of these subjects. The results indicate that the distribution of selenium in plasma fractions reflect the levels of dietary intakes of Semet.

Influence of gender on selenoprotein W, glutathione peroxidase and selenium in tissues of rats.

After feeding a commercial rodent chow for 8 weeks, tissues from male and female rats were collected and examined for selenium content, glutathione peroxidase (GPX) activities and selenoprotein W (Se-W) levels. There were no differences (P > 0.05) between plasma selenium content, plasma GPX activity, whole blood selenium content, or whole blood GPX activity between male and female rats. There was also no gender effect on selenium concentration in muscle, brain, spleen, and skin, but selenium concentration in liver was higher (P < 0.05) in female than in male rats. Western blots indicated that the tissue distribution of Se-W was similar in male and female rats. Se-W protein level was high in testes of male rats but very low in ovaries of female rats. Muscle and skin from female rats had significantly higher (P < 0.05) Se-W levels than from male rats. Consistent with Se-W content, the Se-W mRNA levels from female skins were significantly higher (P < 0.05) than from male rats. The expression of Se-W was different in various tissues and gender influenced this regulation in some tissues.

Selenoprotein W cDNAs from five species of animals.

The nucleotide sequences of the open reading frames of cDNAs for selenoprotein W from skeletal muscle of rat, mouse, sheep, rhesus monkey and human are reported. Theoretical translation of the coding sequences indicated highly similar proteins of 88 (mouse and rat) or 87 (human, monkey and sheep) amino acids. In 73 of 88 positions the specified amino acids are identical for all five proteins. TGA encoding selenocysteine is the 13th codon of all the cDNAs. The mouse, rat and sheep open reading frames terminate with TGA but the human and rhesus monkey coding regions terminate with TAA. The encoded amino acid sequences are identical for the rat and mouse proteins, and for the human and monkey proteins. The similarity of the cDNAs continues in the 3' noncoding regions through the putative selenocysteine insertion sequence (SECIS) elements which are required for correct interpretation of the selenocysteine codon. The region between the SECIS elements and the polyadenylation signals showed much lower similarity. The cloned rat gene for selenoprotein W is 5000 bases long, with the 663 bases of the cDNA in six exons. The transcription start site was identified by nuclease protection assay to be 16 bases upstream of the longest cDNA clone. A canonical TATA box occurs 150 bases upstream, but the assay did not indicate the presence of longer mRNAs.

Conserved features of selenocysteine insertion sequence (SECIS) elements in selenoprotein W cDNAs from five species.

SECIS elements form stem-loop structures in the 3' untranslated regions (UTR) of eukaryotic mRNAs that encode selenoproteins. These elements direct incorporation of selenocysteine at UGA codons, provided the SECIS element lies a sufficient distance from the UGA. The cDNAs encoding skeletal muscle selenoprotein W from human, rhesus monkey, sheep, rat, and mouse contained highly similar SECIS elements that retained important features common to all known SECIS elements. Comparative analysis of these SECIS elements showed that in some regions both predicted secondary structure and nucleotide sequences were conserved, in other areas secondary structure was maintained using different primary sequence, and in still other portions, base pairing was not conserved. The rodent and sheep selenoprotein W mRNAs used UGA as a stop codon and as a selenocysteine codon. Thus, UGA specified both selenocysteine incorporation and termination in a single mRNA. The selenoprotein W SECIS elements contained an additional highly conserved base-paired stem that may prevent inappropriate selenocysteine incorporation at the UGA stop codons.

Selenium influences tissue levels of selenoprotein W in sheep.

Because selenium increases the levels of other selenoproteins, the influence of this element on selenoprotein W was examined in wether sheep fed either a low selenium diet (0.02 mg/kg) or the same diet supplemented with 3 mg selenium as selenite per kilogram diet. Muscle biopsies were taken initially and at 3.5, 7.0 and 10.5 wk. The sheep were killed after the last muscle biopsy and samples from nine tissues were taken. Selenoprotein W was determined in tissues by Western blots with a polyclonal antibody against a synthetic peptide based on the protein sequence of the homologous rat selenoprotein W. In supplemented sheep, muscle selenoprotein W was significantly increased over initial levels (P < 0.05) at 7 wk and afterwards, whereas in sheep consuming the low selenium diet, muscle selenoprotein W levels declined significantly (P < 0.05) after 10.5 wk. This selenoprotein was found in various amounts in all tissues examined. The highest levels of selenoprotein W were found in skeletal muscles and heart and the lowest was found in liver. Except for selenoprotein W in brain, the concentrations of selenoprotein W, selenium and glutathione peroxidase activity were significantly higher (P < 0.05) in all tissues from supplemented sheep than in those from unsupplemented sheep. The selenoprotein W levels in brains of the two groups were not significantly different. Thus, selenoprotein W levels in all tissues of sheep except the brain are sensitive to selenium status.

[Pharmacokinetics of gentamicin after intratracheal administration in tracheotomy patients].

Seventeen tracheotomy patients were given gentamicin (Gen) into trachea at the dosage of 2 and 4 mg.kg-1. Gen concentration in serum was determined by fluorescence polarization immunoassay. Pharmacokinetic parameters were calculated by micro-computer pharmacokinetic program (MCPKP). T1/2Ka, Tp, and Cmax were 0.6 +/- 0.3 h, 1.7 +/- 0.7 h, and 4.6 +/- 1.8 micrograms.ml-1, respectively in 4 mg.kg-1 group and 0.3 +/- 0.3 h, 0.9 +/- 0.5 h, and 0.4 +/- 0.2 microgram.ml-1, respectively in 2 mg.kg-1 group (P < 0.05). T1/2Kel was 30 +/- 11 h in patients of serum creatine (Cr) > 2 mg% and 6 +/- 5 h in patients of Cr < 2 mg% (P < 0.01). No significant difference could be found between Cmax of different renal function patients (P > 0.05).

[Pharmacokinetics of cyclosporin A in renal transplant patients after infusion].

Seventeen patients after renal transplantation were infused iv cyclosporin A (CsA) 0.65 +/- 0.13 mg.kg-1.h-1. Blood CsA was determined by fluorescence polarization immunoassay (FPIA). Pharmacokinetic parameters were calculated from micro-computer pharmacokinetic programme T1/2 beta = 8.6 +/- 3.4 h, Vd = 3.2 +/- 1.3 L.kg-1. No significant difference was found between sexes and between age groups.