Downregulation of miR-361-5p associates with aggressive clinicopathological features and unfavorable prognosis in non-small cell lung cancer.

OBJECTIVE: To assess the impact of miR-361-5p expression levels on non-small-cell lung cancer (NSCLC) survival. PATIENTS AND METHODS: A total of 183 patients with NSCLC who underwent surgery between October 2007 and April 2010 were included in this study. Expression levels of miR-361-5p were detected by using qRT-PCR. The association of miR-361-5p expression with clinicopathologic characteristics of NSCLC patients was analyzed. Kaplan-Meier Plotter was performed to identify the prognostic roles of miR-361-5p in NSCLC patients. Finally, multivariate analysis was performed using the Cox proportional hazard analysis. RESULTS: Results indicated that miR-361-5p was lowly expressed in NSCLC compared with adjacent non-malignant tissues (p < 0.01). And low miR-361-5p expression in NSCLC was significantly correlated with TNM stage (p = 0.000), lymph node metastasis (p = 0.001) and lymphatic invasion (p = 0.032). Kaplan-Meier analysis with the log-rank test indicated that low miR-361-5p expression had a significant impact on overall survival (p < 0.001). Furthermore, Multivariate analyses indicated that miR-361-5p represented an independent predictor for overall survival of NSCLC (p = 0.007). CONCLUSIONS: Our work revealed that miR-361-5p played critical roles in NSCLC progression and could represent a novel prognostic marker in NSCLC patients.

Inhibition kinetics of green crab (Scylla serrata) alkaline phosphatase activity by dithiothreitol or 2-mercaptoethanol.

Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme which catalyzes the nonspecific hydrolysis of phosphate monoesters. Some pollutants in seawater affect the enzyme activity causing loss of the biological function of the enzyme, which affects the exuviating crab-shell and threatens the survival of the animal. The present paper studies the effects of thiohydroxyal compounds on the activity of green crab alkaline phosphatase. The results show that thiohydroxyal compounds can lead to reversible inhibition. The equilibrium constants have been determined for dithiothreitol (DTT) and mercaptoethanol (ME) binding with the enzyme and/or the enzyme-substrate complexes. The results show that both DTT and ME are non-competitive inhibitors. The kinetics of enzyme inactivation by ME at low concentrations has been studied using the kinetic method of the substrate reaction. The results suggest that at pH 10.0, the action of ME on green crab ALP is first quick equilibrium binding and then slow inactivation. The microscopic rate constants were determined for inactivation and reactivation. The rate constant of the forward inactivation (k(+0)) is much larger than that of the reverse reactivation (k(-0)). Therefore, when the ME concentration is sufficiently large, the enzyme is completely inactivated.

Kinetics of inhibition of beta-glucosidase from Ampullarium crossean by bromoacetic acid.

The kinetics of inhibition of beta-glucosidase from Ampullarium crossean by bromoacetic acid (BrAc) has been studied. The results show that the enzyme can be irreversibly and completely inactivated at high BrAc concentration, while at low BrAc concentration, inhibition of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reactions of BrAc with the enzyme were determined. The presence of the substrate offers obvious protection of the enzyme against inhibition by BrAc. The above results suggest that the histidine residue is essential for activity and is situated at or near the active site of the enzyme.

Kinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by sodium (2,2'-bipyridine) oxodiperoxovanadate.

Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme, which catalyzes the nonspecific hydrolysis of phosphate monoesters. The kinetics of inhibition of the enzyme by sodium (2, 2'-bipyridine) oxodiperoxovanadate, pV(bipy), has been studied. The time course of the hydrolysis of p-nitrophenyl-phosphate catalyzed by the enzyme in the presence of different pV(bipy) concentrations showed that at each pV(bipy) concentration, the rate decreased with increasing time until a straight line was approached, the straight line slopes are the same for all concentrations. The results suggest that the inhibition of the enzyme by pV(bipy) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined for the reaction of inhibitor with the enzyme.

[Studies on ecology of Fasciolopsis buski and control strategy of fasciolopsiasis].

The development of eggs of Fasciolopsis buski requires oxygen and the eggs cannot survive anaerobic conditions. The eggs have some resistance to low temperature and can be maintained at 4 degrees C for 3 to 4 months; however, the eggs are killed at 50 degrees C in four hours. The presence of salts can influence the development time of the eggs and reduce their hatching rate. Encysted cercariae exist not only on aquatic plants, but also on the surface of the water. The number of encysted cercariae floating on the water surface is about 3.6% of that of the total encysted cercariae. By inquiring into the case history we found that 10.3-12.8% of the patients and 35.1-40% of the infested pigs were possibly infected by drinking water contaminated with encysted cercariae. The authors suggest the use of fermented silage to feed pigs instead of fresh aquatic green fodders to prevent infection in the animals. In addition, aquatic plants such as water chestnut should be boiled for 1 to 2 minutes before eating to kill the encysted cercariae on the plants.