Fitness of three chemotypes of Fusarium graminearum species complex in major winter wheat-producing areas of China.

In China, Fusarium head blight is caused mainly by the Fusarium graminearum species complex (FGSC), which produces trichothecene toxins. The FGSC is divided into three chemotypes: 3-acetyldeoxynivalenol (3-ADON), 15-acetyldeoxynivalenol (15-ADON), and nivalenol (NIV). In order to predict the geographical changes in the distribution of these chemotype populations in major winter wheat-producing areas in China, the biological characteristics of twenty randomly selected isolates from each of the three chemotypes were studied.

[Protective effect and mechanism of Ecliptae Herba on cigarette smoke extract-induced cytotoxicity of NHBE cells].

Objective: To investigate the protective effect and mechanism of Ecliptae Herba extract on cigarette smoke extract-induced cytotoxicity.

Method: The effect of Ecliptae Herba extract on CSE-induced NHBE cell proliferation was detected by MTT assay. GSH content was determined by DTNB colorimetry.

Ursolic acid inhibits cigarette smoke extract-induced human bronchial epithelial cell injury and prevents development of lung cancer.

Cigarette smoking is the main cause of chronic obstructive pulmonary disease and lung cancer. The present study was aimed to explore the chemopreventive effect of ursolic acid (UA) on these diseases. In the CSE treated normal human bronchial epithelial cell model, UA alleviated cytotoxicity caused by CSE, recovered the intracellular redox balance, and relieved the stimulation of external deleterious factors as well.

14-3-3 interacts with LKB1 via recognizing phosphorylated threonine 336 residue and suppresses LKB1 kinase function.

Here we report a regulatory mechanism by which LKB1 is controlled by 14-3-3 proteins through phorsphorylation of Thr336. The results from the current study indicate that 14-3-3 ζ inhibits LKB1 from phosphorylating its substrate, AMPK (AMP-dependent protein kinase) and attenuates LKB1-mediated G1 cell cycle arrest and apoptosis by interfering with the interaction between LKB1 and its substrates. This regulation does not change either the LKB1 catalytic activity or subcellular localization of LKB1.