Physiological stress against simulated 200-m and 500-m sprints in world-class boat paddlers.

To characterize physiological stress response against simulated short-distance sprints among world-class paddlers. Thirteen dragon boat gold medalists performed 200-m and 500-m simulated race trials on a kayak ergometer in a randomized, counter-balanced, crossover fashion. During the 200-m and 500-m sprints, oxygen consumption (VO2) increased from 8.7 to 31.2 ml/kg/min and from 8.0 to 32.7 ml/kg/min within 60 s, respectively. A plateau of 35 ml/kg/min below maximal VO2(VO2max) (39.7 ± 6.3 ml/kg/min) was reached at 75 s during the 500-m sprint. Respiratory exchange ratio dropped from 1.21 ± 0.16 to 1.07 ± 0.12 and 1.28 ± 0.13 to 1.06 ± 0.16 at 45 s, and resurged to 1.17 and 1.28 at the end of 200-m and 500-m sprints with lactate concentration reached 13 ± 2 and 15 ± 2 mM. Aerobic energy contribution to paddling power increases from ~10% for the first 15 s to ~80% for the last 15 s during the 500-m trial. Postexercise plasma thiobarbituric acid reactive substances increased by 376% and 543% above baseline after 200-m and 500-m trials (P < 0.001, between trials), respectively, followed by quick returns to baseline in 30 min (P < 0.001). Increased plasma creatine kinase (+48%) was observed only after the 500-m trial (P < 0.001, between trials), not 200-m trial. Our data suggest that muscle damage occurred only when maximal sprinting exceeding 2 min, highlighting an importance of volume than intensity on exercise-induced muscle damage.

Role of altholactone in inducing type II apoptosis signalling pathway and expression of cancer-related genes in cervical carcinoma HeLa cell line.

Goniothalamus species (Annonaceae) is a shrub that grows in the rainforest of tropical Asia. Several compounds have been isolated and exhibit the potential use for cancer treatment. In this work, altholactone isolated from Goniothalamus macrophyllus was investigated for its cytotoxicity, apoptosis signalling and the expression of cancer-related genes in the cervical carcinoma HeLa cells. Cytotoxicity was evaluated by MTT assay. Apoptotic characteristics were evaluated by morphological studies. Caspase-3 activity was detected using a fluorogenic substrate. Cytochrome c release from mitochondria and protein Bid were determined by Western blotting and cancer-related genes expression by RT-PCR. The results demonstrated that altholactone was cytotoxic to HeLa (IC50 = 9.6 µg/mL), and apoptotic cell death was manifested by appearance of chromatin condensation and caspase-3 activation, which was inhibited by specific inhibitors of both caspase-8 and -9. Release into the cytosol of cytochrome and cleavage of Bid occurred. Altholactone also caused a decrease in bcl-2 and an increase in p53 expression. These unique properties of altholactone suggest a potential for cancer chemotherapy.

The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli.

In the second step of the molybdenum cofactor (Moco) biosynthesis in Escherichia coli, the l-cysteine desulfurase IscS was identified as the primary sulfur donor for the formation of the thiocarboxylate on the small subunit (MoaD) of MPT synthase, which catalyzes the conversion of cyclic pyranopterin monophosphate to molybdopterin (MPT). Although in Moco biosynthesis in humans, the thiocarboxylation of the corresponding MoaD homolog involves two sulfurtransferases, an l-cysteine desulfurase, and a rhodanese-like protein, the rhodanese-like protein in E. coli remained enigmatic so far. Using a reverse approach, we identified a so far unknown sulfurtransferase for the MoeB-MoaD complex by protein-protein interactions. We show that YnjE, a three-domain rhodanese-like protein from E. coli, interacts with MoeB possibly for sulfur transfer to MoaD. The E. coli IscS protein was shown to specifically interact with YnjE for the formation of the persulfide group on YnjE. In a defined in vitro system consisting of MPT synthase, MoeB, Mg-ATP, IscS, and l-cysteine, YnjE was shown to enhance the rate of the conversion of added cyclic pyranopterin monophosphate to MPT. However, YnjE was not an enhancer of the cysteine desulfurase activity of IscS. This is the first report identifying the rhodanese-like protein YnjE as being involved in Moco biosynthesis in E. coli. We believe that the role of YnjE is to make the sulfur transfer from IscS for Moco biosynthesis more specific because IscS is involved in a variety of different sulfur transfer reactions in the cell.