ABC Television (ABC1 & ABC News 24) - Guest appearance (live).

ABC Television (ABC1 & ABC News 24) - Guest appearance (live).Due to my expertise in media, I was invited to be a guest reviewer of the daily newspapers on national television. This was a live interview, lasting 10 minutes.

Increase in S6K1 phosphorylation in human skeletal muscle following resistance exercise occurs mainly in type II muscle fibres

To investigate the in vivo effects of resistance exercise on translational control in human skeletal muscle, we determined the phosphorylation of AMP-activated kinase (AMPK), eukaryotic initiation factor 4E-binding protein (4E-BP1), p70/p85-S6 protein kinase (S6K1), and ribosomal S6 protein (S6). Furthermore, we investigated whether changes in the phosphorylation of S6K1 are muscle fiber type specific. Eight male subjects performed a single high-intensity resistance exercise session. Muscle biopsies were collected before and immediately after exercise and after 30 and 120 min of postexercise recovery. The phosphorylation statuses of AMPK, 4E-BP1, S6K1, and S6 were determined by Western blotting with phospho-specific and pan antibodies. To determine fiber type-specific changes in the phosphorylation status of S6K1, immunofluorescence microscopy was applied. AMPK phosphorylation was increased approximately threefold immediately after resistance exercise, whereas 4E-BP1 phosphorylation was reduced to 27 ± 6% of preexercise values. Phosphorylation of S6K1 at Thr421/Ser424 was increased 2- to 2.5-fold during recovery but did not induce a significant change in S6 phosphorylation. Phosphorylation of S6K1 was more pronounced in the type II vs. type I muscle fibers. Before exercise, phosphorylated S6K1 was predominantly located in the nuclei. After 2 h of postexercise recovery, phospho-S6K1 was primarily located in the cytosol of type II muscle fibers. We conclude that resistance exercise effectively increases the phosphorylation of S6K1 on Thr421/Ser424, which is not associated with a substantial increase in S6 phosphorylation in a fasted state.

The "refoldability" of selected proteins in ionic liquids as a stabilization criterion, leading to a conjecture on biogenesis

The folding of proteins is usually studied in dilute aqueous solutions of controlled pH, but it has recently been demonstrated that reversible unfolding can occur in other media. Particular stability is conferred on the protein (folded or unfolded) when the process occurs in ‘protic ionic liquids’ (pILs) of controlled proton activity. This activity (‘effective pH’) is determined by the acid and base components of the pIL and is characterized in the present study by the proton chemical shift of the N–H proton. Here we propose a ‘refoldability’ or ‘refolding index’ (RFI) metric for assessing the stability of folded biomolecules in different solvent media, and demarcate high RFI zones in hydrated pIL media using ribonuclease A and hen egg white lysozyme as examples. Then we show that, unexpectedly, the same high RFIs can be obtained in pIL media that are 90% inorganic in character (simple ammonium salts). This leads us to a conjecture related to the objections that have been raised to ‘primordial soup’ theories for biogenesis, objections that are based on the observation that all the bonds involved in biomacromolecule formation are hydrolyzed in ordinary aqueous solutions unless specifically protected. The ingredients for primitive ionic liquids (NH3, CO, HCN, CO2, and water) were abundant in the early earth atmosphere, and many experiments have shown how amino acids could form from them also. Cyclical concentration in evaporating inland seas could easily produce the type of ambient-temperature, non-hydrolyzing, media that we have demonstrated here may be hospitable to biomolecules, and that may be actually encouraging of biopolymer assembly. Thus a plausible variant of the conventional ‘primordial soup’ model of biogenesis is suggested.

Meta-analysis of movements in Atlantic leatherback turtles during the nesting season : conservation implications

Despite decades of conservation efforts on the nesting beaches, the critical status of leatherback turtles shows that their survival predominantly depends on our ability to reduce at-sea mortality. Although areas where leatherbacks meet fisheries have been identified during the long distance movements between 2 consecutive nesting seasons, hot-spots of lethal interactions are still poorly defined within the nesting season, when individuals concentrate close to land. Here we report movements of satellite-tracked gravid leatherback turtles during the nesting season in Western Central Africa, South America and the Caribbean Sea, which account for about 70% of the world population. We show that during and at the end of the nesting season, leatherback turtles have the propensity to remain over the continental shelf, yet sometimes perform extended movements and may even nest in neighbouring countries. Leatherbacks exploit coastal commercial fishing grounds and face substantial accidental capture by regional coastal fisheries (e.g. at least 10% in French Guiana). This emphasises the need for regional conservation strategies to be developed at the ocean scale—both at sea and on land—to ensure the survival of the last leatherback turtles.