Our data indicate that calcium regulates sensitivity in these mechanoreceptor neurons by negative feedback from action potentials onto transduction channels.”
“Aromatic-aromatic interactions have long been believed to play key roles in protein structure, folding, and binding functions. However, we still lack full understanding of the contributions of aromatic-aromatic interactions to protein stability and the timing of their formation during folding. Here, using an aromatic ladder in the beta-barrel protein, cellular retinoic acid-binding protein 1 (CRABP1), as a case study, we find that aromatic pi stacking plays a greater role in the Phe65-Phe71 cross-strand pair, while in another pair,

Phe50-Phe65, hydrophobic interactions

are dominant. The Phe65-Phe71 pair spans beta-strands 4 and 5 in the beta-barrel, which lack interstrand hydrogen bonding, and phosphatase inhibitor we speculate that it compensates energetically for the absence of strand-strand backbone interactions. Using perturbation analysis, we find that both aromatic-aromatic pairs form after the transition state for folding of CRABP1, thus playing a role in the final stabilization of the beta-sheet rather than in its nucleation as had been earlier proposed. The aromatic interaction between strands 4 and 5 in Selleck INCB028050 CRABP1 is highly conserved in the intracellular lipid-binding protein (iLBP) family, and several lines of evidence combine to support a model wherein it acts to maintain barrel structure while allowing the dynamic opening that is necessary for ligand entry. Lastly, we carried out a bioinformatics analysis and found 51 examples of aromatic-aromatic interactions across non-hydrogen-bonded beta-strands outside the iLBPs, arguing for the generality of the role played by this structural motif. (C) 2013 Elsevier Ltd. All rights reserved.”
“Arsenic trioxide has been known to regulate many biological functions such as cell proliferation, apoptosis, differentiation, and angiogenesis in various cell lines. We investigated the involvement of GSH and ROS such as H2O2 and O-2(.-) in the death of As4.1 cells by arsenic trioxide. The intracellular

ROS levels were changed depending on the concentration and length of incubation with arsenic trioxide. The intracellular O-2(.-) level was significantly increased at all the concentrations GSK1838705A tested. Arsenic trioxide reduced the intracellular GSH content. Treatment of Tiron, ROS scavenger decreased the levels of ROS in 10 mu M arsenic trioxide-treated cells. Another ROS scavenger, Tempol did not decrease ROS levels in arsenic trioxide-treated cells, but slightly recovered the depleted GSH content and reduced the level of apoptosis in these cells. Exogenous SOD and catalase did not reduce the level of ROS, but did decrease the level Of O-2(.-). Both of them inhibited GSH depletion and apoptosis in arsenic trioxide-treated cells.