Toward Forecasting Volcanic Eruptions using Seismic Noise

During inter-eruption periods, magma pressurization yields subtle changes of the elastic properties of volcanic edifices. We use the reproducibility properties of the ambient seismic noise recorded on the Piton de la Fournaise volcano to measure relative seismic velocity variations of less than 0.1 % with a temporal resolution of one day. Our results show that five studied volcanic eruptions were preceded by clearly detectable seismic velocity decreases within the zone of magma injection. These precursors reflect the edifice dilatation induced by magma pressurization and can be useful indicators to improve the forecasting of volcanic eruptions.Comment: Supplementary information: http://www-lgit.obs.ujf-grenoble.fr/~fbrengui/brenguier_SI.pdf Supplementary video: http://www-lgit.obs.ujf-grenoble.fr/~fbrengui/brenguierMovieVolcano.av

Energy partition of seismic coda waves in layered media: theory and application to Pinyon Flats Observatory

We have studied the partition of shear, compressional and kinetic energies in the coda of ten earthquakes recorded on a dense array, located at Pinyon Flats Observatory (PFO), California. We observe a clear stabilization of the shear to compressional ($W^s/W^p$) energy ratio in the coda, with an average value of about 2.8. The ratio between the vertical and horizontal kinetic energies ($V^2/H^2$) can be measured from 5 to 25Hz and shows an abrupt transitionfrom 0.1 in the 5-10Hz band, to about 0.8 in the 15-25Hz band. These measured values are in sharp contrast with the theoretical prediction for equipartitioned elastic waves in a homogeneous half-space. To explain these observations, we have developed a theory of equipartition in a layered elastic half-space. Using a rigorous spectral decomposition of the elastic wave equation, we define equipartition as a white noise distributed over the complete set of eigenfunctions. The theory predicts that close to the resonance frequency of a low-velocity layer, the ratio between shear and compressional energies strongly decreases. Using a detailed model of the subsurface at PFO, this conterintuitive result is found to be in good qualitative and quantitative agreement with the observations

Subcellular fractionation of human liver reveals limits in global proteomic quantification from isolated fractions

The liver plays an important role in metabolism and elimination of xenobiotics, including drugs. Determination of concentrations of proteins involved in uptake, distribution, metabolism, and excretion of xenobiotics is required to understand and predict elimination mechanisms in this tissue. In this work, we have fractionated homogenates of snap -frozen human liver by differential centrifugation and performed quantitative mass spectrometry -based proteomic analysis of each fraction. Concentrations of proteins were calculated by the "total protein approach". A total of 4586 proteins were identified by at least five peptides and were quantified in all fractions. We found that the xenobiotics transporters of the canalicular and basolateral membranes were differentially enriched in the subcellular fractions and that phase I and II metabolizing enzymes, the cytochrome P450s and the UDP glucuronyl transferases, have complex subcellular distributions. These findings show that there is no simple way to scale the data from measurements in arbitrarily selected membrane fractions using a single scaling factor for all the proteins of interest. This study also provides the first absolute quantitative subcellular catalog of human liver proteins obtained from frozen tissue specimens. Our data provide quantitative insights into the sub cellular distribution of proteins and can be used as a guide for development of fractionation procedures

Multiple-Enzyme-Digestion Strategy Improves Accuracy and Sensitivity of Label- and Standard-Free Absolute Quantification to a Level That Is Achievable by Analysis with Stable Isotope-Labeled Standard Spiking

Quantification of individual proteins is an essential task in understanding biological processes. For example, determination of concentrations of proteins transporting and metabolizing xenobiotics is a prerequisite for drug disposition predictions in humans based on in vitro data. So far, this task has frequently been accomplished by targeted proteomics. This type of analyses requires preparation of stable isotope labeled standards for each protein of interest. The selection of appropriate standard peptides is usually tedious and the number of proteins that can be studied in a single experiment by these approaches is limited. In addition, incomplete digestion of proteins often affects the accuracy of the quantification. To circumvent these constrains in proteomic protein quantification, label- and standard-free approaches, such as "total protein approach" (TPA) have been proposed. Here we directly compare an approach using stable isotope labeled (SIL) standards and TPA for quantification of transporters and enzymes in human liver samples within the same LC-MS/MS runs. We show that TPA is a convenient alternative to SIL-based methods. Optimization of the sample preparation beyond commonly used single tryptic digestion, by adding consecutive cleavage steps, improves accuracy and reproducibility of the TPA method to a level, which is achievable by analysis using stable isotope-labeled standard spiking