How Wood Fuels\u2019 Quality Relates to the Standards: A Class-Modelling Approach

The quality requirements of wood biofuels are regulated by a series of harmonized international standards. These standards define the technical parameter limits that influence the quality of solid biomass as a fuel. In 2014 the European reference standard for solid biofuel was replaced by the International ISO standard. In the case of wood chips, the main difference between the European and International standards is the definition of particle size distribution classes. In this context, this study analyses the quality of wood chips and its variation over the years according to the \u201cformer\u201d (EN 14691-4) and \u201cin force\u201d (ISO 17225-4) standards. A Soft Independent Modelling of Class Analogy (SIMCA) model was built to predict the best quality of wood chips and to clarify the relationship between quality and standard parameters, time and changes in the standard regulations. The results show that, compared to the EN standards, classification with the ISO standards increases the samples belonging to the best quality classes and decreases the not classified samples. Furthermore, all the SIMCA models have a high sensitivity (>90%), reflect the differences introduced to the quality standards and are therefore suitable for monitoring the quality of wood chips and their changes

HDAC4 preserves skeletal muscle structure following long-term denervation by mediating distinct cellular responses

BACKGROUND: Denervation triggers numerous molecular responses in skeletal muscle, including the activation of catabolic pathways and oxidative stress, leading to progressive muscle atrophy. Histone deacetylase 4 (HDAC4) mediates skeletal muscle response to denervation, suggesting the use of HDAC inhibitors as a therapeutic approach to neurogenic muscle atrophy. However, the effects of HDAC4 inhibition in skeletal muscle in response to long-term denervation have not been described yet. METHODS: To further study HDAC4 functions in response to denervation, we analyzed mutant mice in which HDAC4 is specifically deleted in skeletal muscle. RESULTS: After an initial phase of resistance to neurogenic muscle atrophy, skeletal muscle with a deletion of HDAC4 lost structural integrity after 4 weeks of denervation. Deletion of HDAC4 impaired the activation of the ubiquitin-proteasome system, delayed the autophagic response, and dampened the OS response in skeletal muscle. Inhibition of the ubiquitin-proteasome system or the autophagic response, if on the one hand, conferred resistance to neurogenic muscle atrophy; on the other hand, induced loss of muscle integrity and inflammation in mice lacking HDAC4 in skeletal muscle. Moreover, treatment with the antioxidant drug Trolox prevented loss of muscle integrity and inflammation in in mice lacking HDAC4 in skeletal muscle, despite the resistance to neurogenic muscle atrophy. CONCLUSIONS: These results reveal new functions of HDAC4 in mediating skeletal muscle response to denervation and lead us to propose the combined use of HDAC inhibitors and antioxidant drugs to treat neurogenic muscle atrophy

Dynamics and Hadronization at intermediate transverse momentum at RHIC

The ultra-relativistic heavy-ion program at RHIC has shown that at intermediate transverse momenta ($p_T \simeq 2$-6 GeV) standard (independent) parton fragmentation can neither describe the observed baryon-to-meson ratios nor the empirical scaling of the hadronic elliptic flow ($v_2$) according to the number of valence quarks. Both aspects find instead a natural explanation in a coalescence plus fragmentation approach to hadronization. After a brief review of the main results for light quarks, we focus on heavy quarks showing that a combined fragmentation and quark-coalescence framework is relevant also here. Moreover, within relativistic Langevin simulations we find evidence for the importance of heavy-light resonances in the Quark-Gluon Plasma (QGP) to explain the strong energy loss and collective flow of heavy-quark spectra as inferred from non-photonic electron observables. Such heavy-light resonances can pave the way to a unified understanding of the microscopic structure of the QGP and its subsequent hadronization by coalescence.Comment: Proceedings of the International Workshop on QCD - Martina Franca (Italy), June 2007. To be published in AIP. 6 pages, 6 figure

Denervation does not induce muscle atrophy through oxidative stress

Denervation leads to the activation of the catabolic pathways, such as the ubiquitin-proteasome and autophagy, resulting in skeletal muscle atrophy and weakness. Furthermore, denervation induces oxidative stress in skeletal muscle, which is thought to contribute to the induction of skeletal muscle atrophy. Several muscle diseases are characterized by denervation, but the molecular pathways contributing to muscle atrophy have been only partially described. Our study delineates the kinetics of activation of oxidative stress response in skeletal muscle following denervation. Despite the denervation-dependent induction of oxidative stress in skeletal muscle, treatments with anti-oxidant drugs do not prevent the reduction of muscle mass. Our results indicate that, although oxidative stress may contribute to the activation of the response to denervation, it is not responsible by itself of oxidative damage or neurogenic muscle atrophy

Lowered Tumor Necrosis Factor Receptors, but Not Increased Insulin Sensitivity, with Infliximab

AbstractObjectives: To verify whether Infliximab could modify insulin sensitivity and TNF‐α and GLUT4 mRNA expression in muscle and adipose tissue of morbidly obese subjects. Soluble TNF receptors I and II (TNFR‐I and TNFR‐II) were also assayed.Research Methods and Procedures: Six obese subjects were investigated before and 2 weeks after a single intravenous administration of 5 mg/kg Infliximab; insulin sensitivity was evaluated by euglycemic hyperinsulinemic clamp, and TNF‐α and GLUT4 mRNA expression were assessed by reverse‐transcriptase polymerase chain reaction on muscle and adipose tissue. TNF‐α, TNFR‐I, and TNFR‐II were determined using the ELISA technique.Results: Infliximab infusion did not affect fasting plasma insulin or fasting plasma glucose levels; whole body glucose uptake did not change significantly. TNF‐α and GLUT4 mRNA did not show any significant change in muscle or adipose tissue. Serum TNF‐α was undetectable before and after treatment, whereas TNFR‐I and TNFR‐II concentrations significantly decreased (p < 0.01).Discussion: An explanation for the absence of effect of Infliximab on insulin resistance in morbidly obese subjects may be the paracrine way of action of this cytokine. Because Infliximab is predominantly distributed within the vascular compartment, its effectiveness in penetrating muscle and adipose tissue is potentially low. The significant decrease of TNFR‐I and TNFR‐II might be ascribed to a targeted effect of Infliximab on the immune system

The scaffolding protein NHERF1 sensitizes EGFR-dependent tumor growth, motility and invadopodia function to gefitinib treatment in breast cancer cells.

Triple negative breast cancer (TNBC) patients cannot be treated with endocrine therapy or targeted therapies due to lack of related receptors. These patients overexpress EGFR but are resistant to Tyrosine Kinase Inhibitors (TKIs) and anti-EGFR therapies. Mechanisms suggested for resistance to TKIs include EGFR independence, mutations and alterations in EGFR and in its downstream signalling pathways. Ligand-induced endocytosis and degradation of EGFR play important roles in the down-regulation of the EGFR signal suggesting that its activity could be regulated by targeting its trafficking. Evidence in normal cells showing that the scaffolding protein Na+/H+ Exchanger Regulatory Factor 1 (NHERF1) can associate with EGFR to regulate its trafficking, led us to hypothesize that NHERF1 expression levels could regulate EGFR trafficking and functional expression in TNBC cells and, in this way, modulate its role in progression and response to treatment. We investigated the subcellular localization of NHERF1 and its interaction with EGFR in a metastatic basal like TNBC cell model, MDA-MB-231, and the role of forced NHERF1 overexpression and/or stimulation with EGF on the sensitivity to EGFR specific TKI treatment with gefitinib. Stimulation with EGF induces an interaction of NHERF1 with EGFR to regulate its localization, degradation and function. NHERF1 overexpression is sufficient to drive its interaction with EGFR in non-stimulated conditions, inhibits EGFR degradation and increases its retention time in the plasma membrane. Importantly, NHERF1 overexpression strongly sensitized the cell to the pharmacological inhibition by gefitinib of EGFR-driven growth, motility and invadopodia-dependent ECM proteolysis. The further determination of how the NHERF1-EGFR interaction is regulated may improve our understanding of TNBC resistance to the action of existing anticancer drugs