Spatially Extended Low Ionization Emission Regions (LIERs) at z∼0.9z\sim0.9

We present spatially resolved emission diagnostics for eight $z\sim0.9$ galaxies that demonstrate extended low ionization emission-line regions (LIERs) over kpc scales. Eight candidates are selected based on their spatial extent and emission line fluxes from slitless spectroscopic observations with the HST/WFC3 G141 and G800L grisms in the well-studied GOODS survey fields. Five of the candidates (62.5%) are matched to X-ray counterparts in the \textit{Chandra X-Ray Observatory} Deep Fields. We modify the traditional Baldwin-Philips-Terlevich (BPT) emission line diagnostic diagram to use [SII]/(H$\alpha$+[NII]) instead of [NII]/H$\alpha$ to overcome the blending of [NII] and H$\alpha$+[NII] in the low resolution slitless grism spectra. We construct emission line ratio maps and place the individual pixels in the modified BPT. The extended LINER-like emission present in all of our candidates, coupled with X-Ray properties consistent with star-forming galaxies and weak [OIII]$\lambda$5007\AA\ detections, is inconsistent with purely nuclear sources (LINERs) driven by active galactic nuclei. While recent ground-based integral field unit spectroscopic surveys have revealed significant evidence for diffuse LINER-like emission in galaxies within the local universe $(z\sim0.04)$, this work provides the first evidence for the non-AGN origin of LINER-like emission out to high redshifts.Comment: 11 pages, 1 table, 6 figures, accepted for publication in the Astrophysics Journal (ApJ

Post-mortem degradation of myosin heavy chain in intact fish muscle: Effects of pH and enzyme inhibitors

Fish muscle is rapidly degraded during post-mortem storage, due to proteolytic enzymes acting probably both on muscle cells and connective tissue. In this work we have developed a model system which may be used to study the enzymatic degradation occurring in intact post-mortem fish muscle. Degradation of myosin heavy chain (MHC) was monitored in muscle with pH adjusted to 6.05, 6.3 and 6.9 and in the presence of the enzyme inhibitors PMSF, EDTA, phenanthroline, pepstatin A, antipain, E-64 and the cysteine proteinase activator dithiothreithol (DTT). After storage, myofibrillar proteins were isolated and MHC-specific antibodies used to study the degradation in the different samples. MHC from muscle with pH 6.05 and 6.3 was degraded, while no severe degradation was observed at pH 6.9. Introduction of enzyme inhibitors into the muscle tissue clearly showed that mainly cysteine and aspartic proteinases are responsible for the in situ MHC degradation. This is supported by the severe breakdown of MHC in the muscle samples containing DTT.Peer reviewe

Mitochondrial proteomics on human fibroblasts for identification of metabolic imbalance and cellular stress

<p>Abstract</p> <p>Background</p> <p>Mitochondrial proteins are central to various metabolic activities and are key regulators of apoptosis. Disturbance of mitochondrial proteins is therefore often associated with disease. Large scale protein data are required to capture the mitochondrial protein levels and mass spectrometry based proteomics is suitable for generating such data. To study the relative quantities of mitochondrial proteins in cells from cultivated human skin fibroblasts we applied a proteomic method based on nanoLC-MS/MS analysis of iTRAQ-labeled peptides.</p> <p>Results</p> <p>When fibroblast cultures were exposed to mild metabolic stress – by cultivation in galactose medium- the amount of mitochondria appeared to be maintained whereas the levels of individual proteins were altered. Proteins of respiratory chain complex I and IV were increased together with NAD⁺-dependent isocitrate dehydrogenase of the citric acid cycle illustrating cellular strategies to cope with altered energy metabolism. Furthermore, quantitative protein data, with a median standard error below 6%, were obtained for the following mitochondrial pathways: fatty acid oxidation, citric acid cycle, respiratory chain, antioxidant systems, amino acid metabolism, mitochondrial translation, protein quality control, mitochondrial morphology and apoptosis.</p> <p>Conclusion</p> <p>The robust analytical platform in combination with a well-defined compendium of mitochondrial proteins allowed quantification of single proteins as well as mapping of entire pathways. This enabled characterization of the interplay between metabolism and stress response in human cells exposed to mild stress.</p

Plasma Cytokines/Chemokines as Predictive Biomarkers For Lymphedema in Breast Cancer Patients

Breast cancer-related lymphedema (BCRL) occurs in ~ 40% of patients after axillary lymph node dissection (ALND), radiation therapy (RT), or chemotherapy. First-line palliative treatment utilizes compression garments and specialized massage. Reparative microsurgeries have emerged as a second-line treatment, yet both compression and surgical therapy are most effective at early stages of LE development. Identifying patients at the highest risk for BCRL would allow earlier, more effective treatment. Perometric arm volume measurements, near-infrared fluorescent lymphatic imaging (NIRF-LI) data, and blood were collected between 2016 and 2021 for 40 study subjects undergoing treatment for breast cancer. Plasma samples were evaluated using MILLIPLEX human cytokine/chemokine panels at pre-ALND and at 12 months post-RT. A Mann-Whitne