Calibration of ultraviolet, mid-infrared and radio star formation rate indicators

We present calibrations for star formation rate indicators in the ultraviolet, mid-infrared and radio continuum bands, including one of the first direct calibrations of 150 MHz as a star formation rate indicator. Our calibrations utilize 66 nearby star forming galaxies with Balmer decrement corrected H-alpha luminosities, which span 5 orders of magnitude in star formation rate and have absolute magnitudes of -24<M_r<-12. Most of our photometry and spectrophotometry is measured from the same region of each galaxy, and our spectrophotometry has been validated with SDSS photometry, so our random and systematic errors are small relative to the intrinsic scatter seen in star formation rate indicator calibrations. We find WISE W4 (22.8 micron), Spitzer 24 micron and 1.4 GHz have tight correlations with Balmer decrement corrected H-alpha luminosity, with scatter of only 0.2 dex. Our calibrations are comparable to those from the prior literature for L* galaxies, but for dwarf galaxies our calibrations can give star formation rates that are far greater than those derived from much of the prior literature.M.J.I.B. acknowledges financial support from The Australian Research Council (FT100100280), the Monash Research Accelerator Program (MRA), the Monash Outside Studies Programme (OSP), and the University of Cambridge. Part of this work was undertaken while M.J.I.B. was on OSP (sabbatical) leave at the University of Cambridge, Swinburne University, and the University of Melbourne. M.B. was supported by the MINEDUC-UA project, code ANT 1655. Funding for SDSS-III has been provided by the Alfred P. Sloan Foundation, the Participating Institutions, the National Science Foundation, and the U.S. Department of Energy Office of Science. The SDSS-III Web site is http://www.sdss3.org/. SDSS-III is managed by the Astrophysical Research Consortium for the Participating Institutions of the SDSS-III Collaboration including the University of Arizona, the Brazilian Participation Group, Brookhaven National Laboratory, University of Cambridge, University of Florida, the French Participation Group, the German Participation Group, the Instituto de Astrofisica de Canarias, the Michigan State/Notre Dame/JINA Participation Group, Johns Hopkins University, Lawrence Berkeley National Laboratory, Max Planck Institute for Astrophysics, New Mexico State University, New York University, Ohio State University, Pennsylvania State University, University of Portsmouth, Princeton University, the Spanish Participation Group, University of Tokyo, University of Utah, Vanderbilt University, University of Virginia, University of Washington, and Yale University. The NASA-Sloan Atlas was created by Michael Blanton, with extensive help and testing from Eyal Kazin, Guangtun Zhu, Adrian Price-Whelan, John Moustakas, Demitri Muna, Renbin Yan, and Benjamin Weaver. Funding for the NASA-Sloan Atlas has been provided by the NASA Astrophysics Data Analysis Program (08-ADP08-0072) and the NSF (AST-1211644)

Nuclear envelope structural defects cause chromosomal numerical instability and aneuploidy in ovarian cancer

<p>Abstract</p> <p>Background</p> <p>Despite our substantial understanding of molecular mechanisms and gene mutations involved in cancer, the technical approaches for diagnosis and prognosis of cancer are limited. In routine clinical diagnosis of cancer, the procedure is very basic: nuclear morphology is used as a common assessment of the degree of malignancy, and hence acts as a prognostic and predictive indicator of the disease. Furthermore, though the atypical nuclear morphology of cancer cells is believed to be a consequence of oncogenic signaling, the molecular basis remains unclear. Another common characteristic of human cancer is aneuploidy, but the causes and its role in carcinogenesis are not well established.</p> <p>Methods</p> <p>We investigated the expression of the nuclear envelope proteins lamin A/C in ovarian cancer by immunohistochemistry and studied the consequence of lamin A/C suppression using siRNA in primary human ovarian surface epithelial cells in culture. We used immunofluorescence microscopy to analyze nuclear morphology, flow cytometry to analyze cellular DNA content, and fluorescence <it>in situ </it>hybridization to examine cell ploidy of the lamin A/C-suppressed cells.</p> <p>Results</p> <p>We found that nuclear lamina proteins lamin A/C are often absent (47%) in ovarian cancer cells and tissues. Even in lamin A/C-positive ovarian cancer, the expression is heterogeneous within the population of tumor cells. In most cancer cell lines, a significant fraction of the lamin A/C-negative population was observed to intermix with the lamin A/C-positive cells. Down regulation of lamin A/C in non-cancerous primary ovarian surface epithelial cells led to morphological deformation and development of aneuploidy. The aneuploid cells became growth retarded due to a p53-dependent induction of the cell cycle inhibitor p21.</p> <p>Conclusions</p> <p>We conclude that the loss of nuclear envelope structural proteins, such as lamin A/C, may underlie two of the hallmarks of cancer - aberrations in nuclear morphology and aneuploidy.</p

The desmosome and pemphigus

Desmosomes are patch-like intercellular adhering junctions (“maculae adherentes”), which, in concert with the related adherens junctions, provide the mechanical strength to intercellular adhesion. Therefore, it is not surprising that desmosomes are abundant in tissues subjected to significant mechanical stress such as stratified epithelia and myocardium. Desmosomal adhesion is based on the Ca2+-dependent, homo- and heterophilic transinteraction of cadherin-type adhesion molecules. Desmosomal cadherins are anchored to the intermediate filament cytoskeleton by adaptor proteins of the armadillo and plakin families. Desmosomes are dynamic structures subjected to regulation and are therefore targets of signalling pathways, which control their molecular composition and adhesive properties. Moreover, evidence is emerging that desmosomal components themselves take part in outside-in signalling under physiologic and pathologic conditions. Disturbed desmosomal adhesion contributes to the pathogenesis of a number of diseases such as pemphigus, which is caused by autoantibodies against desmosomal cadherins. Beside pemphigus, desmosome-associated diseases are caused by other mechanisms such as genetic defects or bacterial toxins. Because most of these diseases affect the skin, desmosomes are interesting not only for cell biologists who are inspired by their complex structure and molecular composition, but also for clinical physicians who are confronted with patients suffering from severe blistering skin diseases such as pemphigus. To develop disease-specific therapeutic approaches, more insights into the molecular composition and regulation of desmosomes are required