Nationalism and internationalism in science: the case of the discovery of cosmic rays

The discovery of cosmic rays, a milestone in science, comprised scientists in Europe and the US and took place during a period characterised by nationalism and lack of communication. Many scientists that took part in this research a century ago were intrigued by the penetrating radiation and tried to understand the origin of it. Several important contributions to the discovery of the origin of cosmic rays have been forgotten and in particular that of Domenico Pacini, who in June 1911 demonstrated by studying the decrease of radioactivity with an electroscope immersed in water that cosmic rays could not come from the crust of the Earth. Several historical, political and personal facts might have contributed to the substantial disappearance of Pacini from the history of science.Comment: To be published in European Physical Journal H - Version revised after interaction with the editor and the referee

Development and Demonstration of New Technology for the use of Wind Turbines on Ships

Technology to substantially reduce commercial ship fuel consumption by harnessing sea winds for simultaneous generation of electricity and thrust, has been developed by the company PROPit AB. The basic idea is to apply conventional wind turbine technology for the marine environment, where the turbine will also take the function of sails. Primary target market is tankers or bulk ships with a large and open deck space. Chalmers, in a study co-sponsored by the Swedish Energy Agency and Chalmers Energy Centre, 2011, confirmed fuel saving estimates around 15-30 % for optimal routes, but with higher uncertainties

Integration pågår

Medan unga malmöbor ofta möts över kulturgränser, träffar knappt varannan sjuttioåring någon från en annan kultur. Även om utrymmet för mångfald tycks ha sina gränser och attityderna är polariserade, får ytterligheterna allt svagare stöd

Molecular aging and rejuvenation of human muscle stem cells

Very little remains known about the regulation of human organ stem cells (in general, and during the aging process), and most previous data were collected in short-lived rodents. We examined whether stem cell aging in rodents could be extrapolated to genetically and environmentally variable humans. Our findings establish key evolutionarily conserved mechanisms of human stem cell aging. We find that satellite cells are maintained in aged human skeletal muscle, but fail to activate in response to muscle attrition, due to diminished activation of Notch compounded by elevated transforming growth factor beta (TGF-β)/phospho Smad3 (pSmad3). Furthermore, this work reveals that mitogen-activated protein kinase (MAPK)/phosphate extracellular signal-regulated kinase (pERK) signalling declines in human muscle with age, and is important for activating Notch in human muscle stem cells. This molecular understanding, combined with data that human satellite cells remain intrinsically young, introduced novel therapeutic targets. Indeed, activation of MAPK/Notch restored ‘youthful’ myogenic responses to satellite cells from 70-year-old humans, rendering them similar to cells from 20-year-old humans. These findings strongly suggest that aging of human muscle maintenance and repair can be reversed by ‘youthful’ calibration of specific molecular pathways

Cosmic Ray Spectral Deformation Caused by Energy Determination Errors

Using simulation methods, distortion effects on energy spectra caused by errors in the energy determination have been investigated. For cosmic ray proton spectra, falling steeply with kinetic energy E as E-2.7, significant effects appear. When magnetic spectrometers are used to determine the energy, the relative error increases linearly with the energy and distortions with a sinusoidal form appear starting at an energy that depends significantly on the error distribution but at an energy lower than that corresponding to the Maximum Detectable Rigidity of the spectrometer. The effect should be taken into consideration when comparing data from different experiments, often having different error distributions.Comment: To appear in Nuclear Instr. Method

Protein phosphatase 1c associated with the cardiac sodium calcium exchanger1 regulates its activity by dephosphorylating serine 68 phosphorylated phospholemman

The sodium (Na+)-calcium (Ca2+) exchanger 1 (NCX1) is an important regulator of intracellular Ca2+ homeostasis. Serine 68-phosphorylated phospholemman (pSer-68-PLM) inhibits NCX1 activity. In the context of Na+/K+-ATPase (NKA) regulation, pSer-68-PLM is dephosphorylated by protein phosphatase 1 (PP1). PP1 also associates with NCX1; however, the molecular basis of this association is unknown. In this study, we aimed to analyze the mechanisms of PP1 targeting to the NCX1-pSer-68-PLM complex and hypothesized that a direct and functional NCX1-PP1 interaction is a prerequisite for pSer-68-PLM dephosphorylation. Using a variety of molecular techniques, we show that PP1 catalytic subunit (PP1c) co-localized, co-fractionated, and co-immunoprecipitated with NCX1 in rat cardiomyocytes, left ventricle lysates, and HEK293 cells. Bioinformatic analysis, immunoprecipitations, mutagenesis, pulldown experiments, and peptide arrays constrained PP1c anchoring to the K(I/V)FF motif in the first Ca2+ binding domain (CBD) 1 in NCX1. This binding site is also partially in agreement with the extended PP1-binding motif K(V/I)FF-X5–8Φ1Φ2-X8–9-R. The cytosolic loop of NCX1, containing the K(I/V)FF motif, had no effect on PP1 activity in an in vitro assay. Dephosphorylation of pSer-68-PLM in HEK293 cells was not observed when NCX1 was absent, when the K(I/V)FF motif was mutated, or when the PLM- and PP1c-binding sites were separated (mimicking calpain cleavage of NCX1). Co-expression of PLM and NCX1 inhibited NCX1 current (both modes). Moreover, co-expression of PLM with NCX1(F407P) (mutated K(I/V)FF motif) resulted in the current being completely abolished. In conclusion, NCX1 is a substrate-specifying PP1c regulator protein, indirectly regulating NCX1 activity through pSer-68-PLM dephosphorylation