Characterizing the automatic radon flux transfer standard system Autoflux: laboratory calibration and field experiments

High-quality, long-term measurements of terrestrial trace gas emissions are important for investigations of atmospheric, geophysical and biological processes to help mitigate climate change and protect the environment and the health of citizens. High-frequency terrestrial fluxes of the radioactive noble gas 222Rn, in particular, are useful for validating radon flux maps and used to evaluate the performance of regional atmospheric models, to improve greenhouse gas emission inventories (by the radon tracer method) and to determine radon priority areas for radiation protection goals. A new automatic radon flux system (Autoflux) was developed as a transfer standard (TS) to assist with establishing a traceability chain for field-based radon flux measurements. The operational characteristics and features of the system were optimized based on a literature review of existing flux measurement systems. To characterize and calibrate Autoflux, a bespoke radon exhalation bed (EB) facility was also constructed with the intended purpose of providing a constant radon exhalation under a specific set of controlled laboratory conditions. The calibrated Autoflux was then used to transfer the derived calibration to a second continuous radon flux system under laboratory conditions; both instruments were then tested in the field and compared with modeled fluxes. This paper presents (i) a literature review of state-of-the-art radon flux systems and EB facilities; (ii) the design, characterization and calibration of a reference radon EB facility; (iii) the design, characterization and calibration of the Autoflux system; (iv) the calibration of a second radon flux system (INTE_Flux) using the EB and Autoflux, with a total uncertainty of 9 % (k = 1) for an average radon flux of ∼ 1800 mBq m−2 s−1 under controlled laboratory conditions; and (v)​​​​​​​ an example application of the calibrated TS and INTE_Flux systems for in situ radon flux measurements, which are then compared with simulated radon fluxes. Calibration of the TS under different environmental conditions and at lower reference fluxes will be the subject of a separate future investigation.</p

Association of CD99 short and long forms with MHC class I, MHC class II and tetraspanin CD81 and recruitment into immunological synapses

<p>Abstract</p> <p>Background</p> <p>CD99, a leukocyte surface glycoprotein, is broadly expressed in many cell types. On the cell surface, CD99 is expressed as two distinct isoforms, a long form and a short form. CD99 has been demonstrated to play a key role in several biological processes, including the regulation of T cell activation. However, the molecular mechanisms by which CD99 participates in such processes are unclear. As CD99 contains a short cytoplasmic tail, it is unlikely that CD99 itself takes part in its multi-functions. Association of CD99 with other membrane proteins has been suggested to be necessary for exerting its functions.</p> <p>Results</p> <p>In this study, we analyzed the association of CD99 with other cell surface molecules involved in T cell activation. We demonstrate the association of MHC class I, MHC class II and tetraspanin CD81 with CD99 molecules on the cell surface. Association of CD99 with its partners was observed for both isoforms. In addition, we determined that CD99 is a lipid raft-associated membrane protein and is recruited into the immunologic synapse during T cell activation. The implication of CD99 on T cell activation was investigated. Inhibition of anti-CD3 induced T cell proliferation by an anti-CD99 monoclonal antibody was observed.</p> <p>Conclusions</p> <p>We provide evidence that CD99 directly interact and form the complex with the MHC class I and II, and tetraspanin CD81, and is functionally linked to the formation of the immunologic synapse. Upon T cell activation, CD99 engagement can inhibit T cell proliferation. We speculate that the CD99-MHC-CD81 complex is a tetraspanin web that plays an important role in T cell activation.</p

Essential Roles for Soluble Virion-Associated Heparan Sulfonated Proteoglycans and Growth Factors in Human Papillomavirus Infections

A subset of human papillomavirus (HPV) infections is causally related to the development of human epithelial tumors and cancers. Like a number of pathogens, HPV entry into target cells is initiated by first binding to heparan sulfonated proteoglycan (HSPG) cell surface attachment factors. The virus must then move to distinct secondary receptors, which are responsible for particle internalization. Despite intensive investigation, the mechanism of HPV movement to and the nature of the secondary receptors have been unclear. We report that HPV16 particles are not liberated from bound HSPG attachment factors by dissociation, but rather are released by a process previously unreported for pathogen-host cell interactions. Virus particles reside in infectious soluble high molecular weight complexes with HSPG, including syndecan-1 and bioactive compounds, like growth factors. Matrix mellatoproteinase inhibitors that block HSPG and virus release from cells interfere with virus infection. Employing a co-culture assay, we demonstrate HPV associated with soluble HSPG-growth factor complexes can infect cells lacking HSPG. Interaction of HPV-HSPG-growth factor complexes with growth factor receptors leads to rapid activation of signaling pathways important for infection, whereas a variety of growth factor receptor inhibitors impede virus-induced signaling and infection. Depletion of syndecan-1 or epidermal growth factor and removal of serum factors reduce infection, while replenishment of growth factors restores infection. Our findings support an infection model whereby HPV usurps normal host mechanisms for presenting growth factors to cells via soluble HSPG complexes as a novel method for interacting with entry receptors independent of direct virus-cell receptor interactions

Corruption and the shadow economy: an empirical analysis

Corruption, Shadow economy, Regulation, Tax burden, D73, H26, 017, 05,