Muon radiography and deformation analysis of the lava dome formed by the 1944 eruption of Usu, Hokkaido —Contact between high-energy physics and volcano physics—

Lava domes are one of the conspicuous topographic features on volcanoes. The subsurface structure of the lava dome is important to discuss its formation mechanism. In the 1944 eruption of Volcano Usu, Hokkaido, a new lava dome was formed at its eastern foot. After the completion of the lava dome, various geophysical methods were applied to the dome to study its subsurface structure, but resulted in a rather ambiguous conclusion. Recently, from the results of the levelings, which were repeated during the eruption, “pseudo growth curves” of the lava dome were obtained. The curves suggest that the lava dome has a bulbous shape. In the present work, muon radiography, which previously proved effective in imaging the internal structure of Volcano Asama, has been applied to the Usu lava dome. The muon radiography measures the distribution of the “density length” of volcanic bodies when detectors are arranged properly. The result obtained is consistent with the model deduced from the pseudo growth curves. The measurement appears to afford useful method to clarify the subsurface structure of volcanoes and its temporal changes, and in its turn to discuss volcanic processes. This is a point of contact between high-energy physics and volcano physics

GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane

Over-expression of N-acetylgalactosamine glycoproteins as detected by binding of the lectin from Helix pomatia (HPA), is associated with metastatic competence and poor patient prognosis in a range of human adenocarcinomas. These glycoproteins remain poorly characterised, and their functional role has yet to be elucidated. This study describes characterisation of a range of human breast/breast cancer cell lines for the expression of the N-acetylgalactosaminylated glycoproteins of interest, and their comparison with normal breast epithelium and a range of clinical breast carcinoma samples. Confocal and light microscopy studies revealed cytochemical HPA-binding patterns consistent with a fundamental disruption in normal glycobiosynthetic pathways attending increasing metastatic potential. We report the most complete comparative analysis of HPA-binding ligands from cultured breast cells, clinical breast carcinoma samples and normal breast epithelium to date. Lectin blotting identified 11 major HPA-binding glycoprotein bands common to both clinical tumour samples and breast cell lines and 6 of these bands were also expressed by samples of normal breast epithelium, albeit at much lower levels. Moreover, very marked quantitative but not qualitative differences in levels of expression consistent with metastatic capability were noted. © 2001 Cancer Research Campaignhttp://www.bjcancer.co

In situ annealing of superconducting MgB2 films prepared by pulsed laser deposition

The in situ annealing conditions of pulsed laser deposited MgB2 films were studied. The precursor films were deposited at 250 C from a stoichiometric MgB2 target in a 120mTorr Ar atmosphere. The films were then in situ annealed at a temperature from 450 C to 800 C and an annealing time from 1 minute to 10 minutes. We found that the superconducting properties depend in a crucial way on the annealing conditions: temperature, heating rate and time. The best film with a thickness of ~600nm was obtained under the following annealing conditions: Tanneal=680-690 C, tanneal=1 min, heating rate= 38 C/min. The Tc onset of the film is 28K with a transition width of ~10K. The hysteresis loop of magnetic moment of the film indicates weak field dependence in high fields. Magneto-optical imaging of the film showed quite homogeneous magnetic flux penetration, indicating structural homogeneity. The films without annealing showed no superconductivity.Comment: 12 pages, 6 figure

Modulation of RANTES expression by HCV core protein in liver derived cell lines

<p>Abstract</p> <p>Background</p> <p>Hepatitis C virus (HCV) infection is associated with high percentage of chronicity which implies the ability of the virus to evade or modulate host cell immune system. Modulation of chemokines, such as RANTES may be part of the virus induced pathogenicity. We examined the effect of core and structural proteins of HCV on RANTES expression in two liver derived cell lines, HepG2 and Chang Liver (CHL).</p> <p>Methods</p> <p>HepG2 and Chang Liver (CHL) cell lines were established and selected for constitutive expression of HCV core and structural genes. Flow cytometry and quantitative RT-PCR analysis were performed to examine the effect of HCV core protein on RANTES expression. Luciferase analysis after RANTES-Luc-promoter transfection of established cell lines was assayed by luminometer measurements (RLU) of RANTES promoter activity. IRF-1 and IRF-7 expression was then examined by immunoblotting analysis.</p> <p>Results</p> <p>Results of flow cytometry and RT-PCR analysis indicated that RANTES is differentially regulated by HCV core protein in the two cell lines examined as its expression was inhibited in HepG2 cells, by a reduction of RANTES promoter activity. Conversely, RANTES protein and mRNA were induced by the core protein in CHL cells, through the induction of the promoter.</p> <p>Since HCV genome modulates IRF-1 and IRF-7 in replicon system and IRF-1, IRF-3 and IRF-7 have been reported to regulate RANTES promoter in various cell systems, analysis of the mechanism underlying RANTES modulation by the core protein revealed that IRF-1 expression was induced in HepG2 cells by the core protein, whereas in CHL cells it was expressed at a very low level that was not influenced by transfection with the core protein construct. This suggested that IRF-1 level may mediate the expression of RANTES in cell lines of liver origin. The effect of the core protein on RANTES promoter was countered by co-transfection with NF90, a double-stranded-RNA binding protein that activates some interferon response genes and acts as a component of cell defense against viral infection.</p> <p>Conclusion</p> <p>HCV core protein have opposite effects on the expression of RANTES in different cell types <it>in vitro</it>, possibly reflecting a similar scenario in different microenvironments <it>in vivo</it>.</p

A European-Japanese study on peach allergy : IgE to Pru p 7 associates with severity

Funding Information: M. Fernández‐Rivas received grants or contracts from Instituto de Salud Carlos III, Spanish Government, Aimmune Therapeutics, Diater, and Novartis; payment or honoraria for lectures, presentations, speakers bureaus, manuscript writing, or educational events from Aimmune Therapeutics, Ediciones Mayo S.A., Diater, Ga2LEN, HAL Allergy, GSK, MEDSCAPE, NOVARTIS, and EPG Health; is member of the Data Safety Monitoring Board at DBV and advisory board at Aimmune Therapeutics, Novartis, Reacta Healthcare, and SPRIM. B. Ballmer‐Weber received consulting fees from ALK, Allergopharma, Menarini, Sanofi, Novartis, Thermofisher and Aimune and payment or honoraria for lectures, presentations, speakers bureaus, manuscript writing or educational events from ALK, Menarini, Sanofi, Novartis, and Thermofisher. F. De Blay received grants or contract from Aimmune, Stallergenes Greer, GSK, ALK, Chiesi, and Regeneron. Y. Fukutomi received payment or honoraria for lectures, presentations, speakers bureaus, manuscript writing, or educational events from Thermo Fisher Diagnostics KK. K. Hoffmann‐Sommergruber received funding from Danube Allergy Research Cluster funded by the Country of Lower Austria to (P07) KHS; was Member of the EAACI board until 2022/07. J. Lidholm is employee at Thermo Fisher Scientific. E.N.C Mills received grants or has contracts from Food Standards Agency Patterns and prevalence of adult food allergy (FS101174), European Food Safety Authority (ThRAll; allergenicity prediction [with EuroFIR]) and from Innovate (ML for food allergy); has applied for a patent on oral food challenge meal formulations for diagnosis of food allergy; is member of the Advisory Board of Novartis and Advisory Committee on Novel Foods and Processes; and is shareholder of Reacta Healthcare Ltd. N.G. Papadopoulos received grants or contracts from Capricare, Nestle, Numil, Vianex; received consultancy fees from Abbott, Abbvie, Astra Zeneca, GSK, HAL, Medscape, Menarini/Faes Farma, Mylan, Novartis, Nutricia, OM Pharma, and Regeneron/Sanofi. S. Vieths received royalties or licenses from Schattauer Allergologie Handbuch, Elsevier Nahrungsmittelallergien and Intoleranzen and Karger Food Allergy: Molecular Basis and Clinical Practice; support for attending meetings and/or travel as Associate Editor of the Journal of Allergy and Clinical Immunology. R. van Ree received consulting fees from HAL Allergy, Citeq, Angany, Reacta Healthcare, Mission MightyMe, and Ab Enzymes; received payment of honoraria for lectures, presentations, speakers bureaus, manuscript writing or educational events from HAL Allergy, Thermo Fisher Scientific and ALK; received payment for expert testimony from AB Enzymes; has stock option at Angany. The rest of the authors declare that they have no relevant conflicts of interest. Funding Information: This work was funded by the European Commission under the 6th Framework Programme through EuroPrevall (FP6‐FOOD‐CT‐2005‐514000), and the 7th Framework Programme iFAAM (grant agreement no. 31214). Funding Information: We thank all the patients for their participation in the study. We would like to thank ALK Abello (Madrid, Spain) for their generous gift of SPT reagents. We thank Angelica Ehrenberg, Jonas Östling and Lars Mattsson (Uppsala) for preparing recombinant Cup s 7 and custom ImmunoCAP tests for this study. We acknowledge the support by the 6th and 7th Framework Programmes of the EU, for EuroPrevall (FP6‐FOOD‐CT‐2005‐514000) and iFAAM (Grant agreement no. 312147), respectively. We thank Alejandro Gonzalo Fernández (Hospital Clinico San Carlos, IdISSC, Madrid) for implementing the FASS in the data set. Publisher Copyright: © 2023 The Authors. Allergy published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd.BACKGROUND: Pru p 3 and Pru p 7 have been implicated as risk factors for severe peach allergy. This study aimed to establish sensitization patterns to five peach components across Europe and in Japan, to explore their relation to pollen and foods and to predict symptom severity. METHODS: In twelve European (EuroPrevall project) and one Japanese outpatient clinic, a standardized clinical evaluation was conducted in 1231 patients who reported symptoms to peach and/or were sensitized to peach. Specific IgE against Pru p 1, 2, 3, 4 and 7 and against Cup s 7 was measured in 474 of them. Univariable and multivariable Lasso regression was applied to identify combinations of parameters predicting severity. RESULTS: Sensitization to Pru p 3 dominated in Southern Europe but was also quite common in Northern and Central Europe. Sensitization to Pru p 7 was low and variable in the European centers but very dominant in Japan. Severity could be predicted by a model combining age of onset of peach allergy, probable mugwort, Parietaria pollen and latex allergy, and sensitization to Japanese cedar pollen, Pru p 4 and Pru p 7 which resulted in an AUC of 0.73 (95% CI 0.73-0.74). Pru p 3 tended to be a risk factor in South Europe only. CONCLUSIONS: Pru p 7 was confirmed as a significant risk factor for severe peach allergy in Europe and Japan. Combining outcomes from clinical and demographic background with serology resulted in a model that could better predict severity than CRD alone.Peer reviewe