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- Abelev, B., et al.
(författare)
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K*(892)(0) and phi(1020) production in Pb-Pb collisions at root s(NN)=2.76 TeV
- 2015
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Ingår i: Physical Review C (Nuclear Physics). - 0556-2813. ; 91:2
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Tidskriftsartikel (refereegranskat)abstract
- The yields of the K*(892)(0) and phi(1020) resonances are measured in Pb-Pb collisions at root s(NN) = 2.76 TeV through their hadronic decays using the ALICE detector. The measurements are performed in multiple centrality intervals at mid-rapidity (vertical bar y vertical bar < 0.5) in the transverse-momentum ranges 0.3 < p(T) < 5 GeV/c for the K*(892)(0) and 0.5 < p(T) < 5 GeV/c for the phi(1020). The yields of K*(892)(0) are suppressed in central Pb-Pb collisions with respect to pp and peripheral Pb-Pb collisions (perhaps due to rescattering of its decay products in the hadronic medium), while the longer-lived phi(1020) meson is not suppressed. These particles are also used as probes to study the mechanisms of particle production. The shape of the pT distribution of the phi(1020) meson, but not its yield, is reproduced fairly well by hydrodynamic models for central Pb-Pb collisions. In central Pb-Pb collisions at low and intermediate p(T), the p/phi(1020) ratio is flat in p(T), while the p/pi and phi(1020)/pi ratios show a pronounced increase and have similar shapes to each other. These results indicate that the shapes of the p(T) distributions of these particles in central Pb-Pb collisions are determined predominantly by the particle masses and radial flow. Finally, phi(1020) production in Pb-Pb collisions is enhanced, with respect to the yield in pp collisions and the yield of charged pions, by an amount similar to the Lambda and Xi.
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| 4. |
- Sjölander, Jonatan, et al.
(författare)
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C4b-binding Protein Protects -Cells from Islet Amyloid Polypeptide-induced Cytotoxicity
- 2016
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 291:41, s. 21644-21655
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Tidskriftsartikel (refereegranskat)abstract
- C4BP (C4b-binding protein) is a polymer of seven identical chains and one unique chain synthesized in liver and pancreas. We showed previously that C4BP enhances islet amyloid polypeptide (IAPP) fibril formation in vitro. Now we report that polymeric C4BP strongly inhibited lysis of human erythrocytes incubated with monomeric IAPP, whereas no lysis was observed after incubation with preformed IAPP fibrils. In contrast, incubation with the monomeric -chain of C4BP was less effective. These data indicate that polymeric C4BP with multiple binding sites for IAPP neutralizes lytic activity of IAPP. Furthermore, addition of monomeric IAPP to a rat insulinoma cell line (INS-1) resulted in decreased cell viability, which was restored in the presence of physiological concentrations of C4BP. Treatment of INS-1 cells and primary rat islets with IAPP also diminished their ability to secrete insulin upon stimulation with glucose, which was reversed in the presence of C4BP. Further, C4BP was internalized together with IAPP into INS-1 cells. Pathway analyses of mRNA expression microarray data indicated that cells exposed to C4BP and IAPP in comparison with IAPP alone increased expression of genes involved in cholesterol synthesis. Depletion of cholesterol through methyl--cyclodextrin or cholesterol oxidase abolished the protective effect of C4BP on IAPP cytotoxicity of INS-1 cells. Also, inhibition of phosphoinositide 3-kinase but not NF-B had a similar effect. Taken together, C4BP protects -cells from IAPP cytotoxicity by modulating IAPP fibril formation extracellularly and also, after uptake by the cells, by enhancing cholesterol synthesis.
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