7 research outputs found
On the Polarization of H-alpha Lines Scattered by Neutral Hydrogen in Active Galactic Nuclei
Raman scattering by atomic hydrogen converts the UV continuum around
Ly into optical continuum around H, and the basic atomic physics
has been discussed in several works on symbiotic stars. We propose that the
same process may operate in active galactic nuclei (AGN) and calculate the
linear polarization of the broad emission lines Raman-scattered by a high
column neutral hydrogen compnent. The conversion efficiency of the Raman
scattering process is discussed and the expected scattered flux is computed
using the spectral energy distribution of an AGN given by a typical power law.
The high column H {\sc i} component in AGN is suggested by many observations
encompassing radio through UV and X-ray ranges. When the neutral hydrogen
component with a column density is present around the
active nucleus, it is found that the scattered H is characterized by a
very broad width and that the strength of the polarized flux
is comparable to that of the electron-scattered flux expected from a
conventional unified model of narrow line AGN. The width of the scattered flux
is mainly determined by the column density of the neutral scatterers where the
total scattering optical depth becomes of order unity. The asymmetry in the
Raman scattering cross section around Ly introduces red asymmetric
polarized profiles around H. The effects of the blended Ly and O
{\sc vi} 1034 doublet are also investigated. We briefly discuss the
spectropolarimetric observations performed on the Seyfert galaxy IRAS
110548-1131 and the narrow line radio galaxy Cyg A.Comment: 11 pages, 6 figures, accepted for publication in MNRA
Melittin (MEL) inhibited the HIF-1α protein accumulation induced by the EGF in the CaSki cells.
<p>(A) Dose-dependent effect of MEL on the viability of CaSki cells. Cells were treated with the indicated concentrations of MEL for 24 h. Viability was determined by WST-1 assay. Values represent the means ± SD of triplicate assays. *, <i>p</i><0.05 as compared to untreated control. Results were analyzed using one-way ANOVA. (B) Cells were pretreated with the indicated concentrations of MEL for 30 min, and then induced by EGF treatment for 6 h. (C) Cells were pretreated with the indicated concentrations of MEL for 30 min, and then induced by CoCl<sub>2</sub> treatment for 6 h. Nuclear extracts were subjected to Western blot using antibodies against HIF-1α and HIF-1β.</p
Melittin (MEL) suppressed the EGF-induced migration and angiogenesis in the CaSki cells.
<p>(A and B) CaSki 3×10<sup>4</sup> cells/ml were mixed with 0.5 ml of Matrigel in the presence or absence of EGF (500 ng/ml) and MEL (1 and 2 µg/ml) in vivo. (C and D) Matrigel migration assay was carried out MEL (1 and 2 µg/ml) in the presence of EGF (20 ng/ml). After 24 h incubation, cells bottom side of filter were fixed, stained and counted. Data represents the means ± SD of three independent experiments. *, <i>p</i><0.05 as compared to EGF-treated control. Results were analyzed using one-way ANOVA.</p
Melittin (MEL) suppressed the EGF-induced HIF-1α protein synthesis by inhibiting the ERK and mTOR/p70S6K signaling pathways in the CaSki cells.
<p>(A) Effect of MEL on EGF-induced signaling leading to the expression of HIF-1α in CaSki cells. CaSki cells were pretreated with the indicated concentrations of MEL for 1 h, followed by incubation with EGF for 30 min. The phosphorylated levels of EGFR, P38, ERK, JNK, Akt, mTOR and p70S6K were determined by Western blot analysis. (B) Effects of MEL and inhibitors on EGF-induced expression of HIF-1α in CaSki cells. CaSki cells were pretreated with MEL, SB203580, SP600125, PD98059, wortmannin, rapamycin for 30 min, and then induced by EGF treatment for 6 h. Nuclear extracts were subjected to Western blot using antibodies against HIF-1α or β-actin. Data represents the means ± SD of three independent experiments. *, <i>p</i><0.05 as compared to EGF-treated control. Results were analyzed using one-way ANOVA.</p