Photometric Metallicity Calibration with SDSS and SCUSS and its Application to distant stars in the South Galactic Cap

Based on SDSS g, r and SCUSS (South Galactic Cap of u-band Sky Survey) $u$ photometry, we develop a photometric calibration for estimating the stellar metallicity from $u-g$ and $g-r$ colors by using the SDSS spectra of 32,542 F- and G-type main sequence stars, which cover almost $3700$ deg$^{2}$ in the south Galactic cap. The rms scatter of the photometric metallicity residuals relative to spectrum-based metallicity is $0.14$ dex when $g-r<0.4$, and $0.16$ dex when $g-r>0.4$. Due to the deeper and more accurate magnitude of SCUSS $u$ band, the estimate can be used up to the faint magnitude of $g=21$. This application range of photometric metallicity calibration is wide enough so that it can be used to study metallicity distribution of distant stars. In this study, we select the Sagittarius (Sgr) stream and its neighboring field halo stars in south Galactic cap to study their metallicity distribution. We find that the Sgr stream at the cylindrical Galactocentric coordinate of $R\sim 19$ kpc, $\left| z\right| \sim 14$ kpc exhibits a relative rich metallicity distribution, and the neighboring field halo stars in our studied fields can be modeled by two-Gaussian model, with peaks respectively at [Fe/H]$=-1.9$ and [Fe/H]$=-1.5$.Comment: 8 pages, 7 figures, Accepted for publication in MNRA

Functional Impact Of 14 Single Nucleotide Polymorphisms Causing Missense Mutations Of Human α7 Nicotinic Receptor

The α7nicotinic receptor (nAChR) is a major subtype of the nAChRs in the central nervous system, and the receptor plays an important role in brain function. In the dbSNP database, there are 55 single nucleotide polymorphisms (SNPs) that cause missense mutations of the human α7nAChR in the coding region. In this study, we tested the impact of 14 SNPs that cause missense mutations in the agonist binding site or the coupling region between binding site and channel gate on the receptor function. The wild type or mutant receptors were expressed or co-expressed in Xenopus oocytes, and the agonist-induced currents were tested using two-electrode voltage clamp. Our results demonstrated that 6 mutants were nonfunctional, 4 mutants had reduced current expression, and 1 mutants altered ACh and nicotine efficacy in the opposite direction, and one additional mutant had slightly reduced agonist sensitivity. Interestingly, the function of most of these nonfunctional mutants could be rescued by α7nAChR positive allosteric modulator PNU-120596 and agonist-PAM 4BP-TQS. Finally, when coexpressed with the wild type, the nonfunctional mutants could also influence the receptor function. These changes of the receptor properties by the mutations could potentially have an impact on the physiological function of the α7nAChR-mediated cholinergic synaptic transmission and anti-inflammatory effects in the human SNP carriers. Rescuing the nonfunctional mutants could provide a novel way to treat the related disorders. Copyright