WASP-54b, WASP-56b and WASP-57b: Three new sub-Jupiter mass planets from SuperWASP

We present three newly discovered sub-Jupiter mass planets from the SuperWASP survey: WASP-54b is a heavily bloated planet of mass 0.636$^{+0.025}_{-0.024}$ \mj and radius 1.653$^{+0.090}_{-0.083}$ \rj. It orbits a F9 star, evolving off the main sequence, every 3.69 days. Our MCMC fit of the system yields a slightly eccentric orbit ($e=0.067^{+0.033}_{-0.025}$) for WASP-54b. We investigated further the veracity of our detection of the eccentric orbit for WASP-54b, and we find that it could be real. However, given the brightness of WASP-54 V=10.42 magnitudes, we encourage observations of a secondary eclipse to draw robust conclusions on both the orbital eccentricity and the thermal structure of the planet. WASP-56b and WASP-57b have masses of 0.571$^{+0.034}_{-0.035}$ \mj and $0.672^{+0.049}_{-0.046}$ \mj, respectively; and radii of $1.092^{+0.035}_{-0.033}$ \rj for WASP-56b and $0.916^{+0.017}_{-0.014}$ \rj for WASP-57b. They orbit main sequence stars of spectral type G6 every 4.67 and 2.84 days, respectively. WASP-56b and WASP-57b show no radius anomaly and a high density possibly implying a large core of heavy elements; possibly as high as $\sim$50 M$_{\oplus}$ in the case of WASP-57b. However, the composition of the deep interior of exoplanets remain still undetermined. Thus, more exoplanet discoveries such as the ones presented in this paper, are needed to understand and constrain giant planets' physical properties.

Cloning and characterization of the mouse homologue of the human dendritic cell maturation marker CD208/DC-LAMP

DC-LAMP, a member of the lysosomal-associated membrane protein (LAMP) family, is specifically expressed by human dendritic cells (DC) upon activation and therefore serves as marker of human DC maturation. DC-LAMP is detected first in activated human DC within MHC class II molecules-containing compartments just before the translocation of MHC class II-peptide complexes to the cell surface, suggesting a possible involvement in this process. The present study describes the cloning and characterization of mouse DC-LAMP, whose predicted protein sequence is over 50% identical to the human counterpart. The mouse DC-LAMP gene spans over 25 kb and shares syntenic chromosomal localization (16B2-B4 and 3q26) and conserved organization with the human DC-LAMP gene. Analysis of mouse DC-LAMP mRNA and protein revealed the expression in lung peripheral cells, but also its unexpected absence from mouse lymphoid organs and from mouse DC activated either in vitro or in vivo. In conclusion, mouse DC-LAMP is not a marker of mature mouse DC and this observation raises new questions regarding the role of human DC-LAMP in human DC.

Enhancement of Ca2+-dependent outward current in sheep bladder myocytes by evans blue dye.

Whole-cell and inside-out patch-clamp techniques were used to assess the action of a well-known dye, Evans blue, on membrane currents in bladder isolated smooth muscle cells from sheep. In whole cells Evans blue dose-dependently increased the outward current by up to fivefold. In contrast, Evans blue had no effect on inward Ca2+ current. The effect on outward current was abolished or reduced if the cells were bathed in Ca2+-free solution, iberiotoxin (5 x 10(-8) M), or charybdotoxin (5 x 10(-8) M), but was unaffected by externally applied caffeine (5 mM) or in cells exposed to heparin (1 mg/ml) via the patch pipette. In inside-out patches bathed in a Ca2+ concentration of 5 x 10(-7) M, Evans blue (10(-4) M) increased the open probability of large-conductance (298-pS) Ca2+-dependent K+ channels (BK channels), shifting the half maximal-activation voltage by -70 mV. We conclude that Evans blue dye acts as an opener of BK channels.

Downregulation of beta1,4-galactosyltransferase 1 inhibits CDK11(p58)-mediated apoptosis induced by cycloheximide.

Cyclin-dependent kinase 11 (CDK11; also named PITSLRE) is part of the large family of p34(cdc2)-related kinases whose functions appear to be linked with cell cycle progression, tumorigenesis, and apoptotic signaling. The mechanism that CDK11(p58) induces apoptosis is not clear. Some evidences suggested beta1,4-galactosyltransferase 1 (beta1,4-GT 1) might participate in apoptosis induced by CDK11(p58). In this study, we demonstrated that ectopically expressed beta1,4-GT 1 increased CDK11(p58)-mediated apoptosis induced by cycloheximide (CHX). In contrast, RNAi-mediated knockdown of beta1,4-GT 1 effectively inhibited apoptosis induced by CHX in CDK11(p58)-overexpressing cells. For example, the cell morphological and nuclear changes were reduced; the loss of cell viability was prevented and the number of cells in sub-G1 phase was decreased. Knock down of beta1,4-GT 1 also inhibited the release of cytochrome c from mitochondria and caspase-3 processing. Therefore, the cleavage of CDK11(p58) by caspase-3 was reduced. We proposed that beta1,4-GT 1 might contribute to the pro-apoptotic effect of CDK11(p58). This may represent a new mechanism of beta1,4-GT 1 in CHX-induced apoptosis of CDK11(p58)-overexpressing cells.