Single-Particle Spin-Orbit Strengths of the Nucleon and Hyperons by SU6 Quark-Model

The quark-model hyperon-nucleon interaction suggests an important antisymmetric spin-orbit component. It is generated from a color analogue of the Fermi-Breit interaction dominating in the one-gluon exchange process between quarks. We discuss the strength S_B of the single-particle spin-orbit potential, following the Scheerbaum's prescription. Using the SU6 quark-model baryon-baryon interaction which was recently developed by the Kyoto-Niigata group, we calculate NN, Lambda N and Sigma N G-matrices in symmetric nuclear matter and apply them to estimate the strength S_B. The ratio of S_B to the nucleon strength S_N =~ -40 MeV*fm^5 is (S_Lambda)/(S_N) =~ 1/5 and (S_Sigma)/(S_N) =~ 1/2 in the Born approximation. The G-matrix calculation of the model FSS modifies S_Lambda to (S_Lambda)/(S_N) =~ 1/12. For S_N and S_Sigma, the effect of the short-range correlation is comparatively weak against meson-exchange potentials with a short-range repulsive core. The significant reduction of the Lambda single-particle potential arises from the combined effect of the antisymmetric LS force, the flavor-symmetry breaking originating from the strange to up-down quark-mass difference, as well as the effect of the short-range correlation. The density dependence of S_B is also examined.Comment: 26 page

Involvement of TRPV3 and TRPM8 ion channel proteins in induction of mammalian cold-inducible proteins

Cold-inducible RNA-binding protein (CIRP), RNA-binding motif protein 3 (RBM3) and serine and arginine rich splicing factor 5 (SRSF5) are RNA-binding proteins that are transcriptionally upregulated in response to moderately low temperatures and a variety of cellular stresses in mammalian cells. Induction of these cold-inducible proteins (CIPs) is dependent on transient receptor potential (TRP) V4 channel protein, but seems independent of its ion channel activity. We herein report that in addition to TRPV4, TRPV3 and TRPM8 are necessary for the induction of CIPs. We established cell lines from the lung of TRPV4-knockout (KO) mouse, and observed induction of CIPs in them by western blot analysis. A TRPV4 antagonist RN1734 suppressed the induction in wild-type mouse cells, but not in TRPV4-KO cells. A TRPV3 channel blocker S408271 and a TRPM8 channel blocker AMTB as well as siRNAs against TRPV3 and TRPM8 suppressed the CIP induction in mouse TRPV4-KO cells and human U-2 OS cells. A TRPV3 channel agonist 2-APB induced CIP expression, but camphor did not. Neither did a TRPM8 channel agonist WS-12. These results suggest that TRPV4, TRPV3 and TRPM8 proteins, but not their ion channel activities are necessary for the induction of CIPs at 32 °C. Identification of proteins that differentially interact with these TRP channels at 37 °C and 32 °C would help elucidate the underlying mechanisms of CIP induction by hypothermia

ACCELERATED AROMATIC COMPOUNDS DEGRADATION IN AQUATIC ENVIRONMENT BY USE OF INTERACTION BETWEEN SPIRODELA POLYRRHIZA AND BACTERIA IN ITS RHIZOSPHERE

Joint Research on Environmental Science and Technology for the Eart