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Throughout the body there are smooth muscle cells controlling a myriad of tubes and reservoirs. The cells show enormous diversity and complexity compounded by a plasticity that is critical in physiology and disease. Over the past quarter of a century we have seen that smooth muscle cells contain – as part of a gamut of ion-handling mechanisms – a family of cationic channels with significant permeability to calcium, potassium and sodium. Several of these channels are sensors of calcium store depletion, G-protein-coupled receptor activation, membrane stretch, intracellular Ca2+, pH, phospholipid signals and other factors. Progress in understanding the channels has, however, been hampered by a paucity of specific pharmacological agents and difficulty in identifying the underlying genes. In this review we summarize current knowledge of these smooth muscle cationic channels and evaluate the hypothesis that the underlying genes are homologues of Drosophila TRP (transient receptor potential). Direct evidence exists for roles of TRPC1, TRPC4/5, TRPC6, TRPV2, TRPP1 and TRPP2, and more are likely to be added soon. Some of these TRP proteins respond to a multiplicity of activation signals – promiscuity of gating that could enable a variety of context-dependent functions. We would seem to be witnessing the first phase of the molecular delineation of these cationic channels, something that should prove a leap forward for strategies aimed at developing new selective pharmacological agents and understanding the activation mechanisms and functions of these channels in physiological systems.

Periodic antidot arrays imposed upon two-dimensional hole systems (2DHSs) display a striking dependence of the positive low-field magnetoresistance on the in-plane crystallographic orientation of the superlattice. An enhanced positive magnetoresistance can be ascribed to the 2DHSs non-circular Fermi surface which stabilizes chaotic trajectories for specific crystallographic directions. The effect provides a first example of the role of non-spherical Fermi surfaces on the classical chaotic dynamics of charge carriers. Transport calculations taking into account both the classical chaotic motion of the holes in antidot lattices and the warped Fermi contour confirm this picture.

We measured the magnetoresistance of bilayer quantum Hall (QH) effects at the fractional filling factor $��=2/3$ by changing the total electron density and the density difference between two layers. Three different QH states were separated by two types of phase transition: One is the spin transition and the other is the pseudospin transition. In addition, two different hystereses were detected, one of which is specific to bilayer systems. The phase transitions and the hystereses are described well by a composite fermion model extended to a bilayer system., 4 pages, 5 figures

Physical Review Letters

By tilting the samples in the magnetic field, we measured and compared the Skyrmion excitations in the bilayer quantum Hall (QH) state at the Landau-level filling factor $��=2$ and in the monolayer QH state at $��=1$. The observed number of flipped spins is $N_s=14$ in the bilayer system with a large tunneling gap, and $N_s=7$ in the bilayer system with a small tunneling gap, while it is $N_s=7$ in the monolayer system. The difference is interpreted due to the interlayer exchange interaction. Moreover, we have observed seemingly preferred numbers $N_s=14,7,1$ for the flipped spins by tilting bilayer samples., 4 pages, 4 figures

Direct effects of ONO-1101 ¿(-)-[(S)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl-3-[4-[(S) -2-hydroxy-3-(2-morpholino carbonylamino)ethylamino] propoxy]phenylpropionate monohydrochloride), a novel beta-antagonist, on action potential parameters and membrane currents, and its beta adrenoceptor antagonism were examined in cardiac muscle. Action potential-parameters in papillary muscle of reserpinized animals and membrane currents recorded from single myocytes obtained from guinea pig and rabbit hearts were not affected by 1 to 100 microM ONO-1101. On the other hand, ONO-1101 markedly inhibited the potentiation of Ca current by isoproterenol in single cardiac myocytes of the guinea pig. The concentration-response relationship of Ca current for isoproterenol was shifted to the right. This effect resembled that of esmolol, which is also a beta adrenoceptor antagonist. A Schild plot analysis revealed the slope and pA2 value of each antagonist (ONO-1101, 0.94, 8.0; and esmolol, 0.98, 7.3, respectively) and demonstrated that ONO-1101 is about 5 times more potent than esmolol as a beta-antagonist. Two other effects of isoproterenol: 1) potentiation of delayed rectifier K current and 2) activation of chloride current, were also inhibited by ONO-1101. The time required for 50% removal of beta-antagonism of ONO-1101 and esmolol after the washout was estimated as 4 and 6 min, respectively, in depolarized papillary muscle. These results suggest that ONO-1101 is a potent beta-antagonist whose effects were removed quickly by washout. When applied at what is thought to be a clinical dosage, ONO-1101 had no direct effects on action potential-parameters and membrane currents in cardiac muscle. These characteristics of ONO-1101 suggest that this agent may be effective in clinical use.