26 research outputs found
Electromagnetic Probes
A review is presented of dilepton and real photon measurements in
relativistic heavy ion collisions over a very broad energy range from the low
energies of the BEVALAC up to the highest energies available at RHIC. The
dileptons cover the invariant mass range \mll = 0 - 2.5 GeV/c, i.e. the
continuum at low and intermediate masses and the light vector mesons, . The review includes also measurements of the light vector mesons
in elementary reactions.Comment: To be published in Landolt-Boernstein Volume 1-23A; 40 pages, 24
figures. Final version updated with small changes to the text, updated
references and updated figure
Coupling between Electronic and Vibrational Excitations in Carbon Nanotubes Filled with C(60) Fullerenes
Antibacterial Activity of an Atmospheric Pressure Plasma Jet Against Relevant Wound Pathogens in vitro on a Simulated Wound Environment
Interaction between G proteins and accessory β subunits in the regulation of α1B calcium channels in Xenopus oocytes
The accessory β subunits of voltage-dependent Ca2+ channels (VDCCs) have been shown to regulate their biophysical properties and have also been suggested to antagonise the G protein inhibition of N-type (α1B), P/Q-type (α1A) and α1E channels. Here we have examined the voltage-dependent involvement of the four neuronal isoforms (β1b, β2a, β3 and β4) in the process of G protein modulation of α1B Ca2+ channels.All β subunits hyperpolarised α1B current activation, and all antagonised the G protein-mediated depolarisation of current activation. However, except in the case of β2a, there was no generalised reduction by β subunits in the maximal extent of receptor-mediated inhibition of α1B current.In addition, all VDCC β subunits enhanced the rate of current facilitation at +100 mV, for both receptor-mediated and tonic modulation. The rank order for enhancement of facilitation rate was β3 > β4 > β1b > β2a. In contrast, the amount of voltage-dependent facilitation during tonic modulation was reduced by β subunit co-expression, despite the fact that the apparent Gβγ dissociation rate at +100 mV was enhanced by β subunits to a similar level as for agonist-induced modulation.Our data provide evidence that G protein activation antagonises Ca2+-channel β subunit-induced hyperpolarisation of current activation. Conversely, co-expression of all β subunits increases the apparent Gβγ dimer dissociation rate during a depolarising prepulse. This latter feature suggests the co-existence of bound Ca2+-channel β subunits and Gβγ dimers on the α1B subunits. Future work will determine how the interaction between Gβγ dimers and Ca2+-channel β subunits with α1B results in a functional antagonism at the molecular level