Library

Notes: In this paper we report the results of experiments that compare the x-ray emission from a laser spot in a radiation-filled hohlraum to that from a similar laser spot on a simple disk target. The studies were done using the Nova laser facility [J. D. Lindl, Phys. Plasmas 2, 3933 (1995)] in its 0.35 μm wavelength, 1 ns square pulse configuration. Focal spot intensities were 2–3.5×1015 W/cm2. X-ray images measured x-ray conversion in a hohlraum and from an isolated disk simultaneously. A laser spot inside a hohlraum emitted more x rays, after subtracting the background emission from the hohlraum walls, than a spot on a disk. Numerical models suggest the enhanced spot emission inside the hohlraum is due to an increase in lateral transport relative to the disk. Filamentation in the hohlraum will also increase the spot size. The models agree fairly well with the results on spot spreading but do not explain the overall increase in conversion efficiency. © 1997 American Institute of Physics.

Notes: Of primary concern in next generation inertial confinement fusion (ICF) implosion experiments is Rayleigh–Taylor (RT) instability of the pusher-fuel interface occurring upon acceleration and deceleration of the pusher. This results in mixing of hot fuel with cold pusher material. One method of diagnosing mix in this case is to place spectroscopic dopants both in the capsule fuel region and the innermost region of the capsule wall adjacent to the fuel. As the degree of pusher/fuel mix is increased (typically through placement of controlled perturbations on the outer surface of the capsule) the pusher dopant x-ray emission increases relative to that of the fuel dopant. Experiments of this type using indirectly driven implosions have been carried out on Nova. In this paper we describe some of the important physics issues underlying spectral line formation in these targets and discuss how they are manifested in the modeling and interpretation of experimental data. The importance of radiative transfer as well as high density plasma phenomena such as continuum lowering and Stark broadening is demonstrated. We provide an overview of recent Nova hydrodynamic instability experiments and discuss how the level of instability growth implicit in a given capsule design impacts the diagnosis of mix through x-ray spectroscopy. © 1995 American Institute of Physics.

Notes: Abstract: In the rat brain, the presynaptic 5-hydroxytrypt-amine (5-HT) autoreceptors located on 5-HT terminals correspond to the 5-HT1B subtype. The presence of a 5-HT receptor probably located on 5-HT nerve endings and modulating transmitter release in the human neocortex has been reported, but its detailed pharmacological characterization is not yet available. On the other hand, receptor binding and autoradiographic results indicate that the 5-HT1B receptor subtype is not present in the human brain. We, therefore, studied the modulation of the electrically evoked release of [3H]5-HT by various 5-HT receptor agonists and antagonists in preloaded slices of human neocortex obtained from 18 patients undergoing neurosurgery. The nonselective 5-HT1A/1B/1D receptor agonist 5-carboxamidotryptamine produced a potent inhibition (70% at 0.03 μM) of the electrically evoked release of [3H]5-HT which was blocked by 5-HT receptor antagonists with the following relative order of potency: methiothepin 〉 metergoline = methysergide 〉 propranolol. The selective 5-HT1A receptor agonist 8-hydroxy-2–(di-n-propylamino)tetralin at 0.1 μM did not modify the electrically evoked release of [3H]5-HT. The 5-MT1A/1B receptor agonist RU 24969 was 10 times more potent at inhibiting [3H]5-HT overflow in the rat frontal cortex than in the human neocortex. The potent 5-HT1B receptor antagonist cyanopindolol did not modify the 5-carboxamidotryptamine-induced inhibition of the electrically evoked release of [3H]5-HT in slices of the human neocortex, but produced by itself a small inhibition of [3H]5-HT overflow. The α2-adrenoceptor antagonist yohimbine, which possesses affinity for the 5-HT1D receptor subtype, decreased the release of [3H]5-HT, but only in the presence of the selective α2-adrenoceptor antagonist idazoxan, which by itself increased significantly [3H]5-HT overflow. Taken together, these results support the view that the 5-HT receptor modulating the electrically evoked release of [3H]5-HT in slices of the human neocortex could be of the 5-HT1D subtype. Moreover, preliminary results obtained with idazoxan confirm the existence of a presynaptic α2-adrenoceptor modulating the release of [3H]5-HT in the human neocortex. These α2-heteroreceptors could exert a tonic inhibitory modulation on 5-HT neurotransmission in the human neocortex.

Notes: Abstract: The regional distribution of [3H]zoIpidem, a novel imidazopyridine hypnotic possessing preferential affinity for the BZD1 (benzodiazepine subtype 1) receptor, has been studied autoradiographically in the rat CNS and compared with that of [3H]flunitrazepam. The binding of [3H]zolpidem to rat brain sections was saturable, specific, reversible, and of high affinity (KD= 6.4 nM). It occurred at a single population of sites whose pharmacological characteristics were similar to those of the benzodiazepine receptors labeled with [3H]flunitrazepam. However, ethyl-β-carboline-3-carboxylate and CL 218,872 were more potent displacers of [3H]zolpidem than of [3H]flunitrazepam. The autoradiographic brain distribution of [3H]zolpidem binding sites was qualitatively similar to that previously reported for benzodiazepine receptors. The highest levels of [3H]- zolpidem binding sites occurred in the olfactory bulb (glomerular layer), inferior colliculus, ventral pallidum, nucleus of the diagonal band of Broca, cerebral cortex (layer IV), medial septum, islands of Calleja, subthalamic nucleus, and substantia nigra pars reticulata, whereas the lowest densities were found in parts of the thalamus, pons, and medulla. Comparative quantitative autoradiographic analysis of the binding of [3H]zolpidem and [3H]flunitrazepam [a mixed BZD1/BZD2 (benzodiazepine subtype 2) receptor agonist] in the CNS revealed that the relative density of both 3H- labeled ligands differed in several brain areas. Similar levels of binding for both ligands were found in brain regions enriched in BZD1 receptors, e.g., substantia nigra pars reticulata, inferior colliculus, cerebellum, and cerebral cortex lamina IV. The levels of [3H]zolpidem binding were five times lower than those of [3H]flunitrazepam binding in those brain regions enriched in BZD2 receptors, e.g., nucleus accumbens, dentate gyrus, and striatum. Moreover. [3H]zolpidem binding was undetectable in the spinal cord (which contains predominantly BZD2 receptors). Finally, like CL 218,872 and ethyl-β-carboline-3-carboxylate, zolpidem was a more potent displacer of [3H]flunitrazepam binding in brain regions enriched in BZD1 receptors than in brain areas enriched in BZD2 receptors. The present data add further support to the view that zolpidem, although structurally unrelated to the benzodiazepines, binds to the benzodiazepine receptor and possesses selectivity for the BZD1 receptor subtype.

Notes: Abstract: Tricyclic antidepressants and nontricyclic serotonin (5-hydroxytryptamine) uptake blockers monophasically inhibit [3H]imipramine binding in human platelets. Similarly, serotonin and tryptamine inhibit the binding of [3H]imipramine in the low micromolar range and with a pseudo-Hill coefficient near unity. Dissociation of the [3H]imipramine receptor complex in the presence of uptake inhibitors follows first-order kinetics with a half-life of approximately 60 min. Although serotonin and tryptamine do not decrease [3H]imipramine binding when added under equilibrium conditions, simultaneous addition of serotonin or tryptamine with serotonin uptake inhibitors decreases the rate of ligand-receptor dissociation in a concentration-dependent manner. These data suggest a common site of action for serotonin, which is the substrate of the transporter system, and of tryptamine, its nonhydroxylated analog. This hypothesis is supported by the identification of a high-affinity (Km= 0.55 μM), saturable, and temperature-dependent uptake of [3H]tryptamine in human platelets. Uptake of [3H]tryptamine was inhibited potently by imipramine and nontricyclic serotonin uptake inhibitors with a potency similar to that observed for [3H]serotonin uptake. These data support the hypothesis that in platelets, [3H]imipramine, tricyclic, and nontricyclic serotonin up-take inhibitors bind to a common recognition site that is associated with the serotonin transporter but that differs from the substrate recognition site of the carrier through which serotonin and tryptamine exert a heterotropic allosteric modulation on [3H]imipramine binding.

Notes: Abstract: The activation by endogenous dopamine of the inhibitory 3,4-dihydroxyphenylethylamine (dopamine) receptors modulating the electrically evoked release of [3H]acetylcholine ([3H]ACh) and [3H]dopamine in rat striatal slices is a function of the concentration of dopamine accumulated in the synaptic cleft during electrical stimulation. When the release of 3H-neurotransmitters was elicited with a 2-min period of stimulation at a frequency of 1 Hz, neither dopamine autoreceptors nor dopamine receptors modulating [3H]ACh were activated by endogenously released dopamine. On the other hand, exposure to (S)-sulpiride facilitated the release of [3H]dopamine and [3H]ACh elicited when the 2-min stimulation was carried out at a frequency of 3 Hz but this effect was not observed at a lower frequency of stimulation (1 Hz). In the presence of amphetamine the dopamine receptors modulating the electrically evoked release of [3H]ACh can be activated by endogenous dopamine even at the lower frequency of stimulation (1 Hz). Similar effects can be obtained if the neuronal uptake of dopamine is inhibited by cocaine or nomifensine. The inhibition by amphetamine of the release of [3H]ACh elicited by electrical stimulation at 1 Hz involves dopamine receptors and can be fully antagonized by clozapine, haloperidol, chlorpromazine, or pimozide. The stereoselectivity of this antagonism can be demonstrated with the optical enantiomers of sulpiride and butaclamol. This inhibitory effect of amphetamine on cholinergic neurotransmission appears to be the result of the stimulation of dopamine receptors of the D2 subtype, as they were resistant to blockade by the preferential D1 receptor antagonist SCH 23390. Inhibition of dopamine synthesis with α-methyl-p-tyrosine antagonized the effects of amphetamine on [3H]ACh release. The dopamine receptor-mediated inhibition of the release of [3H]ACh elicited at low frequencies of stimulation from rat striatal slices is a suitable model to test drugs that enhance dopaminergic neurotransmission. In addition, the antagonism of the inhibition of cholinergic neurotransmission by amphetamine in striatal slices represents a useful test for drugs with potential usefulness in clinical situations in which dopaminergic neurotransmission is exacerbated.

Notes: Abstract: [3H]Imipramine binds with high affinity to membranes from different regions of the human brain. The highest density of binding sites was observed in the hypothalamus and substantia nigra and the lowest density in the white matter and cerebellum. As found in rat brain, tricyclic antidepressant drugs are potent inhibitors of [3H]imipramine binding. Atypical antidepressants are, however, much weaker at inhibiting the specific binding. The [3H]imipramine binding site in human cortex is apparently identical to the site already described in the rat brain and in human platelets.

Notes: Abstract: High-affinity specific [3H]imipramine binding has been demonstrated in the brain and platelets of various species including man. Electrolytic lesion of the rat dorsal raphe, which resulted in a significant decrease in the endogenous levels of serotonin produced a reduction in the density of [3H]imipramine binding sites in the hypothalamus and cortex. The affinity constants were unchanged. These results suggest that [3H]imipramine binding sites are located on serotonin nerve terminals.