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At least 55 records · Page 3Linked to original sources
PubMed2003

Localization of [3H]nicotine, [3H]cytisine, [3H]epibatidine, and [125I]alpha-bungarotoxin binding sites in the brain of Macaca mulatta.

We determined the localization of [(3)H]nicotine, [(3)H]cytisine, [(3)H]epibatidine, and [(125)I]alpha-bungarotoxin binding sites in the brain of rhesus monkey by means of receptor autoradiography. The labelings by [(3)H]nicotine, [(3)H]cytisine, and [(3)H]epibatidine were highly concordant, except for epibatidine. Layer IV of some cortical areas, most thalamic nuclei, and presubiculum displayed high levels of labeling for the three ligands. Moderate levels of binding were detected in the subiculum, the septum, and the mesencephalon. Low levels were present in layers I-II and VI of the cortex, the cornu Ammonis, the dentate gyrus, and the amygdala. In addition, the level of epibatidine labeling was very high in the epithalamic nuclei and the interpeduncular nucleus, whereas labeling by nicotine and cytisine was very weak in the same regions. The distribution of [(125)I]alpha-bungarotoxin binding differed from the binding of the three agonists. The labeling was dense in layer I of most cortical areas, dentate gyrus, stratum lacunosum-moleculare of CA1 field, several thalamic nuclei, and medial habenula. A moderate labeling was found in layers V and VI of the prefrontal and frontal cortices, layer IV of primary visual cortex, amygdala, septum, hypothalamus, and some mesencenphalic nuclei. A weak signal was also detected in subiculum, claustrum, stratum oriens, and stratum lucidum of cornu Ammonis and also in some mesencephalic nuclei. The distribution of nicotine, cytisine, and epibatidine bindings corresponds broadly to the patterns observed in rodents, with the marked exception of the epithalamus. However, in monkey, those distributions match the distribution of alpha2 messenger RNA, rather than that of alpha4 transcripts as it exists in rodent brains. The distribution of the binding sites for alpha-bungarotoxin is larger in the brain of rhesus monkeys than in rodent brain, suggesting a more important role of alpha7 receptors in primates.

Alkaloids↗
PubMed1989

Tonazocine mesylate in postoperative pain patients: a double-blind placebo controlled analgesic study.

One hundred-fifty post-operative adult patients with moderate to severe pain were enrolled into this analgesic efficacy study comparing single doses of tonazocine mesylate, a new mixed agonist-antagonist opioid analgesic, with morphine. The patients were randomly assigned to five treatment groups: tonazocine mesylate 2, 4, 8 mg; morphine sulfate 10 mg and a placebo group. The results showed mean total pain relief scores for tonazocine 4 mg were nearly identical with that of morphine sulfate 10 mg while 8 mg of tonazocine were superior to 10 mg of morphine. All the active medication groups were superior to the placebo group (P less than 0.02) for both pain intensity and pain relief. Relative potency determined by the dose response indicates that 3.2 mg of tonazocine is equivalent to 10 mg of morphine. Drowsiness was the main adverse reaction seen in all active treatment groups. Tonazocine mesylate appears to be a potent analgesic with promising clinical usefulness and warrants further study.

Adolescent↗
PubMed1993

Examples of evolution of microstructure in ceramics and composites.

In this article we describe a number of studies involving the direct observation of microstructural evolution. In general these investigations were carried out to establish the mechanistic paths involved. The materials studied range from fibers being evaluated for use in high-temperature ceramic composites to energetic materials used as propellants. In particular we discuss the room temperature imaging of materials difficult to image by conventional means and the use of the chamber atmosphere to influence microstructural evolution. Imaging of hydroxyapatite formed by chemical means is briefly described as an example of a difficult microstructure. Microstructural evolution during calcium aluminate cement hydration relies on the chamber atmosphere to control moisture loss from the hydrating specimens. In some instances microstructural evolution with heating occurred independently of the chamber atmosphere. Grain growth in PZT films formed by sol-gel processes depends strongly on temperature but does not appear to depend on the chamber atmosphere. This is also the case for the combustion of nitroamine propellants in that their combustion does not depend on access to an external source of oxygen. In other studies, the chamber atmosphere played an indirect role in determining microstructure. However, the mechanistic path driving microstructural evolution in copper-based inks used as conductive paths on electronic substrates is atmosphere dependent. These inks are formulated from copper powder, glass, and an organic binder, and the interaction of the binder with an oxidizing atmosphere allows it to be burned out before significant interaction occurs between the copper powder and the glass. Finally, the microstructural variations during the oxidation of structural composites at high temperature were used to allow assessments of their likely failure mechanisms.

Animals↗
PubMed2005

(1)H and (13)C NMR studies of asymmetrically substituted bis- and tris-Tröger's bases.

The (1)H and (13)C NMR spectra of two stereoisomeric bis-Tröger's bases and four stereoisomeric tris-Tröger's bases asymmetrically substituted on the external aromatic rings were recorded and the corresponding signals assigned. The relative configuration of the stereogenic units has been unequivocally determined on the basis of homoallylic couplings and NOE experiments.

Azocines↗
PubMed2003

Differential physiologic responses of alpha7 nicotinic acetylcholine receptors to beta-amyloid1-40 and beta-amyloid1-42.

The beta-amyloid peptides (Abeta), Abeta(1-40) and Abeta(1-42), have been implicated in Alzheimer's disease (AD) pathology. Although Abeta(1-42) is generally considered to be the pathological peptide in AD, both Abeta(1-40) and Abeta(1-42) have been used in a variety of experimental models without discrimination. Here we show that monomeric or oligomeric forms of the two Abeta peptides, when interact with the neuronal cation channel, alpha7 nicotinic acetylcholine receptors (alpha7nAChR), would result in distinct physiologic responses as measured by acetylcholine release and calcium influx experiments. While Abeta(1-42) effectively attenuated these alpha7nAChR-dependent physiology to an extent that was apparently irreversible, Abeta(1-40) showed a lower inhibitory activity that could be restored upon washings with physiologic buffers or treatment with alpha7nAChR antagonists. Our data suggest a clear pharmacological distinction between Abeta(1-40) and Abeta(1-42).

Acetylcholine↗