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At least 955 records · Page 53Linked to original sources
PubMed1989

Dual action of clonidine on insulin release: suppression, but stimulation when alpha 2-adrenoceptors are blocked.

As shown previously clonidine reduces glucose-stimulated insulin release and this effect is mediated by inhibitory postsynaptic alpha 2-adrenoceptors. The present experiments demonstrate that clonidine has the additional property to also stimulate insulin release. This became evident when the alpha 2-adrenoceptors of isolated islets were blocked by benextramine, and thus protected from being stimulated by clonidine. In the presence of benextramine, clonidine no longer reduced, but on the contrary enhanced, the release of insulin in response to glucose. In control experiments benextramine by itself failed to affect insulin release from isolated islets. These results show that the imidazoline derivative clonidine shares the property of other imidazoline compounds to enhance the insulin response to glucose. All of these agents may stimulate insulin by binding to "imidazoline-preferring" sites, that clearly differ from alpha-adrenoceptors.

Adrenergic alpha-Antagonists↗
PubMed1998

Hypotaurine disproportionation reaction: identification of products.

Hypotaurine, concentrated under reduced pressure in HCl solution, partially (30-40%) degrades into taurine (about 30%), 2-aminoethyl-2-aminoethanethiolsulfonate (about 10%) and ethanolamine. The degradation products were identified using LC/APCI-MS, NMR, amino acid analysis and various chromatographies. The identities were confirmed by comparing the HPLS, MS and NMR characteristics of authentic compounds. One of the degradation processes during concentration of HCl solution of hypotaurine is therefore a disproportionation reaction which can interfere with the experimental results, when studying hypotaurine in biological systems.

Chromatography, High Pressure Liquid↗
PubMed1990

Sulfate self-exchange and amino acid transport in calcium-loaded human erythrocytes.

To analyze the effects of Ca2(+)-mediated membrane protein changes on the membrane function, we have studied the SO4(2-) self-exchange and amino acid transport in human erythrocytes after loading them with Ca2+ with the help of ionophore A23187. The SO4(2-) self-exchange is inhibited by 20-30% by loading the erythrocytes with 25 microM to 0.5 mM Ca2+. The extent of this inhibition is almost doubled (50-60%) by increasing the Ca2+ loading concentration to 1.5 mM. This additional effect of 1.5 mM Ca2+ is not correlated with the Ca2(+)-induced ATP depletion or membrane protein degradation, but is caused by the transglutaminase-catalyzed membrane protein crosslinking. Like the SO4(2-) self-exchange, L-alanine and L-cysteine uptakes are also inhibited in Ca2(+)-loaded cells. However, no effect is observed on the L-lysine uptake under identical conditions. These results have been interpreted to suggest that the Ca2(+)-mediated effects on the SO4(2-) self-exchange and amino acid transport are caused perhaps by the Ca2(+)-induced structural rearrangement of the band 3 protein.

Adenosine Triphosphate↗
PubMed1994

An XRF study of trace elements accumulation in kidneys of tumor-bearing mice after treatment with cis-DDP with and without selenite and selenocistamine.

The effect of cis-DDP treatment with and without selenite and selenocistamine was studied on kidneys of tumor-bearing mice. The amounts of cis-DDP, selenite, and selenocistamine injected were chosen so as to be compatible with the treatment of humans. The animals were sacrificed at 7, 14, and 28 d after treatment. The kidneys were removed and subjected to trace element analysis by a novel X-ray fluorescence (XRF) method and for pathological assessment. The results show that following treatment with cis-DDP, K, Fe, Cu, and Zn reach a maximum level after 7 d; K, Fe, and Cu levels were significantly reduced by the addition of selenite. The level of Zn was reduced only in groups treated with selenite whereas that of K and Cu was reduced also in groups treated with selenocistamine with and without cis-DDP. The greatest increase in Pt and Se levels was reached 1 wk after injection with cis-DDP, with and without selenocompounds, and in the case of Pt was partly reduced by addition of selenite. Se returned to control values 2 wk after injection, although Pt was still high in all groups 2 and 4 wk after injection. The results corroborate the findings of our previous studies. The effect of selenocistamine in cis-DDP treated mice was partly insufficient. The pathological examination of the kidneys did not show any differences in the effect of various additives during the study.

Animals↗
PubMed1997

Neuropeptide Y as a stimulator of Na+ -dependent Ca2+ efflux from freshly isolated adult rat cardiomyocytes.

Several physiological stimuli cause a rise in intracellular Ca2+ concentration ([Ca2+]i) in cardiomyocytes. This increased [Ca2+]i must be restored to physiological resting level to ensure response to further stimuli. In the present study, we examined the effect of neuropeptide Y (NPY), which is secreted from certain adrenergic or nonadrenergic neurons, on Ca2+ efflux from freshly isolated, quiescent adult rat cardiomyocytes. The isolated cardiomyocytes were preloaded with 45CaCl2 for 1 h. Then, the fractional release of 45Ca2+ from the cells was measured. NPY stimulated the efflux of 45Ca2+ from isolated adult rat cardiomyocytes in a concentration-dependent manner (10(-8) M to 10(-6) M). NPY (10(-6) M)-induced Ca2+ efflux was 2.0 +/- 0.16% of the total cellular content. The 45Ca2+ efflux from the cells was also stimulated by Y1 receptor agonist, [Leu31, Pro34]NPY, but not by Y2 receptor agonist, NPY13-36. The effect of NPY was inhibited by a peptide NPY inhibitor, NPY18-36 and a non-peptide NPY inhibitor, benextramine to a similar extent. From these results, it is conceivable that the effect of NPY on Ca2+ efflux from cardiomyocytes is mediated through Y1 receptors. It was also observed that NPY caused a rise in [Ca2+]i to almost 150 nM. NPY-stimulated 45Ca2+ efflux was not affected by removal of extracellular Ca2+, but was dependent on the presence of extracellular Na+. Moreover, NPY caused a 22Na+ influx into the cells of about 1.6-fold over the basal value which was inhibited by amiloride and 5-(N,N-dimethyl)-amiloride, known Na+/Ca2+ exchange inhibitors. In addition, isoproterenol also caused 45Ca2+ efflux from the cells and which was enhanced by the addition of NPY. These results suggest that NPY stimulates extracellular Na+-dependent 45Ca2+ efflux from freshly isolated adult rat cardiomyocytes, probably through its stimulatory effect on plasma membrane Y1 receptors with which NPY may couple during Na+/Ca2+ exchange.

Adenosine Triphosphatases↗
PubMed2004

Separation of organoselenium compounds and their electrochemical detection.

A simplified procedure based on ion-exchange separation of selenourea (Se-U) and selenocystamine (Se-CM), which have very close half-wave potential when they are simultaneously analyzed by voltammetric techniques, has been developed and optimized. Thus, selenocystamine remains in the cation exchanger Purolite C 100 H, whereas selenourea is found in the effluent and is determined by square wave cathodic stripping voltammetry using Na(2)CO(3 )as electrolyte. Selenocystamine is then eluted from the cation exchanger using 4 M HCl and analyzed by square wave cathodic stripping voltammetry in the HCl solution. For each voltammetric determination the corresponding parameters were investigated and optimized; the obtained detection limits were 0.3 ng Se mL(-1) for Se-CM and 2 ng Se mL(-1) for Se-U. A flow sheet for the separation of inorganic (Se(IV) and Se(VI)) and organoselenium compounds (Se-U, Se-CM, (CH(3))(2)Se(2), and (CH(3))(2)Se) developed for their electrochemical detection is presented and it was successfully applied to a certified reference material, an environmental soil sample, and a urine sample.

Adult↗
PubMed2006

Hyperhomocysteinemia and low plasma folate as risk factors for central retinal vein occlusion: a case-control study in a Chinese population.

PURPOSE: To determine whether hyperhomocysteinemia and low plasma folate are risk factors for central retinal vein occlusion (CRVO) in the Chinese population. METHODS: A matched case-control study was conducted between July 2004 and May 2005. The study cohort consisted of 64 individuals that had been diagnosed to have CRVO and 64 normal controls (matched for age, gender, hypertension, smoking and drinking habits). None of the cases or controls had a history of diabetes, glaucoma, medication or any other vascular events that might minimize the influence on plasma homocysteine levels. A cross-sectional analysis among the 64 cases was performed to compare the prevalence of hyperhomocysteinemia and low plasma folate among subjects with and without ischemia and subjects with age above 45 and below 45 years. Plasma homocysteine level was measured by means of high-performance liquid chromatography and plasma folate concentration by radioimmunoassay. RESULTS: The CRVO patients had a significantly higher homocysteine level (13.83+/-1.71 micromol/l) than the normal controls (8.05+/-0.58 micromol/l; p=0.003). The plasma folate levels were significantly lower in CRVO patients than in controls (5.62+/-0.39 ng/dl vs 7.23+/-0.60 ng/dl; p=0.032). A 1 micromol/l increase of plasma homocysteine level was associated with an odds ratio of 1.368. Hyperhomocysteinemia was defined as a homocysteine level of >14.97 micromol/l and was seen in 11 patients in the ischemic group, significantly more often than in the non-ischemic group (5 patients; p=0.030). CONCLUSIONS: The results suggest that hyperhomocysteinemia and low plasma folate are independent risk factors for CRVO and are associated with the development of CRVO in the Chinese population.

Adult↗
PubMed1992

Glutathione oxidase activity of selenocystamine: a mechanistic study.

Selenocystamine (RSe-SeR) was shown to catalyze the oxygen-mediated oxidation of excess GSH to glutathione disulfide, at neutral pH and ambient PO2. This glutathione oxidase activity required the heterolytic reduction of the diselenide bond, which produced two equivalents of the selenolate derivative selenocysteamine (RSe-), via the transient formation of a selenenylsulfide intermediate (RSe-SG). Formation of RSe- was the only reaction observed in anaerobic conditions. At ambient PO2, the kinetics and stoichiometry of GSSG production as well as that of GSH and oxygen consumptions demonstrated that RSe- performed a three-step reduction of oxygen to water. The first step was a one-electron transfer from RSe- to dioxygen, yielding superoxide and a putative selenyl radical RSe., which decayed very rapidly to RSe-SeR. In the second step, RSe- reduced superoxide to hydrogen peroxide through a much faster one-electron transfer, also associated with the decay of RSe. to RSe-SeR. The third step was a two-electron transfer from RSe- to hydrogen peroxide, again much faster than oxygen reduction, which resulted in the production of RSe-SG, presumably via a selenenic acid intermediate (RSeOH) which was trapped by excess GSH. This third step was studied on exogenous hydroperoxide in anaerobic conditions, and it could be eliminated from the glutathione oxidase cycle in the presence of excess catalase. The role of RSe- as a one- and two-electron reductant was confirmed by competitive carboxymethylation with iodoacetate. RSe- was able to rapidly reduce ferric cytochrome c to its ferrous derivative. The overall rate of catalytic glutathione oxidation was GSH concentration dependent and oxygen concentration independent. Excess glutathione reductase and NADPH increased the catalytic oxidation of GSH, probably by switching the rate-limiting step from selenylsulfide to diselenide cleavage. When GSH was substituted for dithiothreitol, it was shown to reduce RSe-SeR to RSe- in a fast and quantitative reaction, and selenocystamine behaved as a dithiothreitol oxidase, whose catalytic cycle was dependent on oxygen concentration. The oxidase cycle of glutathione was inhibited by mercaptosuccinate, while that of dithiothreitol was not affected. When mercaptosuccinate was substituted for GSH, a stable selenenylsulfide was formed. These observations suggest that electrostatic interactions affect the reductive cleavage of diselenide and selenenylsulfide linkages. This study illustrates the ease of one-electron transfers from RSe- to a variety of reducible substrates. Such free radical mechanisms may explain much of the cytotoxicity of alkylselenols, and they demonstrate that selenocystamine is a poor catalytic model of the enzyme glutathione peroxidase.

Cystamine↗