Drugs online research references
J Neuroimmunol. 1992 Mar;37(1-2):149-60.
Serotonergic aspects of the response of human platelets to immune-adjuvant muramyl dipeptide.
Polanski M, Karnovsky ML.
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
The human platelet serotonergic responses of aggregation and uptake were shown to be modulated by muramyl peptides. Muramyl dipeptide inhibited serotonin uptake in a temperature dependent and stereospecific manner. It also blocked the binding to platelets of [3H]imipramine, a well-known inhibitor of serotonin uptake. Muramyl dipeptide decreased serotonin2 (5-HT2) mediated platelet aggregation, and blocked the binding of a 5-HT2-specific ligand: lysergic acid diethylamide. Since muramyl peptides are released upon degradation of bacteria, the findings offer a possible mechanism for neuro-immune modulation by emphasizing the interaction between 5-HT (a neurotransmitter) and muramyl peptides (immuno-adjuvants).
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1532180&dopt=Abstract
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Pharmacol Biochem Behav. 1992 Apr;41(4):801-5.
Effects of the 5-HT uptake inhibitors, femoxetine and paroxetine, and a 5-HT1A/B agonist, eltoprazine, on the behavioural satiety sequence.
McGuirk J, Muscat R, Willner P.
Psychology Department, City of London Polytechnic, UK.
In rats allowed access to a 35% sucrose solution, following a 4-h period of food and water deprivation, an initial period of sucrose consumption was followed by a short period of grooming and exploratory behaviour, later superseded by resting. This "behavioural satiety sequence" was advanced in time by the 5-HT uptake inhibitors femoxetine and paroxetine and by the 5-HT1A/B agonist eltoprazine at anorectic and subanorectic doses. These effects, which are similar to those previously observed with another 5-HT uptake inhibitor, fluoxetine, are compatible with an increase in postprandial satiety.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1534413&dopt=Abstract
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J Biol Chem. 1992 Jun 5;267(16):11344-51.
One-step purification of the serotonin transporter located at the human platelet plasma membrane.
Launay JM, Geoffroy C, Mutel V, Buckle M, Cesura A, Alouf JE, Da Prada M.
Claude Bernard Neurochimie des Communications Cellulaires, Hopital Saint-Louis, Paris, France.
A 68-kDa glycoprotein bearing the biological activity of the plasma membrane serotonin (5-hydroxytryptamine, 5-HT) transporter has been purified from human blood platelets, a classical cell model for the study of 5-HT uptake. After treatment of the whole platelet population or its plasma membrane fraction by sulfhydryl-dependent bacterial protein toxins or by digitonin, purification was reproducibly obtained by a one-step affinity chromatography using two different columns with 5-HT or 6-fluorotryptamine as ligands and elution by 5-HT or Na(+)-free buffer. The purified fraction migrated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a single band with an apparent molecular mass of 68 kDa and exhibited an apparent isoelectric point of 5.6-6.2. Two sialic acid residues were detected in the purified material. The purified glycoprotein bound the 5-HT uptake blocker [3H]paroxetine with a Kd (0.25 nM) similar to the one observed for intact human platelets. It also bound [3H] 5-HT but neither [3H]hydroxytetrabenazine nor [3H] ouabain, the respective markers of the granular monoamine transporter and of the Na+,K(+)-ATPase associated to the plasma membrane 5-HT transporter. 5-HT derivatives and 5-HT uptake inhibitors exhibited similar Ki values for 5-HT uptake and paroxetine binding in intact human platelets and in the purified glycoprotein. Under laser UV irradiation, 40% of this purified glycoprotein could be labeled by either [3H]paroxetine or [3H]cyanoimipramine. No labeling was detected with either [3H] gamma-aminobutyric acid or [3H]GBR 12783, the respective markers of gamma-aminobutyric acid and dopamine carriers. The purified 68-kDa protein is therefore likely to correspond at least to the binding domain of the 5-HT transporter located at the human platelet plasma membrane.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1534559&dopt=Abstract
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