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At least 127 records · Page 7Linked to original sources
PubMed1990

Mapping the alpha-subunit site photolabeled by the noncompetitive inhibitor [3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor.

We have characterized the time-resolved labeling of a site on the Torpedo californica electrocyte acetylcholine receptor (ACHR) by the photoreactive noncompetitive inhibitor derivative quinacrine azide (QA). The dependence of [3H]QA labeling on acetylcholine (ACH) concentration and on time is consistent with the preferential labeling by [3H]QA of ACHR in the open state. The ACH-dependent [3H]QA labeling, which was associated predominantly with the alpha-subunit, was blocked by other noncompetitive inhibitors including quinacrine, chlorpromazine, proadifen, histrionicotoxin, and bupivacaine. alpha-Subunit from ACHR labeled with [3H]QA 20 ms after the addition of ACH was cleaved with CNBr, and the fragments were separated by high pressure liquid chromatography. A peptide containing a major site of specific labeling was purified on two different reverse-phase columns. By N-terminal sequencing, amino acid composition, binding to mercurial-agarose, and apparent molecular weight, this [3H]QA-labeled peptide was identified as alpha-208-243, a CNBr fragment containing the putative membrane-spanning helix M1.

Acetylcholine↗
PubMed1989

[The development of desensitization during rhythmic activity of the synapse and in the course of generating a single signal].

The possibility of desensitization (DS) development under the rhythmic activity and during the generation of the single response to acetylcholine was studied in the frog sartorius muscle by voltage-clamp technique. It was revealed, that under conditions promoting DS (hyperpolarization, muscle warming, rise of calcium concentration as well as treatment by the DS--potentiating agent--proadifen) decrease of the postsynaptic membrane sensitivity to the acetylcholine can develop after few multiquantal end-plate currents--and when acetylcholinesterase is inhibited--during the response to a single quantum of acetylcholine.

Animals↗
PubMed1986

Reaction of [3H]meproadifen mustard with membrane-bound Torpedo acetylcholine receptor.

The Torpedo nicotinic acetylcholine receptor (AChR) contains a binding site for aromatic amine noncompetitive antagonists that is distinct from the binding site for agonists and competitive antagonists. To characterize the location and function of this allosteric antagonist site, an alkylating analog of meproadifen has been synthesized, 2-(chloroethylmethylamino)-ethyl-2, 2-diphenylpentanoate HCl (meproadifen mustard). Reaction of [3H]meproadifen mustard with AChR-rich membrane suspensions resulted in specific incorporation of label predominantly into the AChR alpha-subunit with minor incorporation into the beta-subunit. Specific labeling required the presence of high concentration of agonist and was inhibited by reversible noncompetitive antagonists including proadifen, meproadifen, perhydrohistrionicotoxin (HTX), and tetracaine when present at concentrations consistent with the binding affinity of these compounds for the allosteric antagonist site. No specific alkylation of the AChR alpha-subunit was detected in the absence of agonist, or in the presence of the partial agonist phenyltrimethylammonium or the competitive antagonists, d-tubocurarine, gallamine triethiodide, or decamethonium. Reaction with 35 microM meproadifen mustard for 70 min in the presence of carbamylcholine produced no alteration in the concentration of [3H]ACh-binding sites, but decreased by 38 +/- 4% the number of allosteric antagonist sites as measured by [3H]HTX binding. This decrease was not observed when the alkylation reaction was blocked by the presence of HTX. These results lead us to conclude that meproadifen mustard alkylates the allosteric antagonist site in the Torpedo AChR and that part of that site is associated with the AChR alpha-subunit.

Acetylcholine↗
PubMed1982

[Effect of talinolol on the activity of the mixed-function oxidases of rat liver].

Experiments with male rats were performed to compare the in vitro and in vivo effects of talinolol with those of propranolol, alprenolol, practolol, proadifen (SKF 525-A) and barbital. Three in vitro model reactions (amino-phenazone N-demethylation, p-nitroanisol O-demethylation and aniline hydroxylation) as well as the hexobarbital lateral-position time served as parameters. The results obtained show that talinolol, like the other beta-receptor blockers, can inhibit polyfunctional oxidases. There were no indications of an inductive action.

Adrenergic beta-Antagonists↗
PubMed1983

Reaction of quinacrine mustard with the acetylcholine receptor from Torpedo californica.

Amines with local anesthetic activity are typically also noncompetitive inhibitors of the agonist-induced increase in cation permeability mediated by the nicotinic acetylcholine receptor. Quinacrine is such an agent, and we have synthesized tritiated quinacrine mustard, a derivative capable of reacting with nucleophiles. Quinacrine mustard was reacted with receptor-rich membrane from torpedo electric tissue, excess reagent was removed by partition into liposomes, and the modified receptor was extracted and reconstituted with exogenous phospholipid. After reaction of the native membrane with 10 microM quinacrine mustard for 5 min, binding of cobratoxin to the acetylcholine binding sites is inhibited 15%; in contrast, receptor-mediated 86Rb uptake in the reconstituted vesicles is inhibited 70%. When the reaction with quinacrine mustard is carried out in the presence of 10 microM carbamylcholine or 10 microM d-tubocurarine, there is no block of the acetylcholine binding sites; nevertheless, the inhibition of Rb uptake is greater than that resulting from reaction in the absence of acetylcholine binding site ligands. Conversely, when the reaction is carried out in the presence of either 100 microM quinacrine or 100 microM proadifen (also a potent noncompetitive inhibitor), either with or without carbamylcholine or d-tubocurarine, the inhibition of 86Rb uptake is about 70% smaller. Under the same conditions that we used in the functional studies, quinacrine mustard reacts with the four types of chains that constitute the receptor complex, alpha 2 beta gamma delta. The presence of the acetylcholine binding site ligands, however, results in increased reaction with the alpha and beta chains, while the presence of the noncompetitive inhibitors, with or without the acetylcholine binding site ligands, results in decreased reaction with the alpha and beta chains. We conclude that the alpha and beta chains contribute to one or more functionally significant binding sites for noncompetitively inhibiting amines.

Animals↗
PubMedDate not supplied

Preliminary study of the biotransformation of two new drugs, trazodone and etoperidone.

M-Chlorophenylpiperazine (CPP) is formed in the course of biotransformation of trazodone and etoperidone. The biotransformation of the latter compound is more rapid. An enzymatic inhibitor, proadifen (SKF 525A), inhibited the formation of CPP, while an enzymatic inductor, phenobarbital, did not affect it. The elimination rate of CPP was much lower than that of trazodone; its t0.5 was approx. 50-60 min. The pharmacokinetic data may explain well the pharmacological properties of trazodone and etoperidone.

Animals↗
PubMed1993

The effect of non-quantal acetylcholine release on quantal miniature currents at mouse diaphragm.

1. The amplitude and exponential decay time constant of miniature endplate currents (MEPCs) were measured in mouse diaphragms treated with anti-cholinesterase under conditions known to modulate non-quantal acetylcholine (ACh) release. 2. Anti-cholinesterase prolonged MEPC decay and the extent of this initial prolongation was not influenced by non-quantal release. When non-quantal release was present, the decays of MEPCs became increasingly faster over several hours. This increased decay did not occur in the absence of non-quantal release. 3. Potentiation of the non-quantal release by zero Mg2+ and 1 x 10(-5) M choline, on the other hand, led to acceleration of MEPC shortening. 4. Increase of temperature from 15 to 26 degrees C and the presence of the desensitization-promoting drug proadifen (5 x 10(-6) M) accelerated the rate of MEPC shortening. 5. These observations are consistent with increased receptor desensitization due to non-quantal release. Repetitive binding of ACh to postsynaptic receptors which prolongs the time course of MEPC in anti-cholinesterase-treated endplates leads to progressive desensitization in the presence of non-quantal release and to the subsequent shortening of the quantal responses.

Acetylcholine↗
PubMed1996

Effects of feeding Artemisia filifolia and Helenium flexuosum on rabbit cytochrome P450 isozymes.

Six groups of 4 rabbits each were treated as follows: Control; phenobarbital (PB); 3-methylcholanthrene (3MC); proadifen hydrochloride (SKF-525A); Artemisia filifolia and Helenium flexuosum. Prototype P450 inducers (PB and 3MC) increased basal hepatic cytochrome P450 content by 2-3 fold whereas the P450 inhibitor (SKF-525A) had no effect on basal cytochrome P450 content. PB-induction of hepatic microsomes significantly increased the rate of dealkylation of long alkyl chain alkoxyresorufin ethers, benzyloxyresorufin and pentoxyresorufin 47-fold and 17-fold, respectively, but had little or no effect on short alkyl chains. 3MC-induction of microsomes increased dealkylation of all alkoxyresorufin ethers tested, preferentially dealkylating ethers with short alkyl chain in the order: methoxy > ethoxy > propoxy. Artemisia filifolia or Helenium flexuosum had no effect on basal hepatic cytochrome P450 content. However, microsomal dealkylation activity of short alkyl chain alkoxyresorufin ethers (methoxy, ethoxy and propoxy) was inhibited approximately 50%. When these plants are eaten for several days, they may inhibit biotransformation processes in herbivores through the same isoenzymes induced by 3MC.

Animal Feed↗
PubMedDate not supplied

Locomotor activity and motor disturbances induced by the competitive NMDA receptor antagonist CGP 37849.

The study compares the effects of the competitive NMDA receptor antagonist, CGP 37849, on the locomotor activity and motor disturbances after local, unilateral microinjection into nucleus accumbens and caudateputamen or peripheral ip administration. Independently on the route of administration, the compound induced dose-dependent increase in the locomotor activity as well as the symptoms of motor disturbances. In all cases the symptoms of motor disturbances appeared earlier and lasted longer than increase in locomotor activity induced by the same dose of the drug. The long-lasting observation indicated, that CGP 37849 administered in a dose of 20 mg/kg ip increased the locomotor activity of the rats for about 2 h while motor disturbances persisted for about 6 h. Administration of the lowest dose of CGP 37849, i.e. 0.05 microgram into the nucleus accumbens, or 10 mg/kg ip-while without any effect on the locomotor activity-induced the symptoms of motor disturbances. Pretreatment with SKF-525-A (proadifen, an agent inhibiting the metabolism of the drugs), fully antagonized the locomotor hyperactivity induced by CGP 37849 given in a dose of 20 mg/kg, and-in the same time-diminished the degree of motor disturbance symptoms. On the other hand, in the case of the dose of 10 mg/kg of CGP 37849, SKF-525-A did not affect the locomotor activity, but enhanced the motor disturbance symptoms induced by this dose of CGP 37849. In conclusion, the obtained results indicate that CGP 37849 administered peripherally or locally to the brain regions cited above induces motor disturbances at doses lower (or at least similar) than these which stimulate the locomotor activity.

2-Amino-5-phosphonovalerate↗
PubMedDate not supplied

GC-FID determination of cocaine and its metabolites in human bile and vitreous humor.

Gas chromatography was used in combination with flame ionization detection (GC-FID) to develop a method for determining cocaine and its two metabolites, benzoylecgonine (BEG) and ecgonine methyl ester (EME), in bile and vitreous humor. The method used a 12 m x 0.2 mm i.d. column of 0.33 microm film thickness packed with 5% phenylmethylsiloxane, and proadifen as a reference compound. Drug-free bile and vitreous humor samples were used to prepare solutions of the target compounds at concentrations over the range 0.1-4 microg ml(-1) that were subjected to solid-phase extraction through Bond Elut Certify columns and derivatized with 99:1 (v/v) N,O-bis-trimethylsilyltrifluoroacetamide (BSTFA)/trimethylchlorosilane (TMCS). Calibration graphs were highly linear, with correlation coefficients above 0.99 in all instances. Also, the precision of the method was found to be quite acceptable, with coefficients of variation less than 5% for bile and less than 7% for vitreous humor. The average extraction yields ranged from 73.6% to 91.2% for bile and from 71.5% to 92.2% for vitreous humor. The proposed method was used to analyse 26 samples of bile and as many of vitreous humor from individuals fatally poisoned by cocaine, whether alone or in combination with other drugs. The mean drug levels found were 0.75 and 1.54 microg ml(-1) for cocaine in bile and vitreous humor, respectively, 6.35 and 0.94 microg ml(-1) for BEG, and 2.18 and 0.61 microg ml(-1) for EME.

Aqueous Humor↗
PubMedDate not supplied

Gas chromatographic determination of cocaine and its metabolites in blood and urine from cocaine users in northwestern Spain.

A gas chromatographic method with fl ame ionization detection (GC/FID) was developed for the determination of cocaine and its metabolites in blood and urine samples from cocaine users in Northwestern Spain. After a solid-phase extraction with Bond Elut Certify cartridges and a derivatization with bis-trimethylsilyltrifluoroacetamide-trimethylchlorosilane (1%), calibration curves were constructed over 0.4-4 micro g ml(-1) for urine and 0.1-2 micro g ml(-1) for blood, using proadifen as the reference compound. The average extraction recoveries were 75% for urine and 78% for blood. The limits of detection and quantitation were 0.071 and 0.24 micro g ml(-1), respectively. Coefficients of variation were <10% and accuracy was within +/-12%. The average blood concentrations of cocaine, benzoylecgonine and ecgonine methyl ester in 42 living patients were 0.22, 1.43 and 0.16 micro g ml(-1), respectively. Urine samples were collected from individuals in the criminal justice system (70 cases), from drug abusers admitted to emergency rooms (36 cases) and from patients under detoxification treatment (36 cases). The second group exhibited the highest average concentrations (e.g. 0.97 micro g ml(-1) for cocaine, 5.23 micro g ml(-1) for benzoylecgonine and 0.39 micro g ml(-1) for ecgonine methyl ester). Sixty- five fatal intoxications due to cocaine alone or in combination with other drugs were studied, and average blood levels were found to be higher in the deaths related to cocaine alone (e.g. 0.40 micro g ml(-1) for cocaine, 2.38 micro g ml(-1) for benzoylecgonine and 0.38 micro g ml(-1) for ecgonine methyl ester).

Cocaine↗
PubMed2005

Reductase-mediated metabolism of motexafin gadolinium (Xcytrin) in rat and human liver subcellular fractions and purified enzyme preparations.

The biotransformation of motexafin gadolinium (MGd, Xcytrin) was investigated in subcellular rat and human liver fractions. Microsomal MGd metabolism was dependent on NADPH in both species. Cytosolic metabolism in rat and human livers was dependent on NADPH or NADH. Under anaerobic conditions, MGd metabolism increased in liver microsomes and purified enzyme preparations. Cytochrome P450 (CYP450) inhibitors ketoconazole, proadifen, and carbon monoxide increased NADPH-dependent MGd metabolism in microsomes. Treatment of rats with beta-naphthoflavone increased cytosolic metabolism of MGd twofold, but had no effect on microsomal metabolism. Conversely, in liver preparations from phenobarbital treated rats microsomal metabolism of MGd was enhanced twofold, but not in cytosolic preparations. Purified CYP450 reductase from phenobarbital-treated rabbit or untreated human livers metabolized MGd suggesting involvement of CYP450 reductase. Dicumarol, a potent DT-diaphorase inhibitor, inhibited MGd metabolism in both rat and human liver cytosol. These data suggest MGd metabolism in rat liver involves CYP450 reductase and/or DT-diaphorase. In human liver preparations only CYP450 reductase is directly involved in MGd metabolism. A metabolite identified in microsomes and cytosol is a metal-free, reduced form of MGd, indicating that both enzymes generate metabolite 1, which appears to be PCI-0108, a synthetic precursor to MGd.

Animals↗
PubMed1997

Nitric oxide and peroxynitrite affect differently acetylcholine release, choline acetyltransferase activity, synthesis, and compartmentation of newly formed acetylcholine in Torpedo marmorata synaptosomes.

Recent reports proposed that nitric oxide was a modulator of cholinergic transmission. Here, we examined the role of NO on cholinergic metabolism in a model of the peripheral cholinergic nervous synapse: synaptosomes from Torpedo electric organ. The presence of NO synthase was immunodetected in the cell bodies, in the nerve ending area of nerve-electroplate tissue and in the electroplates. Exogenous source of NO was provided from SIN1, a donor of NO and O2-., and an end-derivative peroxynitrite (ONOO-). SIN1 increased calcium-dependent acetylcholine (ACh) release induced by KCl depolarization or a calcium ionophore A23187. The formation of ONOO- was continuously followed by a new chemiluminescent assay. The addition of superoxide dismutase, that decreases the formation of ONOO-, did not impair the stimulation of ACh release, suggesting that NO itself was the main stimulating agent. When the endogenous source of NO was blocked by proadifen, an inhibitor of cytochrome P450 activity of NO synthase, both KCl- and A23187-induced ACh release were abolished; nevertheless, the inhibitor Ng-monomethyl-L-arginine did not modify ACh release when applied in a short time duration of action. Both NO synthase inhibitors reduced the synthesis of ACh from the radioactive precursor acetate and its incorporation into synaptic vesicles as did ONOO- chemically synthesized or formed from SIN1. In addition, choline acetyltransferase activity was strongly inhibited by ONOO- and SIN1 but not by the NO donors SNAP and SNP or, by NO synthase inhibitors. Altogether these results indicate that NO and ONOO modulate presynaptic cholinergic metabolism in the micromolar range, NO (up to 100 microM) being a stimulating agent of ACh release and ONOO- being an inhibitor of ACh synthesis and choline acetyltransferase activity.

Acetylcholine↗
PubMed1990

CGP 28014, a new inhibitor of cerebral catechol-O-methylation with a non-catechol structure.

CGP 28014 (N-(2-pyridone-6-yl)-N',N'-di-n-propylformamidine) or its methanesulfonate salt CGP 28014 A was suspected to be a catechol-O-methyl-transferase (COMT) inhibitor because it was found to reduce the levels of homovanillic acid (HVA) and to increase those of 3,4-dihydroxyphenylacetic acid (DOPAC) in the rat striatum, after oral or intraperitoneal administration. These effects were maintained after repeated administration. The compound was only weakly active as a COMT inhibitor in vitro. However, its effect on striatal HVA and DOPAC was not prevented by pretreatment with the inhibitor of microsomal drug metabolizing enzymes in the liver, proadifen, indicating that, if CGP 28014 acts as a prodrug, its conversion to the active compound is not by oxidative metabolism in the liver. Also, there was no evidence that conversion to 2-amino-6-hydroxypyridine could explain its effects. The in vivo effect of CGP 28014 was substantiated in two additional in vivo test systems. Thus, it inhibited the accumulation of 3-methoxytyramine in the rat striatum after MAO inhibition by clorgyline, and the formation of O-methyl-DOPA from exogenously administered DOPA. It proved to be equipotent or nearly so with tropolone, and also showed a similar duration of action. Similar to tropolone, it increased S-adenosylmethionine levels in the striatum. Pyrogallol, on the other hand, decreased them, because being a substrate of COMT, it consumes methyl groups. This suggests that CGP 28014 does not inhibit COMT because it is a substrate of the enzyme.(ABSTRACT TRUNCATED AT 250 WORDS)

3,4-Dihydroxyphenylacetic Acid↗
PubMed1990

Neuromelanin synthesis in rat and human substantia nigra.

A relation between neuromelanin synthesis and vulnerability of dopaminergic neurons is suggested by the fact that heavily pigmented cells are preferentially lost in aging and Parkinson's disease and that the dopaminergic neurotoxin MPP+ (1-methyl-4-phenyl-pyridine) binds to neuromelanin. To elucidate the mechanism of neuromelanin synthesis, we studied the formation of melanin in homogenates of human and rat substantia nigra tissue "in vitro". It was found that enzymatic processes accounted for 70% and 90% of the melanin formation in homogenates of human and rat tissue, respectively. The enzymatic synthesis was due to the activity of monoamine oxidase (MAO), since it was prevented by selective inhibitors of this enzyme. Both MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) and MPP+ inhibited melanin formation, probably due to their ability to inhibit MAO. No evidence was found for involvement of cytochrome P-450 monooxigenases, which have been postulated to exist in central catecholaminergic neurons. Proadifen reduced melanin formation, not necessarily because it is an inhibitor of P-450 monooxigenases, but rather as it is also a potent inhibitor of MAO. Some antioxidants like ascorbic acid, but not agents destroying hydrogen peroxide, inhibited melanin formation. The findings suggest that the formation of neuromelanin in the substantia nigra involves MAO and non-enzymatic oxidative processes.

1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine↗
PubMed2000

Discovery of an 11 (R)- and 12(S)-lipoxygenase activity in ovaries of the mussel Mytilus edulis.

Eicosanoid biosynthesis was investigated in mussel gonads by incubation of tissue homogenates with radiolabeled arachidonic acid and analysis of the products by radio-high-performance liquid chromatography. No radiolabeled metabolites were formed in homogenates of testes, but two major metabolites were synthesized by ovarian preparations. The radiolabeled metabolites were analyzed by mass spectrometry and chiral chromatography and identified as 11 (R)-hydroxy-5,8,1 2,14-eicosatetraenoic acid and 12(S)-hydroxy-5,8,10,14-eicosatetraenoic acid. In addition, four other nonlabeled metabolites, formed from endogenous substrates, were detected in ovarian extracts. Their structures, determined by mass spectrometric analysis, were the corresponding 11- and 12-hydroxy analogs formed from eicosapentaenoic acid (11-HEPE and 12-HEPE) and 9-hydroxy-6,10,12,15-octadecatetraenoic acid (9-HOTE) and 13-hydroxy-6,9,11,15-octadecatetraenoic acid formecl from stearidonic acid. The biosynthesis of the 11 - and 12-hydroxy products was calcium dependent, localized to the 100,000 x g supernatant cell fraction, and was inhibited by nordihydroguaiaretic acid, but not inhibited by the prostaglandin synthase inhibitors aspirin and indomethacin, or the monoxygenase inhibitor proadifen. Together these data suggested that both the 11 (R)- and 12(S)-hydroxy products were formed from lipoxygenase-type enzymes. Incubation of homogenates of immature ovaries with eicosapentaenoic acid revealed the major product to be I2-HEPE, whereas in mature ovaries mainly 11-HEPE was formed. Extraction of spawned eggs with methanol revealed that predominantly 11-HEPE and 9-HOTE were formed from endogenous substrates. This study shows that female gonads of the mussel express an 11(R)- and 12(S)-lipoxygenase activity whose expression is dependent on differentiation of the ovary.

Animals↗
PubMed1983

Oxidation of dimethylamine and trimethylamine in methazotrophic yeasts by microsomal mono-oxygenases sensitive to carbon monoxide.

Whole cells of Candida boidinii grown on di- or tri-methylamine as sole nitrogen source readily oxidized both amines. The oxidation was potently inhibited by carbon monoxide. Cell-free extracts required the presence of 20 microM FAD before mono-oxygenase activity with both amines could be demonstrated. NADH was a better electron donor than NADPH. Activity was present in cells grown on secondary and tertiary amines but not on primary amines, and was detected in a number of different yeasts. Enzyme activity could be sedimented at 187 000 x g, and was associated with NADPH-cytochrome c reductase activity. It is thus probably microsomal. Activity was inhibited by cyanide, mercaptoethanol, carbon monoxide and proadifen hydrochloride (SKF 525-A).

Candida↗
PubMed1989

Determination of brain concentrations of 8-hydroxy-2-(di-n-propylamino)tetralin by liquid chromatography with electrochemical detection.

A liquid chromatographic method using electrochemical detection is described for the assay of brain concentrations of 8-hydroxy-2-(di-n-propylamino)tetralin (8-OH-DPAT), centrally acting serotonin agonists selective for the 5HT-1A subtype of serotonin receptors. The method is sensitive to approximately 5 ng/g concentrations. After a 1mg/kg s.c. dose of 8-OH-DPAT in rats, its concentration in whole brain declined rapidly during the first 4 hr with a half-life of 26 min. At 30 min after a 1 mg/kg s.c. dose of 8-OH-DPAT, concentrations were approximately equal in hypothalamus, striatum, hippocampus, cerebellum and brain stem but were slightly lower in midbrain. 8-OH-DPAT disappeared from hypothalamus, midbrain and hippocampus at similar rates during the first 90 min after a 1 mg/kg s.c dose. Concentrations of 8-OH-DPAT in whole brain were markedly higher after s.c. than after i.p. administration of 8-OH-DPAT, consistent with earlier data showing 8-OH-DPAT to be more potent when given s.c. than when given i.p. in decreasing brain concentrations of 5-hydroxyindoleacetic acid. Pretreatment with proadifen (SKF-525A), an inhibitor of microsomal drug metabolism, slightly increased brain concentrations of 8-OH-DPAT. Pindolol, which antagonized the elevation of serum corticosterone concentration by 8-OH-DPAT, did not alter brain concentrations of 8-OH-DPAT. The analytical method should be useful in correlating brain concentrations of 8-OH-DPAT with various neurochemical, behavioral or other functional effects that have been described for this compound.

8-Hydroxy-2-(di-n-propylamino)tetralin↗