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PubMed1990

Persistent occultation of the vesamicol receptor.

By binding to a specific receptor, the drug vesamicol [(-)-trans-2-(4-phenylpiperidino)cyclohexanol] noncompetitively inhibits acetylcholine active transport into synaptic vesicles. An analog [(+/-)-trans-5-amino-2-hydroxy-3-(4-phenylpiperidino) tetralin] of vesamicol has been discovered that causes time- (t1/2 = 2.6 min) and temperature-dependent loss of vesamicol binding that is only slowly reversible (t1/2 for recovery = 5.4 h). Assuming a simple two step process of ligand binding followed by a conformational change, an apparent dissociation constant of 4 x 10(-11) M can be calculated. Other analogs of the vesamicol family of drugs also display similar high-affinity binding to the receptor in a manner which resembles the time dependent effects of reserpine binding to chromaffin granules.

Animals↗
PubMed2000

l-Menthol-induced [Ca2+]i increase and impulses in cultured sensory neurons.

We investigated the effects of l-menthol on cultured dorsal root ganglion (DRG) cells, instead of free nerve endings of sensory fibers. Using Fura-2 microfluorimetry, we identified a few DRG neurons that showed an increase in intracellular free Ca2+ concentration ([Ca2+]i) in response to l-menthol. They made up only 10% of the neurons activated by a high K+ solution. l-Menthol induced the [Ca2+]i increase in a dose-dependent manner, with an EC50 of 37.9 microM and a Hill coefficient of 0.97. A related compound, cyclohexanol, had no effect. When extracellular Ca2+ was removed, l-menthol did not induce the [Ca2+]i increase. Whole-cell current-clamp recordings revealed that l-menthol induced depolarization (13.2 mV, receptor potential) leading to impulses. We conclude that l-menthol induced the impulses through activation of menthol receptors in a small subset of the cultured sensory neurons.

Animals↗
PubMed1990

Cysteine, a chelating moiety for synthesis of 99Tcm radiopharmaceuticals. III: Functionalization of hydroxy group for 99Tcm chelation.

A method is offered for converting an organic hydroxy compound to a 99Tcm-binding ligand under mild experimental conditions. Cyclohexanol was selected as a typical hydroxy compound and to this molecule cysteine was attached through substitution at the sulphur atom by a two-step chemical synthesis. The ligand thus obtained could be successfully radiolabelled with 99Tcm. The biodistribution of the resulting radiolabelled compound had the characteristic of a mixed hydrophilic-lipophilic 99Tcm chelate and was similar to that of 99Tcm-HIDA derivatives, a well established class of 99Tcm-chelates. So it may be concluded that the above method of functionalization of a hydroxy compound does not generate any unusual physiological properties and may be recommended as a general method for radiolabelling an organic compound at the alcoholic site with 99Tcm.

Animals↗
PubMed2006

Rubrivivax benzoatilyticus sp. nov., an aromatic, hydrocarbon-degrading purple betaproteobacterium.

A brown-coloured bacterium was isolated from photoheterotrophic (benzoate) enrichments of flooded paddy soil from Andhra Pradesh, India. On the basis of 16S rRNA gene sequence analysis, strain JA2(T) was shown to belong to the class Betaproteobacteria, related to Rubrivivax gelatinosus (99 % sequence similarity). Cells of strain JA2(T) are Gram-negative, motile rods with monopolar single flagella. The strain contained bacteriochlorophyll a and most probably the carotenoids spirilloxanthin and sphaeroidene, but did not have internal membrane structures. Intact cells had absorption maxima at 378, 488, 520, 590, 802 and 884 nm. No growth factors were required. Strain JA2(T) grew on benzoate, 2-aminobenzoate (anthranilate), 4-aminobenzoate, 4-hydroxybenzoate, phthalate, phenylalanine, trans-cinnamate, benzamide, salicylate, cyclohexanone, cyclohexanol and cyclohexane-2-carboxylate as carbon sources and/or electron donors. The DNA G+C content was 74.9 mol%. Based on DNA-DNA hybridization studies, 16S rRNA gene sequence analysis and morphological and physiological characteristics, strain JA2(T) is different from representatives of other photosynthetic species of the Betaproteobacteria and was recognised as representing a novel species, for which the name Rubrivivax benzoatilyticus sp. nov. is proposed. The type strain is JA2(T) (=ATCC BAA-35(T)=JCM 13220(T)=MTCC 7087(T)).

Base Composition↗
PubMed1976

Cobalt and plant development: interactions with ethylene in hypocotyl growth.

Co(2+) promoted elongation of hypocotyl segments of light-grown cucumber (Cucumis sativus) seedlings. Time course and dose response data are presented and interactions with IAA, gibberellin, cyclohexanol, and cotyledons described. Segments without cotyledons responded to Co(2+) only if grown in gas-tight vessels with IAA added. When bases of cotyledons were ringed with an inhibitor of auxin transport, Co(2+) caused no growth promotion in the hypocotyl. Co(2+) prevented lateral swelling of hypocotyls treated with supraoptimal IAA. Removal of ethylene from the atmosphere reduced the Co(2+) response, but Co(2+) did not counteract the inhibitory effect of increased ethylene levels. These results are consistent with the hypothesis that Co(2+) promotes hypocotyl elongation by inhibiting ethylene production. The hypothesis was confirmed by a direct demonstration that Co(2+), at growth-promoting concentrations, powerfully inhibited ethylene production in the cucumber hypocotyl.

Journal Article↗
PubMed1990

Partial purification and characterization of indol-3-ylacetylglucose:myo-inositol indol-3-ylacetyltransferase (indoleacetic acid-inositol synthase).

A procedure is described for the purification of the enzyme indol-3-ylacetylglucose:myo-inositol indol-3-ylacetyltransferase (IAA-myo-inositol synthase). This enzyme catalyzes the transfer of indol-3-ylacetate from 1-0-indol-3-ylacetyl-beta-d-glucose to myo-inositol to form indol-3-ylacetyl-myo-inositol and glucose. A hexokinase or glucose oxidase based assay system is described. The enzyme has been purified approximately 16,000-fold, has an isoelectric point of pH 6.1 and yields three catalytically inactive bands upon acrylamide gel electrophoresis of the native protein. The enzyme shows maximum transferase activity with myo-inositol but shows some transferase activity with scyllo-inositol and myo-inosose-2. No transfer of IAA occurs with myo-inositol-d-galactopyranose, cyclohexanol, mannitol, or glycerol as acyl acceptor. The affinity of the enzyme for 1-0-indol-3-ylacetyl-beta-d-glucose is, Km = 30 micromolar, and for myo-inositol is, Km = 4 millimolar. The enzyme does not catalyze the exchange incorporation of glucose into IAA-glucose indicating the reaction mechanism involves binding of IAA glucose to the enzyme with subsequent hydrolytic cleavage of the acyl moiety by the hydroxyl of myo-inositol to form IAA myo-inositol ester.

Acyltransferases↗
PubMed1984

Inactivation of quinoprotein alcohol dehydrogenases with cyclopropane-derived suicide substrates. .

Quinoprotein alcohol dehydrogenases can be inactivated by cyclopropanol, cyclopropanone hydrate, and, depending on whether they can oxidize secondary alcohols, also by cyclopropanone ethyl hemiketal. Only enzyme molecules containing the oxidized coenzyme (PQQ), but not those with the coenzyme in the semiquinone form (PQQH), become inactivated with these compounds. The inactivation process proceeds without proton production or electron acceptor consumption and free radical is not observed in the inactivated enzyme. It could be demonstrated that a stoichiometric relationship exists between enzyme inactivation, PQQ converted, PQQ adduct formed, and cyclopropanol added. Thus the dimeric and monomeric enzyme become fully inactivated with two and one molecule of cyclopropanol, respectively, indicating that the dimeric enzyme contains two independently acting catalytic sites. Inactivation of the enzyme by cyclopropanol and cyclopropanone hydrate produces chromatographically different PQQ adducts. Since cyclopropanemethanol, cyclobutanol and cyclohexanol are not suicide substrates, the inactivation presumably proceeds via a ring opening such as proposed for the metal-ion-catalysed degradation of cyclopropane derivatives. The results are in accordance with our view on the reaction mechanism of these enzymes but not with that of others [Mincey et al. (1981) Biochemistry 20, 7502-7509]. The reasons why their model has to be refuted are discussed.

Alcohol Oxidoreductases↗
PubMed1987

Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes.

Three-dimensional models of human alcohol dehydrogenase subunits have been constructed, based on the homologous horse enzyme, with computer graphics. All types of class I subunits (alpha, beta, and gamma) and the major allelic variants (beta 1/beta 2 and gamma 1/gamma 2) have been studied. Residue differences between the E-type subunit of the horse enzyme and any of the subunits of the human isozymes occur at 64 positions, about half of which are isozyme-specific. About two thirds of the substitutions are at the surface and all differences can be accommodated in highly conserved three-dimensional structures. The model of the gamma isozyme is most similar to the crystallographically analyzed horse liver E-type alcohol dehydrogenase, and has all the functional residues identical to those of the E subunit except for one which is slightly smaller: Val-141 in the substrate pocket. The residues involved in coenzyme binding are generally conserved between the horse enzyme and the alpha, beta, and gamma types of the human enzyme. In contrast, single exchanges of these residues are the ones involved in the major allelic differences (beta 1 versus beta 2 and gamma 1 versus gamma 2), which affects the overall rate of alcohol oxidation since NADH dissociation is the rate-determining step. Residue 47 is His in beta 2 and Arg in the beta 1, gamma 1, and gamma 2 subunits, and in horse liver alcohol dehydrogenase. Both His and Arg can make a hydrogen bond to a phosphate oxygen atom of NAD; hence the lower turnover rate of beta 1 apparently derives from a charge effect. The substitution to Gly in the alpha subunit results in one less hydrogen bond in NAD binding, and consequently in rapid dissociation. This may explain why the overall rate is an order of magnitude faster than that of beta 1. The important difference between gamma 1 and gamma 2 is an exchange at position 271 from Arg to Gln which can give a hydrogen bond from Gln in gamma 2 to the adenine of NAD. The tighter binding to gamma 2 can account for the slower overall catalytic rate in this isozyme. The kinetics and interactions of cyclohexanol and benzyl alcohol with the isozymes were judged by docking experiments using an interactive fitting program.(ABSTRACT TRUNCATED AT 400 WORDS)

Alcohol Dehydrogenase↗
PubMed1993

Isozyme developments in mammalian class-I alcohol dehydrogenase. cDNA cloning, functional correlations, and lack of evidence for genetic isozymes in rabbit.

Isozyme patterns differ widely among the classical type (class I) of mammalian alcohol dehydrogenases. For the rabbit enzyme, the possibility of isozymes has been reported but structural evidence is lacking. This system was now studied at both the mRNA/cDNA and protein levels. Ten cDNA clones, coding for class-I alcohol dehydrogenase, were isolated from a rabbit liver cDNA library using a human DNA fragment as probe. The cDNA spanned 1296 bp, including the entire coding region. All clones coded for the same polypeptide and Northern blots identified a single mRNA corresponding to about 1.5 kb. Comparison of two protein forms (CC and BC) by HPLC peptide fingerprinting and structural analysis revealed peptide segments identical in amino acid sequence. Consequently, direct protein analyses and Northern blots show the presence of only one primary translation product. The data suggest that lagomorphic alcohol dehydrogenase, like the rodent enzyme, is not as isozyme rich as it may appear superficially, and that secondary modifications contribute substantially to mammalian alcohol dehydrogenase multiplicity. The active center of the rabbit enzyme suggests similarities to the horse S, human gamma, and rat enzyme structures, compatible with a steroid dehydrogenase activity shown experimentally. Typical class-I properties were established by direct analysis and confirmed by structural properties (Km for cyclohexanol 0.8-1.1 mM, for ethanol 1.6-1.9 mM). The isozyme versus species differences mark the variability of class-I alcohol dehydrogenase versus class III and suggest a parallelism between rapid mutational differences and frequent duplicatory events.

Alcohol Dehydrogenase↗
PubMed1985

Accumulation, acetylation, and releasability of diethylhomocholine from a sympathetic ganglion.

Superior cervical ganglia of the cat perfused with [14C]diethylhomocholine [( 14C]DEHCh) synthesized acetyldiethylhomocholine (ADEHCh), but rather little of this ester was released by subsequent preganglionic nerve stimulation. Stimulation evoked the release of an appreciable amount of unchanged DEHCh when ganglia had been exposed to the analogue in the absence of choline (Ch), but did not do so when exposed to both Ch and DEHCh. The release of DEHCh was Ca2+ dependent, and was not the result of the release and subsequent hydrolysis of ADEHCh. This is the first clear demonstration of the release of an unacetylated compound from mammalian tissue; therefore, the characteristics of the transmitter release mechanism are further defined. The effect of preganglionic nerve stimulation on the uptake and acetylation of DEHCh was also measured. Stimulated ganglia accumulated approximately 4 times more labeled analogue and synthesized 7.5 times more ADEHCh than did rested ganglia. Stimulated ganglia perfused with 2-(4-phenylpiperidino)cyclohexanol, a compound considered to inhibit acetylcholine (ACh) release by inhibiting its transport into synaptic vesicles, accumulated 3.4 times as much and acetylated 6 times as much DEHCh as did rested ganglia. When the concentration of Mg2+ in the perfusion medium was increased to block ACh release, accumulation of the labelled analogue was enhanced by stimulation, but its acetylation was increased much less than during perfusion with normal medium. It is concluded that the synthesis of ADEHCh is subject to the same regulation as is ACh synthesis and that the activation of ester synthesis during activity can be dissociated from ester release.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetylation↗
PubMed1986

Stoichiometries of acetylcholine uptake, release, and drug inhibition in Torpedo synaptic vesicles: heterogeneity in acetylcholine transport and storage.

Highly purified Torpedo electric organ synaptic vesicles form a 49 nM suspension at 1 mg protein/ml. Under active transport conditions hundreds of molecules of [3H]acetylcholine ([3H]ACh) can be accumulated per vesicle, which requires the ACh transporter to undergo multiple turnovers. The transport blocker trans-2-(4-phenylpiperidino)cyclohexanol (AH5183) has no effect on storage of endogenous ACh by vesicles. In contrast, AH5183, other blocking drugs, and nonradioactive ACh caused a rapid release of at least 30-63 molecules of newly transported [3H]ACh per vesicle. Thus AH5183 distinguishes recently transported "new" vesicular ACh from "old" endogenous ACh. l-AH5183 inhibits transport of ACh with a half-inhibitory concentration of 16 +/- 7 nM at 12 nM vesicles and 115 +/- 34 nM at 120 nM vesicles. With the assumption that AH5183 acts on a receptor in an unamplified manner about 2.7 or fewer receptors per vesicle need to be occupied to cause inhibition of ACh transport. The apparent amplification in the number of [3H]ACh molecules per vesicle that are released by AH5183 suggests that AH5183 inhibits ACh storage by an indirect mechanism that distinguishes new from old ACh.

Acetylcholine↗
PubMed1986

Acetylcholine transport and drug inhibition kinetics in Torpedo synaptic vesicles.

Steady-state initial velocity uptake of [3H]acetylcholine ([3H]ACh) by purified Torpedo electric organ synaptic vesicles was studied. Transport specific activity decreased at higher vesicle concentration. Michaelis-Menten type kinetics describe [3H]ACh active transport at constant vesicle concentration with no evidence of cooperativity or transporter heterogeneity. The ACh dissociation constant is about 0.3 mM, transport has a maximal velocity of about 1.6 nmol/min/mg protein, and both are dependent on the vesicle preparation. Nonradioactive ACh was a competitive inhibitor with respect to [3H]ACh. The potent transport inhibitor dl-trans-2-(4-phenylpiperidino)cyclohexanol (AH5183) is a non-competitive inhibitor with respect to [3H]ACh, with an inhibition constant of 41 +/- 7 nM. Inhibition by AH5183 is reversible. The results suggest that AH5183 does not bind to the ACh transporter recognition site on the outside of the vesicle membrane, and thus it might inhibit allosterically.

Acetylcholine↗
PubMed1988

Calcium-independent release of acetylcholine from electric organ synaptosomes and its changes by depolarization and cholinergic drugs.

Chemiluminescent detection was applied to measure the continuous spontaneous Ca2+-independent liberation of acetylcholine (ACh) from Torpedo electric organ synaptosomes. Differentiation between the release of ACh and choline was achieved by inhibiting cholinesterases with phospholine, and a way to quantify the continuous release was devised. The method permitted measurements during short time intervals from minute amounts of tissue and without an accumulation of ACh in the medium. Synaptosomes continuously liberated small amounts of ACh during incubations in the presence of 3 mM K+ and in the absence of Ca2+. The spontaneous liberation of ACh was similar both quantitatively and qualitatively at pH values of 8.6 and 7.8. It was unaltered by MgCl2 (10.4 mM), 2-(4-phenylpiperidino)cyclohexanol (10 microM), ouabain (104 microM), atropine (10 microM), and valinomycin (102 nM). Carbamoylcholine brought about a decrease, which could be partially reversed by atropine. The Ca2+-independent output of ACh was increased considerably when the concentration of K+ ions was raised (eightfold at 103 and 35-fold at 203 mM K+). Carbamoylcholine (104 microM) blocked the increase in ACh release produced by high K+; this effect of carbamoylcholine was not reversed by atropine (10 microM). When Ca2+ was added to synaptosomes depolarized by a high concentration of K+, the amount of ACh released during the first 1-3 min after the addition of Ca2+ was at least 20 times higher than in the absence of Ca2+, but the release returned rapidly to predepolarization values. Similarly high values of ACh release could be achieved by adding Ca2+ plus the ionophore A23187 and even higher values by adding Ca2+ plus gramicidin.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetylcholine↗
PubMed1989

Regulation of the vesamicol receptor in cholinergic synaptic vesicles by acetylcholine and an endogenous factor.

Cholinergic synaptic vesicles obtained from Torpedo electric organ have an active transport system for acetylcholine (ACh). Linked to ACh transport is a cytoplasmically oriented receptor for the inhibitory drug (-)-trans-2-(4-phenylpiperidino)cyclohexanol (vesamicol, formerly AH5183). Storage of freshly isolated vesicles for several days leads to more vesamicol binding. This can be induced immediately by hyposmotic lysis of the vesicles, which reseal to form right-side-out ghosts. The increased drug binding was due to a twofold increase in the affinity and a 20% increase in the amount of the receptor expressed, probably as a result of the release of an endogenous factor. Binding of vesamicol to ghosts was specifically inhibited by exogenous ACh acting with a dissociation constant of 18 mM. This suggests that the vesamicol binding site probably is linked to a low-affinity ACh binding site that is different from the higher affinity transport binding site. Equilibrium and kinetic attempts to determine whether exogenous ACh acts on the outside or the inside of the ghost membrane to inhibit vesamicol binding failed because of rapid equilibration of exogenous ACh across the ghost membrane. It is argued that the endogenous factor released by hyposmotic lysis might be ACh. Potential roles for such a transmembrane signal regulating the vesamicol receptor are discussed.

Acetylcholine↗
PubMed1991

Ca2+o-independent veratridine-evoked acetylcholine release from striatal slices is not inhibited by vesamicol (AH5183): mobilization of distinct transmitter pools.

The effect of 2-(4-phenylpiperidino)cyclohexanol (AH5183 or vesamicol), a compound known to block the uptake of acetylcholine (ACh) into cholinergic synaptic vesicles, on the release of endogenous and [14C]ACh from slices of rat striatum was investigated. ACh release was evoked either by electrical stimulation or by veratridine. The effect of electrical stimulation was entirely dependent on external Ca2+. By contrast, veratridine (40 microM) also enhanced ACh release in the absence of Ca2+. Indeed, with veratridine two components were clearly distinguished: one dependent on external Ca2+ and the other not. Vesamicol inhibited [14C]ACh release evoked by both veratridine and electrical stimulation in the presence of external Ca2+, provided it was added to the tissue prior to loading with [14C]choline. With the same treatment vesamicol only slightly affected the release of endogenous ACh. Under the same conditions the Ca2(+)-independent [14C]ACh release evoked by veratridine was not prevented by vesamicol. The differential responsiveness to vesamicol suggests that ACh pools involved in Ca2+o-dependent ACh release are different from those mobilized during Ca2+o-independent ACh release.

Acetylcholine↗
PubMed1992

Vesamicol binding to subcellular membranes that are distinct from catecholaminergic vesicles in PC12 cells.

We have examined PC12 cells for the localization of binding sites for vesamicol [l-2-(4-phenylpiperidino) cyclohexanol], a compound that has previously been shown to bind to cholinergic vesicles and to inhibit the uptake of acetylcholine. Initial studies presented in this article demonstrate the existence of a specific, saturable vesamicol binding site in PC12 cells. Subsequent experiments show that these binding sites reside in a membrane population that is distinct from catecholamine-containing compartments with respect to density and antigenic composition. In particular, vesamicol binding compartments have a lower density than catecholaminergic vesicles and, unlike these latter vesicles, do not appear to contain the vesicle-specific proteins synaptophysin and SV2 as part of the same membrane. These results suggest that vesicular transport proteins for acetylcholine and catecholamines are differentially sorted to distinct membrane compartments in PC12 cells.

Animals↗
PubMed1992

Mobilization of the readily releasable pool of acetylcholine from a sympathetic ganglion by tityustoxin in the presence of vesamicol.

The present experiments tested whether preganglionic stimulation and direct depolarization of nerve terminals by tityustoxin could mobilize similar or different pools of acetylcholine (ACh) from the cat superior cervical ganglia in the presence of 2-(4-phenylpiperidino)cyclohexanol (vesamicol, AH5183), an inhibitor of ACh uptake into synaptic vesicles. In the absence of vesamicol, both nerve stimulation and tityustoxin increased ACh release. In the presence of vesamicol, the release of ACh induced by tityustoxin was inhibited, and just 16% of the initial tissue content could be released, a result similar to that obtained with electrical stimulation under the same condition. When the impulse-releasable pool of ACh had been depleted, tityustoxin still could release transmitter, amounting to some 10% of the ganglion's initial content. This pool of transmitter seemed to be preformed in the synaptic vesicles, rather than synthesized in response to stimuli, as tityustoxin could not release newly synthesized [3H]ACh formed in the presence of vesamicol, and hemicholinium-3 did not prevent the toxin-induced release. In contrast to the results with tityustoxin, preganglionic stimulation could not release transmitter when impulse-releasable or toxin-releasable compartments had been depleted. Our results confirm that vesamicol inhibits the mobilization of transmitter from a reserve to a more readily releasable pool, and they also suggest that, under these experimental conditions, there might be some futile transmitter mobilization, apparently to sites other than nerve terminal active zones.

Acetylcholine↗
PubMed1993

Mobilization of a vesamicol-insensitive pool of acetylcholine from a sympathetic ganglion by ouabain.

These experiments investigate the release of transmitter from the perfused superior cervical ganglia of cats induced by ouabain in the absence or presence of 2-(4-phenylpiperidino)cyclohexanol (vesamicol), a blocker of acetylcholine (ACh) uptake. Ouabain, perfused through the ganglia, released ACh in a Ca(2+)-dependent way. Vesamicol caused some inhibition of the release of ACh by ouabain; however, under this condition, the Na+,K(+)-ATPase inhibitor released five times more transmitter than did preganglionic stimulation at 5 Hz. Also, when ganglia exposed to vesamicol were depleted of the impulse-releasable pool of ACh, subsequent perfusion with ouabain released ACh, and this included ACh newly synthesized in the presence of vesamicol; this phenomenon could be inhibited by the lack of Ca2+ and presence of EGTA, and was completely abolished by perfusion with a medium containing 18 mM Mg2+. To test whether the release of this vesamicol-insensitive Ca(2+)-dependent pool by ouabain is associated with a decrease in the number of synaptic vesicles, ganglia treated with the ATPase inhibitor after the depletion of the impulse-releasable pool of ACh were fixed for electron microscopy. In the presence of Ca2+, coincident with the release of the vesamicol-insensitive pool of ACh, nerve terminals were almost depleted of synaptic vesicles; ganglia treated similarly, but with medium containing 18 mM Mg2+ instead of Ca2+, were not depleted of synaptic vesicles. These results suggest that ouabain releases a vesamicol-insensitive pool of ACh from the sympathetic ganglion and also support the notion that this compartment is vesicular and its exocytosis depends on extracellular Ca2+. It is suggested that empty-vesicle recycling in the presence of vesamicol restricts mobilization of full vesicles to release sites.

Acetylcholine↗