[General and sedative action of some esters of 4-piperidino-cyclohexanol].
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Animals↗
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Thermodynamic elucidation of solute-induced lipid interdigitation phase: lipid interactions with hydrophobic versus amphipathic species.
Comparative thermodynamic studies on the interactions of aqueous dispersions of dipalmitoyl phosphatidylcholine (DPPC) bilayer vesicles with hydrophobic and amphipathic species were conducted to elucidate the nature of the solute-induced interdigitated lipid phase. Cyclohexanol, a strong hydrophobic species, lowers the temperature (tm) of the lipid main phase transition from the gel to the liquid-crystalline phase. Unlike ethanol (an amphipathic species), as reported previously, cyclohexanol does not exert a biphasic effect on tm (lowering tm at lower concentrations and raising tm at higher concentrations). At cyclohexanol greater than or equal to 15.4 mg/ml or 0.154 M, the thermogram of DPPC vesicles exhibits a small transition adjacent to the main phase transition but at a lower temperature. In contrast, ethanol does not promote such a small transition. Furthermore, the enthalpy (delta H) of the transition is increased in the presence of cyclohexanol. The sign of the enthalpy change (delta H-delta Ho) is positive and that of the free energy change (delta G-delta Go) is negative, a characteristic of solute-solute hydrophobic interaction. In contrast, DPPC bilayer vesicles exhibit both (delta H-delta Ho) and (delta G-delta Go) greater than 0 in the presence of ethanol in a concentration range where lipid vesicles exist in an interdigitated phase. To support the above distinct thermodynamic observations, fluorescence steady-state polarization (P) measurements were also performed. At the temperature below tm, the value of P decreases as cyclohexanol concentration increases, while a biphasic effect on P was found in the presence of ethanol. These findings support the postulation that the solute-induced interdigitated lipid phase requires the solute molecule to be amphipathic in nature.
1,2-Dipalmitoylphosphatidylcholine↗
Monitoring of exposure to cyclohexanone through the analysis of breath and urine.
Occupational exposure to cyclohexanone was studied for 59 workers through the analysis of environmental air, alveolar air, and urinary cyclohexanol. Environmental cyclohexanone exposure was measured by personal sampling with a carbon-felt passive dosimeter. Cyclohexanone in alveolar air and cyclohexanol in urine were determined with gas chromatography with a flame ionization detector. The end-of-shift urinary cyclohexanol levels correlated well with the time-weighted average environmental cyclohexanone values (r = 0.66). Urinary cyclohexanol corrected for creatinine correlated best with cyclohexanone in air (r = 0.77); when corrected for specific gravity, it gave a similar correlation coefficient (r = 0.73). When the time-weighted average of the exposure was 25 ppm, the corresponding calculated concentration for urinary cyclohexanol was 54.5 mg/1, 23.3 mg/g of creatinine, or 43.5 mg/l at a specific gravity of 1.018. The relationship between cyclohexanone exposure and its concentration in exhaled breath was found to be poorer than that for cyclohexanone exposure and the urinary metabolite (r = 0.51).
Adolescent↗
The metabolites of cyclohexylamine in man and certain animals.
1. [1-(14)C]Cyclohexylamine hydrochloride was synthesized and given orally or intraperitoneally to rats, rabbits and guinea pigs (dose 50-500mg/kg) and orally to humans (dose 25 or 200mg/person). The (14)C is excreted mainly in the urine, most of the excretion occurring in the first day after dosing. Only small amounts (1-7%) are found in the faeces. 2. In the rat, guinea pig and man, the amine is largely excreted unchanged, only 4-5% of the dose being metabolized in 24h in the rat and guinea pig and 1-2% in man. In the rabbit about two-thirds of the dose is excreted unchanged and about 30% is metabolized. 3. In the rat, five minor metabolites were found, namely cyclohexanol (0.05%), trans-3- (2.2%), cis-4- (1.7%), trans-4- (0.5%) and cis-3-aminocyclohexanol (0.1% of the dose in 24h). 4. In the rabbit, eight metabolites were identified, namely cyclohexanol (9.3%), trans-cyclohexane-1,2-diol (4.7%), cyclohexanone (0.2%), cyclohexylhydroxylamine (0.2%) and trans-3- (11.3%), cis-3- (0.6%), trans-4- (0.4%) and cis-4-aminocyclohexanol (0.2%). 5. In the guinea pig, six minor metabolites were found, namely cyclohexanol (0.5%), trans-cyclohexane-1,2-diol (2.5%) and trans-3- (1.2%), cis-3- (0.2%), trans-4- (0.2%) and cis-4-aminocyclohexanol (0.2%). 6. In man only two metabolites were definitely identified, namely cyclohexanol (0.2%) and trans-cyclohexane-1,2-diol (1.4% of the dose), but man had been given a smaller dose (3mg/kg) than the other species (50mg/kg). 7. The hydroxylated metabolites of cyclohexylamine were excreted in the urine in both free and conjugated forms. 8. Although cyclohexylamine is metabolized to only a minor extent, in rats the metabolism was mainly through hydroxylation of the cyclohexane ring, in man by deamination and in guinea pigs and rabbits by ring hydroxylation and deamination.
Animals↗
The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter species.
1. Acinetobacter TD63 was one of some thirty organisms isolated by elective culture with trans-cyclohexan-1,2-diol as sole source of carbon. The great majority of these isolates displayed the same growth spectrum as Nocardia globerula CL1 and Acinetobacter NCIB 9871 being capable of utilizing trans-cyclohexan-1,2-diol, 2-hydroxycyclohexan-1-one, cyclohexanol, cyclohexanone,1-oxa-2oxocycloheptane and adipate and were assumed to use well described metabolic pathways. 2. Acinetobacter TD63 was distinctive in being incapable of growth with cyclohexanol, cyclohexanone or 1-oxa-2-oxocycloheptane and because of this it was hoped that it would display an alternative pathway for the oxidation of trans-cyclohexan-1,2-diol. 3. Studies with cell extracts have shown the presence of inducible dehydrogenase for the conversion of trans-cyclohexan-1,2-diol to 2-hydroxycyclohexan-1-one and cyclohexan-1,2-dione and of 6-oxohexanoate to adipate. These enzymes are linked into a metabolic sequence by the action of a monooxygenase of broad specificity but efficiently capable of converting 2-hydroxy-cyclohexan-1-one into the lactone 1-oxa-2-oxo-7-hydroxycycloheptane that spontaneously rearranges to yield 6-oxohexanoate. 4. An enzyme capable of attacking cyclohexan-1,2-dione (mono-enol) in the absence of an electron donor or oxygen has also been detected. Evidence has been presented indicating that this enzyme catalyses a keto-enol tautomerization between cyclohexan-1,2-dione (mono-enol) and cyclohexan-1,2-dione (mono-hydrate) and is not involved in the pathway of ring cleavage. 5. The failure of Acinetobacter TD63 to grow with cyclohexanol, cyclohexanone or 1-oxa-2-oxocycloheptane is due not to this organism possessing a distinctive metabolic sequence but to a narrow inducer specificity coupled with an inability to form a lactone hydrolase enabling it to cleave the stable 1-oxa-2-oxocycloheptane which is an intermediate in the established pathway of cyclohexanol and cyclohexanone oxidation.
Acinetobacter↗
Effect of modifiers on the hydrolysis of basic and neutral peptides by carboxypeptidase B1.
The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly. The hydrolysis of the tripeptide Bz-Gly-Gly-Phe is also activated by Bz-Gly and Bz-Gly-Gly, but none of these modifiers activate the hydrolysis of Bz-Gly-Gly-Lys, Z-Leu-Ala-Phe, or Bz-Gly-phenyllactic acid by CPB. All modifiers except cyclohexanol display inhibitory modes of binding when present in high concentration. Examination of Lineweaver-Burk plots in the presence of fixed concentrations of Bz-Gly has shown that activation of the hydrolysis of neutral and basic peptides by CPB, as reflected in the values of the extrapolated parameters, Km(app) and kcat, occurs by different mechanisms. For Bz-Gly-Gly-Phe, activation occurs because the enzyme-modifier complex has a higher affinity than the free enzyme for the substrate, whereas activation of the hydrolysis of Bz-Gly-Lys derives from an increase in the rate of breakdown of the enzyme-substrate complex to give products. Cyclohexanol differs from Bz-Gly and Bz-Gly-Gly in that it displays no inhibitory mode of binding with any of the substrates examined, activates only the hydrolysis of dipeptides by CPB, and has a greater effect on the hydrolysis of the basic dipeptide than on the neurtal dipeptide. Moreover, when Bz-Gly-Lys is the substrate, cyclohexanol activates its hydrolysis by CPB by increasing both the enzyme-substrate binding affinity and the rate of the catalytic step, an effect different from that observed when Bz-Gly is the modifier. The anomalous kinetic behavior of CPB is remarkably similar to that of carboxypeptidase A, and is a good indication that both enzymes have very similar structures in and around their respective active sites. A binding site for activator molecules down the cleft of the active site is proposed for CPB to explain the observed kinetic behavior.
Animals↗
Procedures for measuring cytochrome P-450-dependent hydroxylation activity in reproductive tissues.
Cytochrome P-450 is present in the endoplasmic reticulum at varying concentrations in almost all tissues. However, the existence and role of cytochrome P-450 in normal and neoplastic reproductive tissues has not been clearly demonstrated. Our interest lies in the possibility that variations in cytochrome P-450 levels may influence the responsiveness of breast and endometrial carcinomas to endocrine therapy. This may be of particular importance with agents such as tamoxifen where hydroxylation reactions are known to alter therapeutic activities. Therefore, a simple, sensitive spectrophotometric assay for determining levels of cytochrome P-450-dependent cyclohexane hydroxylase activity in breast and uterine microsomes has been developed. Cyclohexane was chosen as a substrate because of the relatively high levels of cyclohexane hydroxylase activity in tumor microsomes and because cyclohexane serves as a substrate for several forms of cytochrome P-450. In order to confirm the results of the spectrophotometric assay, a direct method utilizing isotope dilution gas chromatography/mass spectrometry (GC/MS) has been developed for detecting low levels of the hydroxylated product, cyclohexanol. By employing a stable isotopically labeled analog of cyclohexanol (cyclohexanol-d12), good agreement was demonstrated between the simple, indirect method (measuring NADPH oxidation at 340 nm) and the more complex, direct method (measuring cyclohexanol formation) utilizing GC/MS. The agreement of results obtained using these two techniques indicates that they are equally valid measures of NADPH-dependent cyclohexane hydroxylase activity. The use of the spectrophotometric method is proposed for rapid, multiple assays such as in the clinical setting, reserving GC/MS analysis for use as a research tool.
Animals↗
A spectroscopic investigation of the conformational dynamics of insulin in solution.
A conformational change, termed the T --> R transition, which can be detected by visible, circular dichoric, and fluorescence spectroscopy, occurs in native insulin and tryptophan substituted insulin analogs ([TrpB25]-, [TrpB26]-, [GlyB24,TrpB25]-, and [GlyB24,TrpB26]insulin) upon binding specific alcohol ligands, including phenol and cyclohexanol. In these studies we have demonstrated that changes in the visible absorbance spectrum of an insulin6(Co2+)2 solution are not a definitive means of determining the occurrence of T --> R transitions in the presence of alcohol ligands. We also have presented evidence that fast protein liquid chromatography (FPLC) can be used to determine the aggregation state of insulin and that des-octapeptide(B23-30)insulin (DOI) forms Zn(2+)-coordinated hexamers that appear to be stabilized by the T --> R transformation. Using fluorescence spectroscopy, we have shown that in the presence of specific alcohol ligands the B-chain COOH-terminal residues, particularly position B25, of hexameric, as well as monomeric insulin undergo a conformational change which appears to be related to the T --> R transformation. Circular dichroic studies indicate that a conformation similar to the R-state of metal-coordinated hexameric insulin can be induced by binding cyclohexanol; however, this new conformational state (RI-state) exists independent of divalent metal ion coordination, and therefore of hexamer formation. We further show that monomeric insulin can be induced to assume the RI-state upon alcohol binding, therefore illustrating the first defined conformational change described for monomeric insulin. We suggest that this new conformation may be an intermediate state in the T --> R transformation in metal-coordinated hexameric insulin, such that T --> RI --> R. The model presented here of the structural adjustments undergone by insulin upon binding cyclohexanol provides further insight into the conformational flexibility of insulin in solution.
Circular Dichroism↗
Reactivity of horse liver alcohol dehydrogenase with 3-methylcyclohexanols.
The specificity of horse liver alcohol dehydrogenase for cyclohexanol and its 3-methyl derivatives was investigated by stopped-flow and initial velocity kinetic studies. The (1S,3S)-3-methylcyclohexanol was 7 times more reactive (V/Km) than cyclohexanol, whereas the (1R,3R)-3-methylcyclohexanol was at least 1000 times less reactive than its enantiomer. Computer simulation of the transient reaction of NAD+ and the cyclohexanols catalyzed by the enzyme suggests that the rate of transfer of hydrogen from the alcohol to NAD+ is increased with the 1S,3S isomer. Modeling of the three-dimensional structure of the ternary complex of the enzyme suggests that the 1S,3S isomer should only bind in a productive, reactive mode, whereas the 1R,3R isomer would bind predominantly in a nonproductive, inhibitory mode.
Alcohol Dehydrogenase↗
Assessment of the toxicity of cyclohexanone administered intravenously to Wistar and Gunn rats.
The toxicity of cyclohexanone, used as a solvent cement in polyvinyl chloride medical devices, was assessed in Wistar and Gunn rats. The Gunn rat was used because it has a negligible activity of UDP glucuronosyltransferase toward bilirubin and certain other aglycones. Cyclohexanone was administered iv for 28 consecutive days to Wistar and Gunn rats in two doses (50 and 100 mg/kg), using solutions containing 0.25 and 0.50 g per 100 ml, respectively, at a constant volume of 20 mg/kg. Saline (0.9% NaCl) was used as the control. Daily observations for signs of toxicity showed no adverse effects in Wistar or Gunn rats injected with either dose. Daily weight changes of control and test animals were similar. Ophthalmologic examinations revealed no treatment-related structural lesions. No adverse effects were noted when the data from the hemogram or clinical chemistry parameters were evaluated. Gross pathological and histopathologic assessment showed no alterations due to cyclohexanone treatment. Urinary excretions of total and glucuronide conjugates of cyclohexanol were similar for Wistar and Gunn rats; less than 1% was excreted as free cyclohexanone and cyclohexanol. It is concluded that the Gunn rat is capable of forming glucuronides of cyclohexanol and that cyclohexanone at these doses has a negligible toxic potential.
Animals↗
Disposition of acetone, methyl ethyl ketone and cyclohexanone in acute poisoning.
A case of coma due to the drinking of a liquid cement for polyvinyl chloride resin, containing acetone, methyl ethyl ketone, cyclohexanone and polyvinyl chloride is described. The patient also simultaneously ingested the alcoholic beverage, sake. After gastric lavage, plasma exchanges and direct hemoperfusions, the patient recovered. The concentrations of these chemicals in plasma and urine were analyzed at various time intervals to estimate the clearance. The elimination half lives for acetone and methyl ethyl ketone were 18 hours and 10 hours, respectively. Although cyclohexanone made up the largest component in the solvents, the blood level was extremely low and a large amount of cyclohexanol, a metabolite of cyclohexanone was detected in the blood and urine. The glucuronide metabolite of cyclohexanol was also estimated after the hydrolysis with beta-glucuronidase. Since the conversion of cyclohexanone to cyclohexanol is known to be catalyzed by alcohol dehydrogenase, possible interactions between sake ingestion and cyclohexanone metabolism is proposed.
Acetone↗
Biotransformation of hexapropymate in man. Part 2: Isolation and identification of metabolites.
This paper deals with the isolation and identification of hexapropymate metabolites in man. This hypnotic drug is hydroxylated on different positions of the cyclohexane nucleus as was shown by IR, 1H-NMR and MS data of the isolated metabolites and their hydrolysis products. For the determination of the position and conformation of the metabolically introduced hydroxyl group, it was necessary to synthesize different reference compounds [12] and compare their physico-chemical data with those of the isolated metabolites. In this way the following phase-I-metabolites could be identified: 4a-hydroxy-1-(2'propynyl)cyclohexanol-1-carbamate (4a-hydroxyhexapropymate), 4e-hydroxy-1-(2'propynyl)cyclohexanol-1-carbamate (4e-hydroxyhexapropymate) and 3e-hydroxy-1-(2'propynyl)cyclohexanol-1-carbamate. The first two metabolites are also partially excreted in the form of glucuronides.
Biotransformation↗
Menthol blocks dihydropyridine-insensitive Ca2+ channels and induces neurite outgrowth in human neuroblastoma cells.
Voltage-gated Ca2+ channels were identified in LA-N-5 human neuroblastoma cells using the Ca2+ sensitive fluorescent probe, fura-2. Using a variety of "classical" Ca2+ channel blockers, we have demonstrated the presence of both dihydropyridine (DHP)-sensitive and -insensitive channel types that can be activated by depolarization of the cells with either high K+ or gramicidin in the bathing solution. Brief exposure of LA-N-5 cells to menthol blunted the depolarization-induced Ca2+ influx though both DHP-sensitive and DHP-insensitive channels. This effect is concentration dependent (50% maximal blocking effect with 0.25 mM menthol), rapid in onset, and readily reversible. The specificity of the Ca2(+)-channel blocking effect of menthol was demonstrated in parallel studies using compounds with similar structures: menthone blocked Ca2+ channels with about half the potency of menthol, while cyclohexanol was without effect. Addition of either menthol or menthone to LA-N-5 cultures induced neurite outgrowth, cellular clustering, and reduction of cell growth in a dose-dependent fashion that correlated with the ability of these compounds to inhibit the DHP-insensitive Ca2+ influx. Cyclohexanol had no biologic activity. Taken together, the parallel potency for blockade of DHP-insensitive Ca2+ influx with the biologic activity of menthol suggests a role for certain types of Ca2+ channels in triggering growth and morphologic changes in LA-N-5 cells.
Acetylcholinesterase↗
NAD+-dependent ethanol oxidation: redox effects and rate limitation.
Effects of ethanol on interconversion of cyclohexanol and cyclohexanone was studied in isolated hepatocytes. Oxidation and reduction catalyzed by alcohol dehydrogenase were markedly inhibited and stimulated, respectively. The changed ratio between the rates indicated that the ratio of NAD+ to NADH bound to alcohol dehydrogenase decreased several hundred times. This is much more than for the NAD+ system used by, e.g., lactate dehydrogenase, and deuterium from [1,1-2H2] ethanol was incorporated in cyclohexanol much more than in, e.g., lactate. These results indicate that the coenzyme bound to alcohol dehydrogenase is not equilibrated with free coenzyme. Thus, the dissociation of NADH might be rate-limiting for ethanol oxidation. Deuterium transfer from chiral [1-2H] ethanols and [2-2H] glycerol in hepatocytes indicated that cytosolic malate dehydrogenase and lactate dehydrogenase were not completely equilibrated, whereas there was no difference in the utilization of NADH formed at alcohol dehydrogenase and at glycerol-3-phosphate dehydrogenase. Fluxes in redox reactions during ethanol oxidation may be too high for equilibration of cytosolic dehydrogenases.
Animals↗
Secondary 15N isotope effects on the reactions catalyzed by alcohol and formate dehydrogenases.
Secondary 15N isotope effects at the N-1 position of 3-acetylpyridine adenine dinucleotide have been determined, by using the internal competition technique, for horse liver alcohol dehydrogenase (LADH) with cyclohexanol as a substrate and yeast formate dehydrogenase (FDH) with formate as a substrate. On the basis of less precise previous measurements of these 15N isotope effects, the nicotinamide ring of NAD has been suggested to adopt a boat conformation with carbonium ion character at C-4 during hydride transfer [Cook, P. F., Oppenheimer, N. J. & Cleland, W. W. (1981) Biochemistry 20, 1817]. If this mechanism were valid, as N-1 becomes pyramidal an 15N isotope effect of up to 2-3% would be observed. In the present study the equilibrium 15N isotope effect for the reaction catalyzed by LADH was measured as 1.0042 +/- 0.0007. The kinetic 15N isotope effect for LADH catalysis was 0.9989 +/- 0.0006 for cyclohexanol oxidation and 0.997 +/- 0.002 for cyclohexanone reduction. The kinetic 15N isotope effect for FDH catalysis was 1.004 +/- 0.001. These values suggest that a significant 15N kinetic isotope effect is not associated with hydride transfer for LADH and FDH. Thus, in contrast with the deformation mechanism previously postulated, the pyridine ring of the nucleotide apparently remains planar during these dehydrogenase reactions.
Alcohol Dehydrogenase↗
Mechanistic deductions from isotope effects in multireactant enzyme mechanisms.
In the enzymatic mechanism with two or more substrates, comparison of the isotope effects on the maximum velocity and on the apparent V/K values when each substrate concentration is varied allows one to deduce the kinetic mechanism and obtain quantitative information on the relative rates at which substrates dissociate from the enzyme, as opposed to undergoing reaction to give products. Theory is also presented for using the effects of other reactants on the apparent isotope effects determined by the equilibrium perturbation method to determine the same information. With liver alochol dehydrogenase, DPN is not released at an appreciable rate from the E-DPN-cyclohexanol complex, while cyclohexanol is released much more rapidly than it reacts to give products, so that the mechanism appears ordered. With DPNH and cyclohexanone, however, the reaction is random since DPNH can be released from the ternary complex at a finite rate. With yeast alcohol dehydrogenase, acetone, when present, prevents DPNH release from the enzyme so that the mechanism at equal rates from E-DPN-2-propanol so tht the reaction is random in this direction.
Alcohol Oxidoreductases↗
Investigation of the arylnitroso reductase activity of pig liver aldehyde reductase.
The reduction of p-nitroso-N-dimethylaniline, p-nitroso-N-diethylaniline, p-nitrosophenol and p-nitroso-N-phenylaniline with NADPH in the presence of aldehyde reductases 1 and 2 is described. The reactivity of these nitroso substrates is increased by hydrophobic substituents and those promoting OH- elimination from the molecule of the reduced substrate. NN-Dimethylbenzoquinonedi-iminium cation was proved to be the reaction product formed from p-nitroso-N-dimethylaniline. The kinetics of the reduction of p-nitroso-N-dimethylaniline catalysed with aldehyde reductase 1 are rather complex at pH 7, and the preferred-pathway mechanism is probably involved. The reaction sequence approaches the ordered pattern at pH 8.5. It was shown that NADPH in equilibrium NADP+ recyclization proceeds in the presence of NADP+, p-nitroso-N-dimethylaniline, cyclohexanol and aldehyde reductase 1, the alcohol oxidation being the slowest step in this reaction. However, the rate of cyclohexanol oxidation surpasses that of the dissociation of NADPH from the enzyme.
Alcohol Oxidoreductases↗
Effect of ethanol on the redox state of the coenzyme bound to alcohol dehydrogenase studied in isolated hepatocytes.
Hepatocytes were isolated from fed female rats and incubated with a redox indicator system consisting of cyclohexanone and unlabelled or perdeuterated cyclohexanol. The concentrations and deuterium contents of these were measured by g.l.c. and g.l.c.-m.s. of oxime t-butyldimethylsilyl derivatives. The equilibrium composition represented the redox state of the coenzyme bound to alcohol dehydrogenase, since 4-methylpyrazole inhibited the interconversion. Reduction appeared to be catalysed to a small extent also by an NADPH-dependent aldehyde reductase. The NADH/NAD+ ratio on alcohol dehydrogenase was 3 orders of magnitude higher in the presence of ethanol than in its absence. This redox shift has the degree expected from reported kinetic constants. The shift was due both to a decreased rate of oxidation and to an increased rate of reduction in the indicator system. The results indicate that the redox effect of ethanol on the free NAD system is due to efficient removal of acetaldehyde from a near-equilibrium system consisting of ethanol, acetaldehyde and bound coenzymes, together with dissociation of NADH from the enzyme. The effect on the redox state of the bound coenzyme was less marked when the ethanol was deuterated at C-1, indicating an isotope effect. The 2H excess in the cyclohexanol formed was about 70% of that in the [1,1-2H2]ethanol. This dilution, which is caused by binding of free NADH to the enzyme, indicates that reoxidation of cytosolic NADH partly limits the rate of ethanol oxidation.
Alcohol Dehydrogenase↗