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PubMed1983

Potentiation of ethanol toxicity by cyanamide in relation to acetaldehyde accumulation.

The possibility that acetaldehyde accumulation potentiates the acute toxicity of ethanol was studied by pretreating rats with cyanamide, an aldehyde dehydrogenase inhibitor. At 30 min after administration of ethanol (7 to 9 g/kg, po), the levels of acetaldehyde in femoral venous blood of cyanamide-treated rats were increased from 10 to 20 to 600 mumol/liter and at death the concentrations of acetaldehyde in heart blood and cerebrospinal fluid were still 7 to 9 and 4 to 9 times higher, respectively, than in rats given ethanol only. The cyanamide pretreatment (25 mg/kg) significantly increased the mortality of rats given 6.5 to 7.0 g/kg ethanol and decreased the LD50 of ethanol from 7.3 to 5.9 g/kg. Cyanamide increased the late mortality, possibly because of sustained acetaldehyde accumulation. Although administration of the alcohol dehydrogenase inhibitor, 4-methylpyrazole (4-MP, 10 mg/kg), prevented the accumulation of acetaldehyde, it only partly counteracted the effect of cyanamide on mortality. After coadministration of cyanamide and 4-MP, the LD50 of ethanol was 6.5 g/kg, and after 4-MP alone, 6.7 g/kg. 4-MP by itself seemed to increase the early mortality of rats to ethanol poisoning. The results suggest that the potentiating effect of cyanamide on ethanol toxicity can partly be explained by acetaldehyde accumulation and that 4-MP can be used to inhibit this accumulation providing its central depressant effect is taken into account.

Acetaldehyde↗
PubMed2006

Evidence of cyanamide production in hairy vetch Vicia villosa.

Cyanamide (NH(2)CN) has recently been isolated as a plant growth inhibitor from Vicia villosa, which is the first discovery of cyanamide from natural sources. To reveal the presence of the biosynthesized cyanamide in plants, 3.4 mM potassium ((15)N)nitrate was administered to 15- to 35-day-old plants of V. villosa, from which the cyanamide was purified and subjected to GC/MS analysis. The isotopic ratio (15)N/((14)N + (15)N) of the cyanamide was calculated to be 0.143, while that of the cyanamide extracted from V. villosa grown in the presence of a natural N source was 0.0065. The (15)N-enrichment proved de novo biosynthesis of cyanamide.

Cyanamide↗
PubMedDate not supplied

Comparison of cyanamide and placebo in the treatment of alcohol dependence of adolescents.

AIMS: About 50% of alcoholic patients relapse within 3 months of treatment. Previous studies have suggested that cyanamide may help to prevent such relapse. The aim of our study was to assess the efficacy and safety of long-term cyanamide treatment in alcohol dependence of adolescents. METHODS: In this, double-blind, placebo-controlled study, we recruited 26 patients, aged 16-19 years, with chronic (frequent and regular) or episodic (frequent, but irregular) alcohol dependence. Patients were randomly allocated treatment with cyanamide (200 mg daily) or a placebo for 90 days. Patients were assessed on the day the treatment was started, and on days 30 and 90, by interview, self-report, questionnaire and laboratory screening. Patients were classified as abstinent, relapsing or non-attending. Time to first treatment failure (relapse or non-attendance) was the primary outcome measure. RESULTS: The cyanamide (n = 13) and placebo (n = 13) groups were well matched in terms of baseline demographic and alcohol-related variables. Mean cumulative abstinence duration was significantly greater in the cyanamide group than in the placebo group. Apart from occasional diarrhoea, there was no difference in side effects between groups. CONCLUSIONS: Cyanamide seems to be an effective and well tolerated pharmacological adjunct to psychosocial and behavioural treatment programmes for the treatment of some adolescent alcohol-dependent patients. Because of reported hepatotoxic, haematological and dermatological side effects, patients should be observed continuously by experienced clinicians. Further studies are necessary to prove the efficacy of cyanamide in adolescents.

Adolescent↗
PubMedDate not supplied

N-acetylcyanamide, the major urinary metabolite of cyanamide in rat, rabbit, dog, and man.

The structure of the major urinary metabolite of cyanamide, the active component of the alcohol deterrent agents Temposil , Dipsan , and Abstem , in rats, rabbits, and dogs has been established as N- acetylcyanamide by its identity with chemically synthesized N- acetylcyanamide , and by conversion of the metabolite and the synthetic product to identical derivatives, viz. to N-benzyl-N- acetylcyanamide and to N-(p-nitrobenzyl)-N- acetylcyanamide . The latter derivatives were analyzed by pulsed positive/negative ion chemical ionization mass spectroscopy. Urine from patients receiving cyanamide as a treatment mode was shown to contain N- acetylcyanamide by chemical ionization mass spectrometric analysis of the isolated p-nitrobenzyl derivative, thereby establishing that N- acetylcyanamide is also a metabolite in man. The major portion (87%) of the first 27-hr urinary radioactivity excreted by the dog after receiving a low dose of [14C]cyanamide (0.04 mmol/kg, po) was N- acetylcyanamide , as determined by inverse isotope dilution and measurement of the specific radioactivity of its N-p-nitrobenzyl derivative. This indicates that at low doses acetylation is also a major route of biotransformation of cyanamide in the dog. Hepatic N-acetyltransferase, isolated from the rabbit and dog, catalyzed the transfer of the acetyl group from acetyl-S-CoA to [14C]cyanamide producing N-acetyl[14C]cyanamide. The enzyme isolated from the liver of a rapid acetylator phenotype rabbit was twice as effective as the dog enzyme in catalyzing this transfer. Thus, the enzyme responsible for this biotransformation of cyanamide is an acetyl-S-CoA-dependent N-acetyltransferase.

Acetylation↗
PubMed1996

Noncompetitive-like inhibition of ethanol elimination by cyanamide treatment: pharmacokinetic study.

The effect of acetaldehyde accumulation of ethanol elimination is of interest in medico-legal practice in Japan. We examined the pharmacokinetic mechanism of the inhibition of ethanol metabolism by cyanamide, an inhibitor of mitochondrial aldehyde dehydrogenase. An ethanol solution (0.25-2.0 g/kg body weight) was injected intravenously into male rabbits with or without administration of cyanamide. Cyanamide was injected intraperitoneally (25 mg/kg body weight) to the cyanamide-treated group 2 hr before ethanol injection. Blood ethanol and acetaldehyde concentrations were measured periodically by head-space gas chromatography. The MULTI(RUNGE) computer program was applied for the pharmacokinetic analysis. One- or two-compartment open models with Michaelis-Menten elimination kinetics were used for simultaneous multi-line fitting. The ethanol elimination rate decreased by cyanamide treatment. The border-point concentration between pseudolinear and curvilinear phases was not affected by cyanamide treatment. The estimated Vmax value decreased by cyanamide treatment, whereas the K(m) value did not change. Our results correspond to a noncompetitive-like inhibition of ethanol metabolism. K(m) is related to the border point between pseudolinear and curvilinear phases. Thus, our findings in the blood ethanol concentration-time curve suggest adequate curve-fitting. The product, or competitive, inhibition of alcohol dehydrogenase by acetaldehyde had been reported in enzymological study. The pharmacokinetic manner of inhibition in vivo was different from the enzymologic mechanism in vitro. Other metabolic factors related to ethanol metabolism are thought to be more important than acetaldehyde accumulation itself.

Acetaldehyde↗
PubMed1976

[The influence of straw, particularly rice straw, together with calcium-cyanamide on the microbiological activity of two Portuguese soils (author's transl)].

The influence of calcium-cyanamide upon the microbiological activity was tested in pot experiments under controlled conditions in two Portuguese soils (sandy and loamy) after the addition of rice or wheat straw (rice straw 0.275% N, wheat straw 0.307% N). The amount of straw was equalled to 100 dz/ha, the application of calcium-cyanamide to 25, 50 and 100 kg N/ha. In the containers treated with straw the total amount of microorganisms (Koch-method) was higher in sandy than in loamy soil after 30 days, but after 70 days it was higher in loamy soil. The content of active nitrogen (NH4 + NO3) increased, when calcium-cyanamide was added, but decreased after the application of straw. After 70 days sandy soil again showed an increase of active nitrogen. Straw increased the rates of CO2-production considerably, wheat straw was superior to rice straw. Calcium-cyanamide increased the CO2-production more in sandy than in loamy soil or German loess, which was also used for this experiment. Only in the case of rice straw higher doses of calcium-cyanamide had a positive effect. After 70 days the CO2-production rose only when rice straw was applied. The dehydrogenase-activity was increased in both soils, but a superiority of wheat straw occurred in sandy soil only. The microbiological activity in the pots with straw was higher in sandy than in loamy soil, the addition of calcium-cyanamide accelerated it. Doses of 25-50 kg N/ha are sufficient generally. The period of the formation of insoluble organic N-compounds, usually connected with the application of organic matter with a wide N:C-ratio, seems to be reduced by the addition of calcium-cyanamide.

Actinomycetales↗
PubMed1993

Inhibition of rat hepatic mitochondrial aldehyde dehydrogenase isozymes by repeated cyanamide administration: pharmacokinetic-pharmacodynamic relationships.

The inhibition of rat hepatic mitochondrial aldehyde dehydrogenase (ALDH) isozymes was studied in apparent steady-state conditions after repeated intra-peritoneal cyanamide administration. The low-Km mitochondrial ALDH isozyme was more susceptible to cyanamide-induced inhibition (DI50 = 0.104 mg kg-1) than the high-Km isozyme (DI50 = 8.52 mg kg-1), with almost complete inhibition occurring at 0.35 mg kg-1 total cyanamide administered for the low-Km isozyme. The relationships between plasma and liver cyanamide concentrations and the inhibition of high-Km ALDH were established by means of the sigmoid Imax model. The effect of dosing rate on the plasma concentration of cyanamide at apparent steady-state showed non-linearity, indicating that clearance or first-pass metabolism of cyanamide during its absorption after intraperitoneal administration did not remain constant throughout the range of doses studied.

Aldehyde Dehydrogenase↗
PubMed1981

Cyanamide mediated syntheses of peptides containing histidine and hydrophobic amino acids.

Using the model of a primitive earth evaporation pond, the synthesis of three histidyl peptides in yields up to 11% was demonstrated when aqueous solutions of histidine, leucine, ATP, cyanamide, and MgCl2 were evaporated and heated for 24 h at 80 degrees C. In addition, peptides were formed in yields of up to 56%, 35%, and 21%, respectively for phenylalanine, leucine, and alanine when aqueous solutions of the appropriate amino acid were evaporated and heated with cyanamide and one or more of the following components: ATP, AMP, 4-amino-5-imidazole carboxamide, or MgCl2. The greatest peptide yield occurred at pH 3. But peptide formation was demonstrated for a system of Leu, cyanamide, and MgCl2 adjusted to pH 7 with NH4OH. Peptide synthesis was also studied in the presence of CaCl2, ZnCl2, different adenosine nucleotides, and UTP to compare their effects on peptide synthesis. The optimum conditions for cyanamide mediated peptide synthesis were also studied in terms of pH, reaction time, reaction temperature, and cyanamide concentration. The major side product in nearly all reactions studied appears to be an amino acid-cyanamide adduct. Peptides were analyzed and identified by thin layer chromatography, acid hydrolysis, and enzymatic degradation.

Amino Acids↗
PubMed1999

Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?

The interaction of human carbonic anhydrase (hCA) isozymes I and II with cyanamide, a linear molecule isoelectronic with the main physiological substrate of the enzyme, CO(2), was investigated through spectroscopic, kinetic, and X-ray crystallographic studies. We show here that cyanamide is hydrated to urea in the presence of CAs, and that it also acts as a weak non-competitive inhibitor (K(I)=61+/-3 mM and 238+/-9 mM for hCA II and hCA I, respectively) towards the esterasic activity of these enzymes, as tested with 4-nitrophenyl acetate. Changes in the spectrum of the Co(II)-hCA II derivative observed in the presence of cyanamide suggest that it likely binds the metal ion within the CA active site, adding to the coordination sphere, not substituting the metal-bound solvent molecule. It thereafter undergoes a nucleophilic attack from the metal-bound hydroxide ion, forming urea which remains bound to the metal, as observed in the X-ray crystal structure of hCA II soaked in cyanamide solutions for several hours. The urea molecule is directly coordinated to the active site Zn(II) ion through a protonated nitrogen atom. Several hydrogen bonds involving active site residues Thr199 and Thr200 as well as three water molecules (Wat99, Wat122, and Wat123) further stabilize the urea-hCA II adduct. Kinetic studies in solution further proved that urea acts as a tight binding inhibitor of the two isozymes hCA I and hCA II, with very slow binding kinetics (k(on) = 2.5 x 10(-5)s(-1)M(-1)). A mechanism to explain the hydration process of cyanamide by CAs, as well as the tight binding of urea in the active site, is also proposed based on the hypothesis that urea is deprotonated when bound to the enzyme. Cyanamide is thus the first true suicide substrate of this enzyme for which binding has been documented by means of X-ray crystallographic and spectroscopic studies.

Carbonic Anhydrases↗
PubMed1986

Differential inhibition of rat tissue catalase by cyanamide.

The relative sensitivity of rat tissue catalase to inhibition by intraperitoneally administered cyanamide was liver greater than kidney greater than heart greater than brain, whereas the activity of the erythrocyte enzyme was affected minimally. The measured ED50 values for cyanamide in these tissues were 31, 44, 107 and 680 mumoles/kg body weight for liver, kidney, heart and brain respectively. On a molar basis, cyanamide was approximately twenty times more potent than 3-amino-1,2,4-triazole (3-AT) in inhibiting hepatic catalase in vivo in the rat. Like 3-AT, cyanamide inhibited erythrocyte catalase activity in vitro in the presence of hydrogen peroxide. The apparent similarities between the inhibition of hepatic catalase by cyanamide and 3-AT in vivo suggest that cyanamide belongs to the family of 3-AT-like catalase inhibitors.

Amitrole↗
PubMed1986

Effects of cyanamide on body weight and brain monoamines and metabolites in rats.

Cyanamide, a disulfiram-like drug used in the treatment of alcoholism, decreased in a dose-dependent manner (2-25 mg/kg) the body weight gain curve in rats, which resulted in a marked decrease of body weight (10-35%). Long-term administration of cyanamide also decreased food intake (6-34%) in a dose-dependent manner (2-25 mg/kg). Both effects of cyanamide were reversible. After the acute and long-term administration (1-12 months) of cyanamide (8-35 mg/kg) the brain concentration of 3-methoxy-4-hydroxyphenylethyleneglycol sulphate (MOPEG-SO4) was also significantly increased (26-46%). Cyanamide, however, had no effects on the brain concentration of noradrenaline, dopamine, 5-hydroxytryptamine, tryptophan and 5-hydroxyindolacetic acid. It is suggested that the loss of weight, the decrease in food intake and the increase in brain MOPEG-SO4 induced by cyanamide reflect possible anorectic properties of the drug.

Animals↗
PubMed2002

The effect of cyanamide and 4-methylpyrazole on the ethanol-induced locomotor activity in mice.

To assess the role of cyanamide and 4-methylpyrazole (4-MP) in mediating ethanol-induced locomotor activity in mice, they were pretreated with cyanamide (12.5, 25, or 50 g/kg) prior to one ethanol injection (2.4 g/kg) and showed significantly depressed locomotor activity compared with control groups. Cyanamide (25 mg/kg) also cancelled out the biphasic action of ethanol (0, 0.8, 1.6, 2.4, 3.2, or 4 g/kg) on locomotor activity. The action of cyanamide and 4-MP in combined administration was also tested. Our data show that pretreatment with 4-MP alone does not change the spontaneous or ethanol-induced locomotor activity. Conversely, when mice were pretreated with cyanamide and 4-MP, the depressive effect of cyanamide on the locomotor activity induced by ethanol disappeared, and the locomotor activity rose to levels similar to those of the control group, recovering the biphasic ethanol effect. These effects cannot be attributed to peripheral elevated blood acetaldehyde levels, as pretreatment with 4-MP prevents accumulation of acetaldehyde. These data might suggest some influence of brain catalase and aldehyde dehydrogenase (ALDH) on the effects of ethanol.

Animals↗
PubMed1986

Acyl, N-protected alpha-aminoacyl, and peptidyl derivatives as prodrug forms of the alcohol deterrent agent cyanamide.

Cyanamide (H2NC identical to N), a potent aldehyde dehydrogenase (AlDH) inhibitor that is used therapeutically as an alcohol deterrent agent, is known to be rapidly metabolized and excreted in the urine as acetylcyanamide (1). On the basis of our observation that 1 is deacetylated to cyanamide in vivo, albeit very slightly, thereby serving as a precursor of prodrug form of the latter, several acyl derivatives of cyanamide were synthesized specifically as prodrugs, including benzoylcyanamide (2), pivaloylcyanamide (3), and 1-adamantoylcyanamide (4), as well as long- and medium-chain fatty acyl derivatives such as palmitoyl- (6), stearoyl- (7), and n-butyrylcyanamide (5). N-Protected alpha-aminoacyl and peptidyl derivatives of cyanamide were also synthesized, and these include N-carbobenzoxyglycyl- (10), hippuryl- (13), N-benzoyl-L-leucyl- (14), N-carbobenzoxyglycyl-L-leucyl- (18), N-carbobenzoxy-L-pyroglutamyl- (22), L-pyroglutamyl-L-leucyl- (19), and L-pyroglutamyl-L-phenylalanylcyanamide (20). All of these prodrugs of cyanamide raised ethanol-derived blood acetaldehyde levels in rats significantly over controls 3 h after ip drug administration, and some of these were still capable of elevating blood acetaldehyde 16 h post drug administration. A selected group of cyanamide prodrugs were also evaluated by the oral route of administration and showed nearly equivalent activity as the ip route in elevating ethanol-derived blood acetaldehyde. These results suggest potential utility of these prodrugs as deterrent agents for the treatment of alcoholism.

Acylation↗
PubMed2002

Generation of protein adducts with malondialdehyde and acetaldehyde in muscles with predominantly type I or type II fibers in rats exposed to ethanol and the acetaldehyde dehydrogenase inhibitor cyanamide.

BACKGROUND: Alcoholic myopathy is known to primarily affect type II muscle fibers (glycolytic, fast-twitch, anaerobic), whereas type I fibers (oxidative, slow-twitch, aerobic) are relatively protected. OBJECTIVE: We investigated whether aldehyde-derived adducts of proteins with malondialdehyde and acetaldehyde are formed in muscle of rats as a result of acute exposure to ethanol and acetaldehyde. The differences between type I muscle, type II muscle, and liver tissue were also assessed. DESIGN: The formation and distribution of malondialdehyde- and acetaldehyde-protein adducts were studied with immunohistochemistry in soleus (type I) muscle, plantaris (type II) muscle, and liver in 4 groups of rats. The different groups were administered saline (control), cyanamide (an acetaldehyde dehydrogenase inhibitor), ethanol, and cyanamide + ethanol. RESULTS: Treatment of rats with ethanol and cyanamide + ethanol increased the amount of aldehyde-derived protein adducts in both soleus and plantaris muscle. The greatest responses in malondialdehyde-protein and acetaldehyde-protein adducts were observed in plantaris muscle, in which the effect of alcohol was further potentiated by cyanamide pretreatment. Malondialdehyde- and acetaldehyde-protein adducts were also found in liver specimens from rats treated with ethanol and ethanol + cyanamide; the most abundant amounts were found in rats given cyanamide pretreatment. CONCLUSIONS: Acute ethanol administration increases protein adducts with malondialdehyde and acetaldehyde, primarily in type II muscle. This may be associated with the increased susceptibility of anaerobic muscle to alcohol toxicity. Higher acetaldehyde concentrations exacerbate adduct formation, especially in type II-predominant muscles. The present findings are relevant to studies on the pathogenesis of alcohol-induced myopathy.

Acetaldehyde↗
PubMed1995

Cyanamide-associated alcoholic liver disease: a sequential histological evaluation.

This is the first study that we are aware of that followed the histopathological progression of the liver disease that was caused by the combination of both chronic alcohol use and cyanamide, an antidipsotropic agent. Two sequential liver biopsy specimens were obtained on 29 alcoholics who relapsed with varying histories of cyanamide treatment. Cyanamide induced ground-glass inclusions (GGIs) in the hepatocytes. Two groups were identified, depending on whether GGIs proliferated or regressed, which was, in turn, found contingent on the duration of cyanamide treatment and the drug-free period. Group 1 included 14 cases in which GGIs either emerged only in the second biopsy specimen or else were increased in the second specimen as compared in the initial specimen. Group 2 composed of 15 cases in which GGIs were either not observed in either specimen or decreased in the second specimen as compared in the initial specimen. Acidophilic bodies were sequentially increased in five cases (36%) of group 1 and in none of group 2. The severity of portal inflammation worsened in 10 cases (71%) of group 1 but in 2 cases (13%) of group 2, although the changes in fibrotic process did not differ between two groups. These differences could not be explained on the basis of the daily ethanol consumption and the length of relapses of the two groups. Thus, when cyanamide-treated alcoholics relapsed, the combined effect of cyanamide and alcohol produced the development of acidophilic bodies and portal inflammation along with the emergence of GGIs.

Adult↗
PubMed1997

Cyanamide-induced granulocytopenia.

We report a 64-year-old male with granulocytopenia and dermatitis due to cyanamide treatment. We administered cyanamide for alcoholism. After about one month he suffered from scaly erythema over his whole body and granulocytopenia (granulocyte; 140/microliter) with maturation arrest in bone marrow. After cessation of cyanamide and the start of granulocyte colony-stimulating factor administration, the skin eruption ameliorated gradually, and the peripheral blood granulocyte counts increased. Cyanamide showed positive results in the drug lymphocyte stimulation test (198%) and the patch test led to the diagnosis of granulocytopenia and dermatitis induced by cyanamide. After restarting glibenclamide and diazepam administration, his granulocytopenia did not reoccur. To our knowledge, this is the first report of a case with granulocytopenia induced by cyanamide.

Agranulocytosis↗
PubMed2005

Update: hydrogen cyanamide-related illnesses--Italy, 2002-2004.

Hydrogen cyanamide is used in agriculture as a plant growth regulator and is applied to many deciduous plants to stimulate uniform budbreak after dormancy, resulting in uniform flowering and maturity. Hydrogen cyanamide is highly toxic, and adverse health effects from contact include severe irritation and ulceration of the eyes, skin, and respiratory tract. The substance also inhibits aldehyde dehydrogenase and can produce acetaldehyde syndrome (e.g., vomiting, parasympathetic hyperactivity, dyspnea, hypotension, and confusion) when exposure coincides with alcohol use. After Dormex (Degussa AG, Trostberg, Germany), a pesticide product containing hydrogen cyanamide (49% by weight), was introduced in Italy in 2000, a total of 23 cases of acute illness associated with exposure to this chemical were identified in early 2001. This led to a temporary suspension of sales and usage of Dormex on February 23, 2002, and strengthening of protective measures, as specified on the pesticide label when sales were resumed on June 20, 2003. This report describes 28 additional cases of hydrogen cyanamide-related illness that occurred during 2002-2004, 14 of which occurred after sales resumed. These illnesses suggest that the preventive measures adopted in Italy in 2003 to protect workers using hydrogen cyanamide are inadequate. Workers exposed to hydrogen cyanamide should be provided adequate information, training, personal protective equipment (PPE), and engineering controls.

Cyanamide↗
PubMedDate not supplied

Inactivation mechanism of low-KM rat liver mitochondrial aldehyde dehydrogenase by cyanamide in vitro.

The inactivation of low-KM rat liver mitochondrial aldehyde dehydrogenase (ALDH) by the alcohol-sensitizing agent cyanamide (H2NCN) has been studied in vitro. The effect of the concentrations of NAD+ at different concentrations of catalase on the inactivation of ALDH by cyanamide (20 and 200 microM) in vitro point to an ALDH-NAD(+)-catalase complex prior to the binding to cyanamide to form the holoenzyme-inhibitor complex. Cyanamide itself could be responsible for the inactivation of ALDH. The possibility that both irreversibly inactivated ALDH and cyanamide remain free at the end of the inactivation process is discussed. The effects of pH and ionic strength on the inactivation process are also described. The pseudo-first order rate constants for inactivation of low-KM ALDH depends on both effects, suggesting that electrostatic forces are involved in the process and that a group with pK approximately 6.8, presumably a histidine residue, at the active site of ALDH could be involved. A representative equation for the inactivation process of low-KM ALDH by cyanamide in vitro has been fitted to experimental kinetic data, involving both catalase and inhibitor concentrations.

Aldehyde Dehydrogenase↗