Inhibition of plant and mammalian diamine oxidases by hydrazine and guanidine compounds

Biegański, Tadeusz; Osinska, Z.; Maśliński, Cz.

doi:10.1016/0020-711x(82)90080-5

Cited by 14 publications

(7 citation statements)

References 28 publications

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“…This will in the future probably lead to more precise information about the interaction between AMG and DAO. The concentration of AMG needed to accomplish 50% inhibition of pig kidney enzyme activity was reported by Bieganski et al [21] to be 38 nM which corresponds well to values reported from other tissues and species [19,[22][23][24].…”

Section: Inhibition Of Diamine Oxidasesupporting

confidence: 66%

Biological effects of aminoguanidine: An update

Nilsson¹

1999

Inflammation Research

193

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Aminoguanidine (AMG) was prepared more than 100 years ago. During the last 10 years two important effects of AMG have been discovered which have made this molecule attract a lot of interest. Firstly, AMG inhibits, in vitro and in vivo, formation of highly reactive advanced glycosylation end products (AGEs) associated with pathogenesis of secondary complications to diabetes and with cardiovascular changes in aging. AMG ameliorates various complications to diabetes and prevents age related arterial stiffening and cardiac hypertrophy, effects probably dependent on inhibition of AGEs formation. Secondly, AMG inhibits NO synthase particularly the inducible NO synthase isoform making AMG an important pharmacological tool. The inducible NO synthase isoform is associated with production of large quantities of NO synthase in response to e. g. cytokines. When these effects of AMG were disclosed it had already been known for many years that AMG, in nM concentrations, inhibits diamine oxidase. This enzyme catalyzes degradation of biologically active diamines such as histamine and putrescine. Data obtained from studies using AMG should be interpreted with precaution since this substance interferes with several important regulatory systems. In this review these important targets for AMG are addressed.

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Section: Inhibition Of Diamine Oxidasesupporting

confidence: 66%

Biological effects of aminoguanidine: An update

Nilsson¹

1999

Inflammation Research

193

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“…Since it is known that inhibition of diamine oxidase by guanidines is progressive with time [1,17], a standard incubation period of 3 min was adopted prior to the addition of substrates. However, for the polyamine oxidase pre-incubation for up to 1 h in the presence of arcaine gave the same degree of inhibition, and in a similar experiment with diamine oxidase, inhibition was unchanged for up to 15 min.…”

Section: Enzymes and Substratesmentioning

confidence: 99%

The inhibition and activation of polyamine oxidase from oat seedlings

Smith

1985

Plant Growth Regul

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In a homologous series of di-guanidines (NH2C(= NH)NH(CH2)xNHC(= NH) NH2) where x = 2-12, greatest inhibition of polyamine oxidase was found with x : 8. The synthetic fungicide guazatine NH2C(= NH)NH --(CH ~)s,....~ N H NH2C(= NH)NH --(CH2)8 /was particularly effective as an inhibitor of polyamine oxidase, with Ki of ca 10-~ M. Inhibition due to the tri-amine derived from guazatine by hydrolysis was less effective by a factor of ca 200. Comparison of various inorganic salts at I Mshowed that polyamine oxidase activity was enhanced in the order RbC1 > KCI > KBr > NH,CI > NaNO 3 > LiCI = NaC1 > control (no salt) > CaC12 = MgCI~. Activity in RbC1 was about 4 to 5 times greater than in the salt-free control. Enzyme activity is rapidly lost during assay. This loss of activity could not be attributed to inhibition by aminopropylpyrroline or diaminopropane. Moreover the superoxide scavenger copper salicylate had no protective effect on enzyme activity.

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“…Elevated histamine levels in the CSF of MS patients have also been reported by MOLN.~.R and MOLDAV. ~N (1966) [6], but the comparison is hampered by different assay methods.…”

Section: Discussionmentioning

confidence: 99%

“…Using radioactive cadaverine as substrate for diamine oxidase measurement of the amount of ~4C-Al-piperideine formed was a procedure devised for estP mating diamine oxidase levels [6]. However, following injection of cadaverine to rats fi aminovaleric acid was found in the urine [7][8], indicating that cadaverine underwent metabolic degradation through two oxidative reactions, the first reaction leading to the formation of 6-aminovaleraldehyde and the second giving rise to the corresponding amino acid.…”

Section: Introductionmentioning

confidence: 99%

Diamine oxidase in the hen

Biegański

1983

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In adult hens diamine oxidase (histaminase) activity was found in gastrointestinal tract (with the highest value in ileum), liver and spleen. Intestinal diamine oxidase is predominantly a particle-bound enzyme. In the intestine oxidation of putrescine leads to delta 1-pyrroline formation, in liver both delta 1-pyrroline and gamma-aminobutyric acid are formed. The inhibitor properties of hen intestinal and rat intestinal diamine oxidases are very similar and differ from pea seedling diamine oxidase. The natural dipeptides carnosine and anserine are relatively potent inhibitors of hen intestinal diamine oxidase.

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Inhibition of plant and mammalian diamine oxidases by hydrazine and guanidine compounds

Cited by 14 publications

References 28 publications

Biological effects of aminoguanidine: An update

Biological effects of aminoguanidine: An update

The inhibition and activation of polyamine oxidase from oat seedlings

Diamine oxidase in the hen

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