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Histamine — Pyridine Coenzyme Interactions

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Histamine and Anti-Histaminics

Abstract

Certain enzyme catalyzed interactions of histamine with either diphosphopyridine nucleotide (coenzyme I, abbreviated DPN+) (Alivisatos, 1958a, b; Alivisatos et al., 1960) or triphosphopyridine nucleotide (coenzyme II, abbreviated TPN+) (Alivisatos and Abdel-Latif, 1960; Abdel-Latif and Alivisatos, 1961 a) lead to displacement products in which the nicotinamide moiety of pyridine coenzymes is irreversibly replaced by histamine.

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References

  • Abdel-Latif, A. A., and S. G. A. Alivisatos: Imidazolytic processes. IV. Enzymic formation of triphosphohistamine nucleotide. J. biol. Chem. 236, 2710 (1961a).

    PubMed  CAS  Google Scholar 

  • Abdel-Latif, A. A., and S. G. A. Alivisatos: Alternative pathways of enzymic formation of ribotides and ribosides of histamine. Biochim. biophys. Acta (Amst.) 51, 398 (1961b).

    Article  CAS  Google Scholar 

  • Abdel-Latif, A. A., and S. G. A. Alivisatos: Purification and properties of pyridine nucleosidase (Glycosidase) from bull semen. J. biol. Chem. 237, 500 (1962).

    PubMed  CAS  Google Scholar 

  • Alechinsky, A.: Nicotinamide et choc histaminique. C. R. Soc. Biol. (Paris) 141, 524 (1947).

    CAS  Google Scholar 

  • Alivisatos, S. G. A.: Formation of histamine containing dinucleotides by enzymatic interaction of histamine and coenzyme I. Nature (Lond.) 181, 271 (1958a).

    Article  CAS  Google Scholar 

  • Alechinsky, A.: Enzymatic interaction of histamine and coenzyme I with formation of a new dinucleotide. Fed. Proc. 17, 180 (1958b).

    Google Scholar 

  • Alechinsky, A.: The mechanism of action of diphosphopyridine nucleotidases. Nature (Lond.) 183, 1034 (1959).

    Article  Google Scholar 

  • Alechinsky, A.: Mechanism of the gastric secretion of hydrogen ions. Nature (Lond.) 186, 368 (1960).

    Article  Google Scholar 

  • Alechinsky, A.: Histamine-Pyridine Coenzyme Interactions. In a Symposium of the Histamine Club, Chicago, April 1964. Edited by G. Ungar. Fed. Proc. In Press.

    Google Scholar 

  • Alechinsky, A., and A. A. Abdel-Latif: Enzymic interaction of Tpn with histamine. Proc. 138th Nat. Meet. Amer. Chem. Soc., p. 26c (1960).

    Google Scholar 

  • Alechinsky, A., and A. A. Abdel-Latif: unpublished observations.

    Google Scholar 

  • Alechinsky, A., and A. A. Abdel-Latif, F. Ungar, and G. A. Mourkides: In vivo degradation of histamine-adenine dinucleotide phosphate to histamine ribonucleoside. Nature 199, 907 (1963).

    Article  Google Scholar 

  • Alechinsky, A., and O. F. Denstedt: Lactic dehydrogenase and Dpnase activity of blood. Science 114. 281 (1951).

    Article  Google Scholar 

  • Alechinsky, A., and L. Lamantia: Resistance to acid hydrolysis of N-ribosyl derivatives of various substituted imidazoles and pyrimidine imidazoles (purines). Biochem. biophys. Res. Commun. 2, 164 (1960).

    Google Scholar 

  • Alechinsky, A., and L. Lamantia, and B. Matijevitcn: Imidazolytic processes. V. Enzymically catalyzed reactivity of certain imidazoles with coenzyme I. Biochim. biophys. Acta (Amst). 58, 201 (1962).

    Google Scholar 

  • Alechinsky, A., and L. Lamantia, F. Ungar, and B. Savich: Enzymic formation of inosinic-adenylic pyrophosphate. Biochim. biophys. Acta (Amst.) 30, 660 (1958).

    Article  Google Scholar 

  • Alechinsky, A., and L. Lamantia, In: J. H. Shaffer, G. A. Logrirpo, and M. W. Chase: (Editors), “Mechanisms of Hypersensitivity”, p. 259. Boston: Little, Brown and Co. 1959.

    Google Scholar 

  • Alechinsky, A., and L. Lamantia, A. Jibril, and G. A. Mourkides: Non-enzymic reactions of indoles with pyridine coenzymes and related structures. Biochim. biophys. Acta (Amst.) 51, 361 (1961).

    Article  Google Scholar 

  • Alechinsky, A., F. Ungar, O. Callaghan, and C. Biava: Effect of indoles and imidazoles, including serotonin and histamine, on the morphology and oxidative phosphorylation of guinea pig liver mitochondria. Nature 201, 47 (1964).

    Article  Google Scholar 

  • Alechinsky, A., F. Ungar, and L. Lukacs: On the mechanism of biologic histaminic reactions, p. 387. Vth International Congress of Biochemistry, Moscow, August 1961 b. London: Pergamon Press 1961.

    Google Scholar 

  • Alechinsky, A., F. Ungar, and L. Lukacs, and L. Lamantia: Imidazolytic processes. Iii. Enzymic conversion of coenzyme I to histamine dinucleotide. J. biol. Chem. 235, 1742 (1960).

    Google Scholar 

  • Alechinsky, A., and H. G. Williams-Ashman: Serotonin-mediated oxidation of dihydronico-tinamide derivatives by cytochrome c. Biochim. biophys. Acta (Amst.) 86, 392 (1964).

    Article  Google Scholar 

  • Alechinsky, A., and D. W. Woolley: Solubilization and purification of the diphosphopyridine nucleotidase from beef spleen. J. biol. Chem. 219, 823 (1956).

    Google Scholar 

  • Butturini, U.: Sull’azione antiistamica ed antiallergica dell’amide nicotinica; ricerche cliniche e sperimentali. G. Clin. med. 27, 681 (1946).

    CAS  Google Scholar 

  • Crowley, G. M.: Enzymatic synthesis of imidazoleacetic acid ribotide. Fed. Proc. 19, 309 (1960).

    Google Scholar 

  • Dainow, I.: Recherches cliniques sur certaines propriétés anti-allergiques de la nicotinamide. Z. Vitaminforsch. 15, 245 (1944).

    Google Scholar 

  • Estabrook, R. W., J. Gonze, and S. P. Nissley: A possible role for pyridine nucleotide in coupling mechanism of oxidative phosphorylation. Fed. Proc. 22, 1071 (1963).

    PubMed  CAS  Google Scholar 

  • Eys, J. Van: The reaction of quarternary pyridine derivatives with imidazoles. J. biol. Chem. 233, 1203 (1958).

    CAS  Google Scholar 

  • Fernandes, J. F., O. Castellani, and M. Plese: Biosynthesis of histamine ribotide and imidazoleacetate ribotide. Biochem. biophys. Res. Commun. 3, 679 (1960).

    CAS  Google Scholar 

  • Grossman, L., and N. O. Kaplan: Nicotinamide riboside phosphorylase from human erythrocytes. I. Phosphorolytic activity. J. biol. Chem. 231, 717 (1958).

    CAS  Google Scholar 

  • Halpern, B. N., I. DAÏNow: Recherches expérimentales sur une nouvelle propriété pharmacodynamique de l’amide nicotinique: action antagoniste vis-à-vis de certain effets de l’histamine. Z. Vitaminforsch. 15, 250 (1944).

    CAS  Google Scholar 

  • Heppel, L. A., and R. J. Hilmoe: Purification and properties of 5-nucleotidase. J. biol. Chem. 188, 665 (1951).

    PubMed  CAS  Google Scholar 

  • Hofmann, E. C. G.: Dpn- und Tpn-spezifische Nucleosidasen in Erythrocyten. I. Spezifität und Reinigung der Enzyme. Biochem. Z. 329, 428 (1957).

    CAS  Google Scholar 

  • Kaplan, N. O.: In: P. D. Boyer, H. Lardy, and K. Myrback (Editors), “The Enzymes” Vol. 3, p. 166. New York and London: Academic Press 1960.

    Google Scholar 

  • Karjala, S. A.: The partial characterization of a histamine metabolite from rat and mouse urine. J. Amer. chem. Soc. 77, 504 (1955).

    Article  CAS  Google Scholar 

  • Kobayashi, Y.: A histamine metabolizing enzyme system of mouse liver. Arch. Biochem. 71, 352 (1957).

    Article  PubMed  CAS  Google Scholar 

  • Kornberg, A., and W. E. Pricer, JR.: Nucleotide pyrophosphatase. J. biol. Chem. 182, 763 (1950).

    CAS  Google Scholar 

  • Kosower, E. M.: “Molecular Biochemistry” pp. 109, 250. New York: McGraw-Hill 1962.

    Google Scholar 

  • Leone, E., and L. Bonaduce: Soluble pyridine nucleotide nucleosidase from seminal vesicles. Biochim. biophys. Acta (Amst.) 31, 292 (1959).

    Article  CAS  Google Scholar 

  • Mejbaum, W.: Über die Bestimmung kleiner Pentosemengen insbesondere in Derivaten der Adenylsäure. Hoppe-Seylers Z. physiol. Chem. 258, 117 (1939).

    CAS  Google Scholar 

  • Mota, I., and W. Dias DA Silva: Antigen-induced damage to isolated sensitized mast cells. Nature (Lond.) 186, 245 (1960a).

    Article  CAS  Google Scholar 

  • Mota, I., and W. Dias DA Silva: The anti-anaphylactic and histamine releasing properties of the antihistamines. Their effect on the mast cells. Brit. J. Pharmacol. 15, 396 (1960b).

    PubMed  CAS  Google Scholar 

  • Mota, I., and W. Dias DA Silva, and J. Ferreirafernandes: The inhibition of mast cell damage and histamine release in anaphylaxis by pyridine and diphosphopyridine nucleotidase inhibitors. Comparison with compound 48/80. Brit. J. Pharmacol. 15, 405 (1960).

    PubMed  CAS  Google Scholar 

  • Muraoka, S., M. Inoue, and H. Yamasaki: Enzymic formation of histamine ribotide from histamine dinucleotide. Nature (Lond.) 190, 532 (1961).

    Article  CAS  Google Scholar 

  • Peter, J. V., D. E. Hultquist, M. Deluca, G. Kreil, and P. D. Boyer: Bound phosphohistidine as an intermediate in a phosphorylation reaction of oxidative phosphorylation catalyzed by mitochondrial extracts. J. biol. Chem. 238, PC 1182 (1963).

    Google Scholar 

  • Schauer, R. W.: Catabolism of physiological quantities of histamine in vivo. Physiol. Rev. 39, 116 (1959).

    Google Scholar 

  • Tabor, H., and O. Hayaishi: The excretion of imidazoleacetic acid riboside following the administration of imidazoleacetic acid or histamine to rats. J. Amer. chem. Soc. 77, 505 (1955).

    Article  CAS  Google Scholar 

  • Wallenfels, K., D. Stathakos, and H. Diekmann: A new procedure for the solubilization of beef spleen diphosphopyridine nucleotidase. Biochem. biophys. Res. Commun. 3, 632 (1960).

    CAS  Google Scholar 

  • Zatman, L. J., N. O. Kaplan, and S. P. Colowick: Inhibition of spleen diphosphopyridine nucleotidase by nicotinamide, an exchange reaction. J. biol. Chem. 200, 197 (1953).

    PubMed  CAS  Google Scholar 

  • Zatman, L. J., N. O. Kaplan, and S. P. Colowick, and M. M. Ciotti: Effect of isonicotinic acid hydrazide on diphosphopyridine nucleotidases. J. biol. Chem. 209, 453 (1954).

    PubMed  CAS  Google Scholar 

  • Zeller, E. A., and J. Barsky: In vivo inhibition of liver and brain monoamine oxidase by 1-isonicotinyl-2-isopropyl hydrazine. Proc. Soc. exp. Biol. (N. Y.) 81, 459 (1952).

    CAS  Google Scholar 

  • Zeller, E. A., P. Stern, and L. A. Blanksma: Degradation of histamine by monoamine oxidase. Naturwissenschaften 43, 157 (1956).

    Article  CAS  Google Scholar 

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Mauricio Rocha e Silva

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Alivisatos, S.G.A. (1966). Histamine — Pyridine Coenzyme Interactions. In: Rocha e Silva, M. (eds) Histamine and Anti-Histaminics. Handbuch der experimentellen Pharmakologie / Handbook of Experimental Pharmacology, vol 18 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-12016-3_28

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  • DOI: https://doi.org/10.1007/978-3-662-12016-3_28

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-662-12018-7

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