Cyanide intoxication-I. An oral chronic animal model
The effects of oral chronic cyanide administration to mice were studied. Cyanide intoxication was confirmed by the increased levels of this poison and the concomitant inhibition of cytochrome oxidase activity in liver, brain, heart and blood. The detoxifying enzyme rhodanese was measured. The state...
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| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
1989
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 09657caa a22009377a 4500 | ||
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| 001 | PAPER-723 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203003.0 | ||
| 008 | 190411s1989 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0024604682 | |
| 024 | 7 | |2 cas |a cyanide, 57-12-5; cytochrome c oxidase, 72841-18-0, 9001-16-5; thiocyanate, 302-04-5; thiosulfate sulfurtransferase, 9026-04-4; Cyanides; Cytochrome-c Oxidase, EC 1.9.3.1; Proteins; Sulfur, 7704-34-9; Thiocyanates; Thiosulfate Sulfurtransferase, EC 2.8.1.1 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a GEPHD | ||
| 100 | 1 | |a Buzaleh, A.M. | |
| 245 | 1 | 0 | |a Cyanide intoxication-I. An oral chronic animal model |
| 260 | |c 1989 | ||
| 270 | 1 | 0 | |m del C. Batlle, A.M.; Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), CONICET, Facultad de Ciencias Exactas y Naturales, 1448 Buenos Aires, Argentina |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Albaum, Tepperman, Bodansky, The in vivo inactivation by cyanide of brain cytochrome oxidase and its effect on glycolysis and on the high energy phosphorous compounds in brain (1946) J Biol Chem, 164, pp. 45-51 | ||
| 504 | |a Ballantyne, Artifacts in the definition of toxicity by cyanides and cyanogens (1983) Fundamental and Applied Toxicology, 3, pp. 400-408 | ||
| 504 | |a Boxer, Rickards, Studies on the metabolism of the carbon of cyanide and thiocyanate (1952) Arch. Biochem., 39, pp. 7-12 | ||
| 504 | |a Finazzi Agró, Federici, Giovagnoli, Cannella, Cavallini, Effect of sulfur binding on rhodanese fluourescence (1972) European Journal of Biochemistry, 28, pp. 89-93 | ||
| 504 | |a Guilbault, Kramer, Specific detection and determination of cyanide using various quinone derivatives (1965) Analytical Chemistry, 37, pp. 1395-1400 | ||
| 504 | |a Himwich, Saunders, Enzymatic conversion of cyanide to thiocyanate (1948) Am. J. Physiol., 153, pp. 348-354 | ||
| 504 | |a Isom, Way, Lethality of cyanide in the absence of inhibition of liver cytochrome oxidase (1976) Biochem. Pharmac., 25, pp. 605-608 | ||
| 504 | |a Isom, Burrows, Way, Effect of oxygen on the antagonism of cyanide intoxication (1982) Cytochrome oxidase in vivo, 65, pp. 250-256. , Tox. appl. Pharmac | ||
| 504 | |a Koh, The determination of micro amounts of polythionates I A photometric method for the determination of pentathionate by means of its cyanolysis (1965) Bulletin of the Chemical Society of Japan, 38, pp. 1510-1515 | ||
| 504 | |a Lowry, Rosebrough, Farr, Randall, Protein measurement with the Folin-Phenol reagent (1951) J. biol. Chem., 193, pp. 265-275 | ||
| 504 | |a Schubert, Brill, Antagonism of experimental cyanide toxicity in relation to the in vivo activity of cytochrome oxidase (1968) J. Pharmac. exp. Ther., 162, pp. 352-359 | ||
| 504 | |a Solomonson, (1982) Cyanide in Biology, pp. 11-28. , Academic Press, London | ||
| 504 | |a Sörbo, Crystalline rhodanese I Purification and physico-chemical examination (1953) Acta Chemica Scandinavica, 7, pp. 1129-1136 | ||
| 504 | |a Vázquez, Buzaleh, Wider, Batlle, Red blood cell rhodanese: its possible role in modulating δ-aminolevulinate synthetase activity in mammals (1987) Int. J. Biochem., 19, pp. 217-219 | ||
| 504 | |a Vennesland, Castic, Conn, Solomonson, Volini, Westley, Cyanide metabolism (1982) Fedn Proc., 41, pp. 2639-2648 | ||
| 504 | |a Way, Cyanide intoxication and its mechanism of antagonism (1984) A. Rev. Pharmac. Tox., 24, pp. 451-481 | ||
| 504 | |a Westley, Adler, Westley, Nishida, The sulfur-transferases (1983) Fundamental and Applied Toxicology, 3, pp. 377-382 | ||
| 504 | |a Wilson, Cyanide in human diseases a review of clinical and laboratory evidence (1983) Fundamental and Applied Toxicology, 3, pp. 397-399 | ||
| 504 | |a Wood, Cooley, Detoxification of cyanide by cystine (1956) J Biol Chem, 218, pp. 449-457 | ||
| 504 | |a Yonetani, Ray, Studies on cytochrome oxidase VI. Kinetics of the aerobic oxidation of ferrocytochrome c by cytochrome oxidase (1965) J. biol. Chem., 240, pp. 3392-3398 | ||
| 520 | 3 | |a The effects of oral chronic cyanide administration to mice were studied. Cyanide intoxication was confirmed by the increased levels of this poison and the concomitant inhibition of cytochrome oxidase activity in liver, brain, heart and blood. The detoxifying enzyme rhodanese was measured. The state of the sulfane sulfur pool was investigated by determination of the cyanide labile-sulfur levels. A clear correlation between rhodanese activity and sulfur content was obtained as a consequence of cyanide action. These results support the belief that rhodanese plays a fundamental role in the detoxification process of cyanide, in preventing cyanide reaching the target tissues. © 1989. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: Secretaria de Ciencia y Tecnica, Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: The results obtained indicate that an animal model for chronic cyanide intoxication can be produced by oral administration of the toxin to mice. Under the conditions described, cyanide intoxication was demonstrated by the high levels of cyanide accumulated in organs and blood, as well as by the corresponding inhibition of cytochrome oxidase activity; although it should be considered that the degree of inhibition in tissue homogenates may not be an accurate reflection of the situation in rive (Ballantyne, 1983). The fact that rhodanese activity was detectable even without adding cyanide to the incubation mixture, is also indicative of the presence of the toxin in these tissues• The diminished activity of liver rhodanese could be attributed to the high levels of cyanide in the tissue; this effect would be magnified by the lower hepatic levels of labile sulfur measured which would reduce the degree of conversion of rhodanese to its active sulfur substituted form (Finazzi Agr6 et al., 1972). During the first clays of intoxication a 50% increase of brain rhodanese activity was detected, showing this enzymatic system to be functioning at its maximal rate detoxifying the cyanide in this target tissue• No changes were detected for the heart enzyme measured in the presence of cyanide, but it was slightly modified when no substrate was added to the incubation system. Although labile sulfur concentration was significantly diminished, the system still retained the control activity levels in this vital organ• The high labile sulfur values found in blood correspond with the formation of the very active sulfur substituted form of the enzyme and therefore we would not expect its activity to be modified by the excess of cyanide detected in this tissue• This is the form of rhodanese which would actually detoxify the cyanide. In conclusion, one of the earliest effects of cyanide seems to be an inhibition of the hepatic rhodanese which is presumably due to either blockage by excess binding to the active site and/or depletion of the sulfane-sulfur pool. These changes do not seem to occur in blood where rhodanese functions at its maximal rate, thus preventing cyanide reaching the target tissues and therefore exerting its lethal action• Acknowledgements--A. M. del C. BatUe holds the post of Scientific Research in the Argentine National Research Council (CONICET); E. Vfizquez and A. M. Buzaleh are research fellows at the CONICET. This work was supported by grants from the CONICET, the SECYT, SecretafiA de Salud Pfblica del Ministerio de Bienestar Social, UBA and Banco de la N~ci6n Argentina. We wish to express our gratitude to Lic. S. Afonso for the excellent drawings, and to Laboratios Promeco, B. Aires for providing the animals. | ||
| 593 | |a Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), CONICET, Facultad de Ciencias Exactas y Naturales, 1448 Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a CYANIDE |
| 690 | 1 | 0 | |a CYTOCHROME C OXIDASE |
| 690 | 1 | 0 | |a THIOCYANATE |
| 690 | 1 | 0 | |a THIOSULFATE SULFURTRANSFERASE |
| 690 | 1 | 0 | |a ANIMAL CELL |
| 690 | 1 | 0 | |a ANIMAL EXPERIMENT |
| 690 | 1 | 0 | |a ANIMAL MODEL |
| 690 | 1 | 0 | |a BLOOD |
| 690 | 1 | 0 | |a BRAIN |
| 690 | 1 | 0 | |a DETOXIFICATION |
| 690 | 1 | 0 | |a HEART |
| 690 | 1 | 0 | |a INTOXICATION |
| 690 | 1 | 0 | |a LIVER |
| 690 | 1 | 0 | |a MOUSE |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a ADMINISTRATION, ORAL |
| 690 | 1 | 0 | |a ANIMAL |
| 690 | 1 | 0 | |a CYANIDES |
| 690 | 1 | 0 | |a CYTOCHROME-C OXIDASE |
| 690 | 1 | 0 | |a MICE |
| 690 | 1 | 0 | |a PROTEINS |
| 690 | 1 | 0 | |a SULFUR |
| 690 | 1 | 0 | |a SUPPORT, NON-U.S. GOV'T |
| 690 | 1 | 0 | |a THIOCYANATES |
| 690 | 1 | 0 | |a THIOSULFATE SULFURTRANSFERASE |
| 690 | 1 | 0 | |a TIME FACTORS |
| 700 | 1 | |a Vazquez, E.S. | |
| 700 | 1 | |a Del Battle, C.A.M. | |
| 773 | 0 | |d 1989 |g v. 20 |h pp. 323-327 |k n. 3 |p Gen. Pharmacol. Vasc. Syst. |x 03063623 |w (AR-BaUEN)CENRE-4808 |t General Pharmacology | |
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| 856 | 4 | 0 | |u https://doi.org/10.1016/0306-3623(89)90267-X |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_03063623_v20_n3_p323_Buzaleh |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03063623_v20_n3_p323_Buzaleh |y Registro en la Biblioteca Digital |
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| 999 | |c 61676 | ||