Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition
Some late complications of diabetes are associated with alterations in the structure and function of proteins due to glycation and free radicals generation. Aspirin inhibits protein glycation by acetylation of free amino groups. In the diabetic status, it was demonstrated that several enzymes of hem...
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| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
2000
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 11837caa a22012977a 4500 | ||
|---|---|---|---|
| 001 | PAPER-2339 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203144.0 | ||
| 008 | 190411s2000 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0034213854 | |
| 024 | 7 | |2 cas |a Aspirin, 50-78-2; Blood Glucose; Catalase, EC 1.11.1.6; Enzyme Inhibitors; Hemoglobin A, Glycosylated; Hydroxymethylbilane Synthase, EC 2.5.1.61; Porphobilinogen Synthase, EC 4.2.1.24; Streptozocin, 18883-66-4 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a CBINA | ||
| 100 | 1 | |a Caballero, F. | |
| 245 | 1 | 0 | |a Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition |
| 260 | |c 2000 | ||
| 270 | 1 | 0 | |m Batlle, A.Viamonte 1881 10 A, C1056ABA Buenos Aires, Argentina; email: batlle@mail.retina.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Brownlee, M., Lilly Lecture. Glycation and diabetes complications (1994) Diabetes, 43, pp. 836-841 | ||
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| 504 | |a Bastar, I., Seckin, S., Uysal, M., Aykac-Toker, G., Effect of streptozotocin on glutathione and lipid peroxide levels in various tissues of rats (1998) Res. Commun. Mol. Pathol. Pharmacol., 102, pp. 265-272 | ||
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| 520 | 3 | |a Some late complications of diabetes are associated with alterations in the structure and function of proteins due to glycation and free radicals generation. Aspirin inhibits protein glycation by acetylation of free amino groups. In the diabetic status, it was demonstrated that several enzymes of heme pathway were diminished. The aim of this work has been to investigate the in vivo effect of short and long term treatment with acetylsalicylic acid in streptozotocin induced diabetic mice. In both treatments, the acetylsalicylic acid prevented δ-aminolevulinic dehydratase and porphobilinogen deaminase inactivation in diabetic mice and blocked the accumulation of lipoperoxidative aldehydes. Catalase activity was significantly augmented in diabetic mice and the long term treatment with aspirin partially reverted it. We propose that oxidative stress might play an important role in streptozotocin induced diabetes. Our results suggest that aspirin can prevent some of the late complications of diabetes, lowering glucose concentration and probably inhibiting glycation by acetylation of protein amino groups. Copyright (C) 2000 Elsevier Science Ireland Ltd. |l eng | |
| 536 | |a Detalles de la financiación: A. Batlle and E. Vazquez are members of the Career of Scientific Researcher at the Argentine National Research Council (CONICET). F. Caballero and E. Gerez hold the post of Research Assistant at the CONICET. This work has been supported by grants from the CONICET and the University of Buenos Aires, Argentina. We are very grateful to B. Corvalan for technical assistance. | ||
| 593 | |a Department of Biological Chemistry, FCEN, Univ. Buenos Aires, Ctro. I., Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ACETYLSALICYLIC ACID |
| 690 | 1 | 0 | |a EXPERIMENTAL DIABETES MELLITUS |
| 690 | 1 | 0 | |a GLYCATION |
| 690 | 1 | 0 | |a HEME ENZYMES INACTIVATION |
| 690 | 1 | 0 | |a LIPID PEROXIDATION |
| 690 | 1 | 0 | |a OXIDATIVE STRESS |
| 690 | 1 | 0 | |a ACETYLSALICYLIC ACID |
| 690 | 1 | 0 | |a CATALASE |
| 690 | 1 | 0 | |a GLUCOSE |
| 690 | 1 | 0 | |a HEME |
| 690 | 1 | 0 | |a PORPHOBILINOGEN DEAMINASE |
| 690 | 1 | 0 | |a PORPHOBILINOGEN SYNTHASE |
| 690 | 1 | 0 | |a ANIMAL EXPERIMENT |
| 690 | 1 | 0 | |a ANIMAL MODEL |
| 690 | 1 | 0 | |a ANIMAL TISSUE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a ENZYME INACTIVATION |
| 690 | 1 | 0 | |a GLYCATION |
| 690 | 1 | 0 | |a LIPID PEROXIDATION |
| 690 | 1 | 0 | |a LIVER |
| 690 | 1 | 0 | |a MALE |
| 690 | 1 | 0 | |a MOUSE |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a OXIDATIVE STRESS |
| 690 | 1 | 0 | |a PROTEIN GLYCOSYLATION |
| 690 | 1 | 0 | |a STREPTOZOCIN DIABETES |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a ASPIRIN |
| 690 | 1 | 0 | |a BLOOD GLUCOSE |
| 690 | 1 | 0 | |a CATALASE |
| 690 | 1 | 0 | |a DIABETES MELLITUS, EXPERIMENTAL |
| 690 | 1 | 0 | |a DIET |
| 690 | 1 | 0 | |a EATING |
| 690 | 1 | 0 | |a ENZYME INHIBITORS |
| 690 | 1 | 0 | |a HEMOGLOBIN A, GLYCOSYLATED |
| 690 | 1 | 0 | |a HYDROXYMETHYLBILANE SYNTHASE |
| 690 | 1 | 0 | |a LIPID PEROXIDATION |
| 690 | 1 | 0 | |a MALE |
| 690 | 1 | 0 | |a MICE |
| 690 | 1 | 0 | |a OXIDATIVE STRESS |
| 690 | 1 | 0 | |a PORPHOBILINOGEN SYNTHASE |
| 690 | 1 | 0 | |a STREPTOZOCIN |
| 700 | 1 | |a Gerez, E. | |
| 700 | 1 | |a Batlle, A. | |
| 700 | 1 | |a Vazquez, E. | |
| 773 | 0 | |d 2000 |g v. 126 |h pp. 215-225 |k n. 3 |p Chem.-Biol. Interact. |x 00092797 |w (AR-BaUEN)CENRE-4162 |t Chemico-Biological Interactions | |
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