Abstract:
The effect of in vitro glycation on δ-aminolevulinic dehydratase (ALA-D) under several experimental conditions was investigated. When preincubated with 500 mM glucose at 37°C for 20 hr, ALA-D was 80% inactivated and glycated hemoglobin levels were increased more than fourfold.Thiobarbituric acid species were not modified during glycation; therefore ALA-D inactivation cannot be attributed to glucose autoxidation.Acetyl salicylic acid was effective in preventing both hemoglobin glycation and ALA-D inactivation by glucose.A method has been developed for measuring protein glycation in vitro, in a crude preparation of red blood cells, which can also be applied to sugars other than glucose. Copyright (C) 1998 Elsevier Science Inc.
Registro:
Documento: |
Artículo
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Título: | Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention |
Autor: | Caballero, F.A.; Gerez, E.N.; Polo, C.F.; Vazquez, E.S.; Del C. Batlle, A.M. |
Filiación: | Ctro. de Invest. sobre P., (CONICET - FCEN, UBA), Ciudad Universitaria, Pabellón II, 1428 Buenos Aires, Argentina Viamonte 1881 10 A, 1056 Buenos Aires, Argentina
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Palabras clave: | δ-aminolevulinic dehydratase; Acetyl salicylic acid; Carbohydrates; Enzyme inactivation; Glycated hemoglobin; Glycation; Lipid peroxidation; acetylsalicylic acid; carbohydrate; glycosylated hemoglobin; porphobilinogen synthase; thiobarbituric acid; article; enzyme activity; enzyme inactivation; erythrocyte; human; human cell; lipid peroxidation; priority journal; protein glycosylation; temperature; Aspirin; Carbohydrate Metabolism; Carbohydrates; Glucose; Glycosylation; Hemoglobin A, Glycosylated; Humans; Lipid Peroxidation; Porphobilinogen Synthase; Temperature; Time Factors |
Año: | 1998
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Volumen: | 31
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Número: | 3
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Página de inicio: | 441
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Página de fin: | 445
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DOI: |
http://dx.doi.org/10.1016/S0306-3623(98)00016-0 |
Título revista: | General Pharmacology
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Título revista abreviado: | Gen. Pharmacol.
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ISSN: | 03063623
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CODEN: | GEPHD
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CAS: | Aspirin, 50-78-2; Carbohydrates; Glucose, 50-99-7; Hemoglobin A, Glycosylated; Porphobilinogen Synthase, EC 4.2.1.24
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Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03063623_v31_n3_p441_Caballero |
Referencias:
- Batlle, A., Ferramola, A., Grinstein, M., Purification and general properties of δ-aminolevulinate dehydratase from cow liver (1967) Biochem. J., 104, pp. 244-249
- Beswick, H., Harding, J., Aldehydes and dicarbonyls in nonenzymic glycosylation of proteins (1985) Biochem. J., 226, pp. 385-389
- Brownlee, M., Glycation products and the pathogenesis of diabetic complications (1992) Diabetes Care, 15, pp. 1835-1843
- Brownlee, M., Glycation and diabetic complications (1994) Diabetes, 43, pp. 836-841
- Brownlee, M., The pathological implications of proteins glycation (1995) Clin. Inv. Med., 18, pp. 275-281
- Caballero, F., Gerez, E., Polo, C., Mompo, O., Vazquez, E., Schultz, R., Bernabó, J., Batlle, A., Estudio sobre las alteraciones en el camino metabólico del hemo en una población de pacientes diabéticos (1995) Medicina, 55, pp. 117-124
- Cerami, A., Bucala, R., Vlassara, H., A common pathogenic mechanism for diabetic complications (1991) In Diabetic Complications: Epidemiology and Pathogenic Mechanisms, pp. 37-44. , (Edited by Andreani D., Gueriguian J., Striker G. and Conti F.) Raven Press, New York
- Cherian, M., Abraham, E., In vitro glycation and acetylation (by aspirin) of rat crystallins (1993) Life Sci., 52, pp. 1699-1707
- Fu, M., Wells-Knecht, K., Blackledge, J., Lyons, T., Thorpe, S., Baynes, J., Glycation, glycoxidation and cross-linking of collagen by glucose: Kinetics, mechanism and inhibition of late stages of the Maillard reaction (1994) Diabetes, 43, pp. 676-683
- Jain, S., Palmer, N., The effect of oxygen radicals metabolites and vitamin E on glicosylation of proteins (1997) Free Radical Biol. Med., 22, pp. 593-596
- Kochakian, M., Manjula, B., Egan, J., Chronic dosing with aminoguanidine and novel advanced glycosylation end product-formation inhibitors ameliorates cross-linking of tail tendon collagen in STZ-induced diabetic rats (1996) Diabetes, 45, pp. 1694-1700
- Nagaraj, R., Shipanova, Y., Faust, F., Protein cross-linking by Maillard reaction: Isolation, characterization and in vivo detection of lysine-lysine cross-link derived from methylglyoxal (1996) J. Biol. Chem., 271, pp. 19338-19345
- Niehaus, W., Samuelson, B., Formation of malondialdehyde from phospholipid arachidonate during microsomal lipid peroxidation (1968) Eur. J. Biochem., 6, pp. 126-130
- Parker, M., England, J., Da Costa, J., Hess, R., Goldstein, D., Improved colorimetric assay for glycosylated hemoglobin (1981) Clin. Chem., 27, pp. 669-672
- Polo, C., Vazquez, E., Gerez, E., Caballero, F., Batlle, A., STZ-induced diabetes in mice and heme pathway enzymes: Effect of allylisopropylacetamide and α-tocopherol (1995) Chem. Biol. Int., 95, pp. 327-334
- Rendell, M., Nieremberg, J., Brannan, C., Valentine, J., Stephen, P., Dodd, S., Mercer, P., Walder, J., Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo (1986) Lab. Clin. Med., 108, pp. 286-293
- Schwartz, J., The role of glycohemoglobin and other proteins in diabetes management (1995) Diabetes Rev., 3, pp. 269-287
- Strowig, S., Raskin, P., Glycemic control and complications of diabetes: After diabetes control and complications trial (1995) Diabetes Rev., 3, pp. 237-257
- Swamy, M., Abraham, E., Inhibition of lens crystallin glycation and high molecular weight aggregate formation by aspirin in vitro and in vivo (1989) Invest. Ophthalmol. Vis. Sci., 30, pp. 1120-1126
- Syrovy, I., Glycation of myofibrillar proteins and ATPase activity after incubation with eleven sugars (1994) Physiol. Res., 43, pp. 61-64
- Thorpe, S., Baynes, J., Role of the Maillard reaction in diabetes mellitus and diseases of aging (1996) Drugs Aging, 9, pp. 69-77
- Trüeb, B., Holenstein, C., Fischer, C., Winterhalter, K., Nonenzymatic glycosylation of proteins: A warning (1980) J. Biol. Chem., 255, pp. 6717-6720
- Wolff, S., Dean, R., Glucose autoxidation and protein modification: The potential role of "autoxidative glycosylation" in diabetes (1987) Biochem. J., 245, pp. 243-250
- Yim, H., Kang, S., Hah, Y., Chock, P., Yim, M., Free radicals generated during the glycation reaction of amino acids by methylglyoxal (1996) J. Biol. Chem., 270, pp. 28228-28233
Citas:
---------- APA ----------
Caballero, F.A., Gerez, E.N., Polo, C.F., Vazquez, E.S. & Del C. Batlle, A.M.
(1998)
. Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention. General Pharmacology, 31(3), 441-445.
http://dx.doi.org/10.1016/S0306-3623(98)00016-0---------- CHICAGO ----------
Caballero, F.A., Gerez, E.N., Polo, C.F., Vazquez, E.S., Del C. Batlle, A.M.
"Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention"
. General Pharmacology 31, no. 3
(1998) : 441-445.
http://dx.doi.org/10.1016/S0306-3623(98)00016-0---------- MLA ----------
Caballero, F.A., Gerez, E.N., Polo, C.F., Vazquez, E.S., Del C. Batlle, A.M.
"Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention"
. General Pharmacology, vol. 31, no. 3, 1998, pp. 441-445.
http://dx.doi.org/10.1016/S0306-3623(98)00016-0---------- VANCOUVER ----------
Caballero, F.A., Gerez, E.N., Polo, C.F., Vazquez, E.S., Del C. Batlle, A.M. Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention. Gen. Pharmacol. 1998;31(3):441-445.
http://dx.doi.org/10.1016/S0306-3623(98)00016-0