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Abstract:

A frequent coexistence of diabetes and porphyria disease has been reported. Under normal conditions, porphyrin biosynthesis is well regulated to only form the amount of heme required for the synthesis of the various hemoproteins. The activity of some heme enzymes and rhodanese in streptozotocin (STZ) induced diabetic mice and in allylisopropylacetamide (AIA) induced experimental acute porphyria mice has been examined. The role of α-tocopherol (α-T), reported to prevent protein glycation in vitro, has also been investigated. AIA induced hepatic δ-aminolevulinic acid synthetase (ALA-S) activity in control animals but was ineffective in the diabetic group. α-Tocopherol did not modify ALA-S activity in either group. δ-Aminolevulinic acid dehydratase (ALA-D) and deaminase activities were significantly diminished both in liver and blood of diabetic animals. α-Tocopherol prevented inhibition of ALA-D, deaminase and blood rhodanese activities in diabetic animals but α-tocopherol by itself did not affect the basal levels of the enzymes studied. The potential use of a-tocopherol to prevent late complications of diabetes, including the onset of a porphyria like syndrome is considered. © 1995.

Registro:

Documento: Artículo
Título:STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol
Autor:Polo, C.F.; Vázquez, E.S.; Gerez, E.N.; Caballero, F.A.; del C. Batlle, A.M.
Filiación:Centro de Investigacions sobre Porfirinas y Porfirias (CIPYP), (CONICET - UBA), Ciudad Universitaria, Pabellon II, 2do Piso, 1428 Buenos Aires, Argentina
Palabras clave:Allylisopropylacetamide; Streptozotocin induced diabetes; α-Tocopherol; δ-Aminolevulinic acid; 5 aminolevulinate synthase; allylisopropylacetamide; alpha tocopherol; deaminase; porphobilinogen synthase; streptozocin; thiosulfate sulfurtransferase; acute intermittent porphyria; animal experiment; animal model; animal tissue; article; blood level; controlled study; disease association; heme synthesis; intraperitoneal drug administration; liver level; male; mouse; nonhuman; protein glycosylation; streptozocin diabetes; 5-Aminolevulinate Synthetase; Allylisopropylacetamide; Animal; Blood Glucose; Diabetes Mellitus, Experimental; Heme; Male; Mice; Nucleoside Deaminases; Porphobilinogen Synthase; Porphyria, Acute Intermittent; Streptozocin; Support, Non-U.S. Gov't; Thiosulfate Sulfurtransferase; Vitamin E
Año:1995
Volumen:95
Número:3
Página de inicio:327
Página de fin:334
DOI: http://dx.doi.org/10.1016/0009-2797(94)03573-Q
Título revista:Chemico-Biological Interactions
Título revista abreviado:Chem.-Biol. Interact.
ISSN:00092797
CODEN:CBINA
CAS:5 aminolevulinate synthase, 9037-14-3; allylisopropylacetamide, 299-78-5; alpha tocopherol, 1406-18-4, 1406-70-8, 52225-20-4, 58-95-7, 59-02-9; deaminase, 9067-84-9; porphobilinogen synthase, 9036-37-7; streptozocin, 18883-66-4; thiosulfate sulfurtransferase, 9026-04-4; 5-Aminolevulinate Synthetase, EC 2.3.1.37; Allylisopropylacetamide, 299-78-5; Blood Glucose; Heme, 14875-96-8; Nucleoside Deaminases, EC 3.5.4; Porphobilinogen Synthase, EC 4.2.1.24; Streptozocin, 18883-66-4; Thiosulfate Sulfurtransferase, EC 2.8.1.1; Vitamin E, 1406-18-4
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092797_v95_n3_p327_Polo

Referencias:

  • Pirart, Why don't we teach and treat diabetic patients better? (1978) Diabetes Care, 1, p. 139
  • Brownlee, Cerami, The biochemistry of the complications of diabetes mellitus (1981) Annu. Rev. Biochem., 50, p. 385
  • Renold, Mintz, Muller, Cahill, Jr, (1978) The etabolic basis of inherited disease, p. 80. , J.B. Stanbury, J.B. Wyngaarden, D.S. Fredrickson, McGraw-Hill Books Co, New York
  • Sterling, Silver, Riketts, Development of porphyria in diabetes mellitus (1949) Arch. Int. Med., 84, p. 965
  • Burnham, Fossnaugh, Porphyria, diabetes and their relations (1961) Arch. Dermatol., 83, p. 717
  • Goerz, Korda, Porphyria cutanea tarda (PCT) und diabetes mellitus (1977) Z. Haut., 52, p. 1165
  • Welland, Factors affecting excretion of porphyrin precursors by patients with acute intermittent porphyria: I. Effect of diet (1964) Metabolism, 13, p. 232
  • Felsher, Redeker, Acute intermittent porphyria: effect of diet and griseofulvin (1967) Medicine, 46, p. 217
  • Yalouris, Raptis, Effects of diabetes on porphyric attacks (1987) Br. Med. J., 295, p. 1237
  • Bitar, Weiner, Diabetes-induced metabolic alterations in heme synthesis and degradation and various heme-containing enzymes in female rats (1984) Diabetes, 33, p. 37
  • Djordjevic, δ-Aminolevulinic acid dehydratase activity in erythrocytes of diabetic patients (1985) Ann. Int. Physiol. Biochim., 93, p. 285
  • Ceriello, Giugliano, Quatraro, Russo, Torella, A preliminary note of inhibiting effect of α-tocopherol (vit. E) on protein glycation (1988) Diabetes Metab., 14, p. 40
  • Marver, Tschudy, Perlroth, Collins, δ-Aminolevulinic acid synthetase I. Studies in liver homogenates (1966) J. Biol. Chem., 241, p. 2803
  • Batlle, Ferramola, Grinstein, Purification and general properties of δ-aminolevulinate dehydratase from cow liver (1967) Biochem. J., 104, p. 244
  • Batlle, Wider, Stella, A simple method for measuring erythrocyte porphobilinogenase and its use in the diagnosis of acute intermittent porphyria (1978) Int. J. Biochem., 9, p. 871
  • Sörbo, Crystalline rhodanese I Purification and physico-chemical examination (1953) Acta Chemica Scandinavica, 7, p. 1129
  • Lowry, Rosenbrough, Fall, Randall, Protein measurement with the Folinphenol reagent (1951) J. Biol. Chem., 193, p. 265
  • Bonkowsky, Collins, Doherty, Tschudy, The glucose effect in rat liver: studies of δ-aminolevulinic synthase and tyrosine aminotransferase (1973) Biochim. Biophys. Acta, 320, p. 561
  • Giger, Meyer, Induction of δ-aminolevulinate synthase a cytochrome P-450 hemoprotein in hepatocyte culture (1981) J. Biol. Chem., 256, p. 11182
  • Schoenfeld, Greenblat, Epstein, Lahav, Beigel, Altsman, An in vitro model demonstrating the glucose effect and the influence of fasting on porphyrin metabolism (1982) FEBS Lett., 138, p. 277
  • Watson, (1970) Molecular Biology of the Gene, p. 435. , 2nd edition, W.A. Benjamin Inc, New York, Harvard University and Cold Spring Harbor Laboratory
  • Kim, Kikuchi, Mechanism of allylisopropylacetamide induced increase of δ-aminolevulinate synthetase in liver mitochondria (1974) Arch. Biochem. Biophys., 164, p. 293
  • Arvanitakis, Folscroft, Stitt, Effect of alloxan induced diabetes on intestinal peptidases in rat (1978) Endocrinology, 102, p. 1118
  • Chang, Noble, Wyse, High glucose-induced enzyme activity changes in cultured cell lines established from the kidneys of Chinese hamsters with aglycosuria or spontaneous glycosuria (1981) Experientia, 37, p. 934
  • Hough, Avioli, Teitelbaum, Fallon, Alkaline phosphatase activity in chronic streptozotocin induced insulin deficiency in the rat: effect of insulin replacement (1981) Metab. Clin. Exp., 30, p. 1190
  • Iino, Fishman, The effect of sucrose and other carbohydrates on human alkaline phosphatase isoenzyme activity (1979) Clin. Chim. Acta., 92, p. 197
  • Pollak, Coradello, Leban, Maxa, Sternberg, Widham, Lubec, Inhibition of alkaline phosphatase activity by glucose (1983) Clin. Chim. Acta., 133, p. 15
  • Beswick, Harding, Aldehydes and dicarbonyls in non-enzymic glycosylation of proteins (1985) Biochem. J., 226, p. 385
  • Wolff, Dean, Glucose autoxidation and protein modification. The potential role of ‘autoxidative glycosylation’ in diabetes (1987) Biochem. J., 245, p. 243

Citas:

---------- APA ----------
Polo, C.F., Vázquez, E.S., Gerez, E.N., Caballero, F.A. & del C. Batlle, A.M. (1995) . STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol. Chemico-Biological Interactions, 95(3), 327-334.
http://dx.doi.org/10.1016/0009-2797(94)03573-Q
---------- CHICAGO ----------
Polo, C.F., Vázquez, E.S., Gerez, E.N., Caballero, F.A., del C. Batlle, A.M. "STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol" . Chemico-Biological Interactions 95, no. 3 (1995) : 327-334.
http://dx.doi.org/10.1016/0009-2797(94)03573-Q
---------- MLA ----------
Polo, C.F., Vázquez, E.S., Gerez, E.N., Caballero, F.A., del C. Batlle, A.M. "STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol" . Chemico-Biological Interactions, vol. 95, no. 3, 1995, pp. 327-334.
http://dx.doi.org/10.1016/0009-2797(94)03573-Q
---------- VANCOUVER ----------
Polo, C.F., Vázquez, E.S., Gerez, E.N., Caballero, F.A., del C. Batlle, A.M. STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol. Chem.-Biol. Interact. 1995;95(3):327-334.
http://dx.doi.org/10.1016/0009-2797(94)03573-Q