STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol
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...
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1995
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092797_v95_n3_p327_Polo http://hdl.handle.net/20.500.12110/paper_00092797_v95_n3_p327_Polo |
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paper:paper_00092797_v95_n3_p327_Polo2023-06-08T14:33:58Z STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol 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 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. 1995 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092797_v95_n3_p327_Polo http://hdl.handle.net/20.500.12110/paper_00092797_v95_n3_p327_Polo |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol |
| topic_facet |
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 |
| description |
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. |
| title |
STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol |
| title_short |
STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol |
| title_full |
STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol |
| title_fullStr |
STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol |
| title_full_unstemmed |
STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and α-tocopherol |
| title_sort |
stz-induced diabetes in mice and heme pathway enzymes. effect of allylisopropylacetamide and α-tocopherol |
| publishDate |
1995 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092797_v95_n3_p327_Polo http://hdl.handle.net/20.500.12110/paper_00092797_v95_n3_p327_Polo |
| _version_ |
1768543733459976192 |