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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2000
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092797_v126_n3_p215_Caballero http://hdl.handle.net/20.500.12110/paper_00092797_v126_n3_p215_Caballero |
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paper:paper_00092797_v126_n3_p215_Caballero2023-06-08T14:33:57Z Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition Gerez, Esther Noemí Batlle, Alcira María del Carmen Vázquez, Elba Susana Acetylsalicylic acid Experimental diabetes mellitus Glycation Heme enzymes inactivation Lipid peroxidation Oxidative stress acetylsalicylic acid catalase glucose heme porphobilinogen deaminase porphobilinogen synthase animal experiment animal model animal tissue article controlled study enzyme activity enzyme inactivation glycation lipid peroxidation liver male mouse nonhuman oxidative stress protein glycosylation streptozocin diabetes Animals Aspirin Blood Glucose Catalase Diabetes Mellitus, Experimental Diet Eating Enzyme Inhibitors Hemoglobin A, Glycosylated Hydroxymethylbilane Synthase Lipid Peroxidation Male Mice Oxidative Stress Porphobilinogen Synthase Streptozocin 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. Fil:Gerez, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vazquez, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2000 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092797_v126_n3_p215_Caballero http://hdl.handle.net/20.500.12110/paper_00092797_v126_n3_p215_Caballero |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Acetylsalicylic acid Experimental diabetes mellitus Glycation Heme enzymes inactivation Lipid peroxidation Oxidative stress acetylsalicylic acid catalase glucose heme porphobilinogen deaminase porphobilinogen synthase animal experiment animal model animal tissue article controlled study enzyme activity enzyme inactivation glycation lipid peroxidation liver male mouse nonhuman oxidative stress protein glycosylation streptozocin diabetes Animals Aspirin Blood Glucose Catalase Diabetes Mellitus, Experimental Diet Eating Enzyme Inhibitors Hemoglobin A, Glycosylated Hydroxymethylbilane Synthase Lipid Peroxidation Male Mice Oxidative Stress Porphobilinogen Synthase Streptozocin |
spellingShingle |
Acetylsalicylic acid Experimental diabetes mellitus Glycation Heme enzymes inactivation Lipid peroxidation Oxidative stress acetylsalicylic acid catalase glucose heme porphobilinogen deaminase porphobilinogen synthase animal experiment animal model animal tissue article controlled study enzyme activity enzyme inactivation glycation lipid peroxidation liver male mouse nonhuman oxidative stress protein glycosylation streptozocin diabetes Animals Aspirin Blood Glucose Catalase Diabetes Mellitus, Experimental Diet Eating Enzyme Inhibitors Hemoglobin A, Glycosylated Hydroxymethylbilane Synthase Lipid Peroxidation Male Mice Oxidative Stress Porphobilinogen Synthase Streptozocin Gerez, Esther Noemí Batlle, Alcira María del Carmen Vázquez, Elba Susana Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition |
topic_facet |
Acetylsalicylic acid Experimental diabetes mellitus Glycation Heme enzymes inactivation Lipid peroxidation Oxidative stress acetylsalicylic acid catalase glucose heme porphobilinogen deaminase porphobilinogen synthase animal experiment animal model animal tissue article controlled study enzyme activity enzyme inactivation glycation lipid peroxidation liver male mouse nonhuman oxidative stress protein glycosylation streptozocin diabetes Animals Aspirin Blood Glucose Catalase Diabetes Mellitus, Experimental Diet Eating Enzyme Inhibitors Hemoglobin A, Glycosylated Hydroxymethylbilane Synthase Lipid Peroxidation Male Mice Oxidative Stress Porphobilinogen Synthase Streptozocin |
description |
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. |
author |
Gerez, Esther Noemí Batlle, Alcira María del Carmen Vázquez, Elba Susana |
author_facet |
Gerez, Esther Noemí Batlle, Alcira María del Carmen Vázquez, Elba Susana |
author_sort |
Gerez, Esther Noemí |
title |
Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition |
title_short |
Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition |
title_full |
Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition |
title_fullStr |
Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition |
title_full_unstemmed |
Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition |
title_sort |
preventive aspirin treatment of streptozotocin induced diabetes: blockage of oxidative status and revertion of heme enzymes inhibition |
publishDate |
2000 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092797_v126_n3_p215_Caballero http://hdl.handle.net/20.500.12110/paper_00092797_v126_n3_p215_Caballero |
work_keys_str_mv |
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_version_ |
1768546378518102016 |