Luiz F. Stoppiglia, Luiz F. Rezende, Fabiano Ferreira, Eliane Filiputti, Everardo M. Carneiro, Antonio C. Boschero
{"title":"低H2O2浓度下离体新生大鼠胰岛过氧化物酶系统的表征。","authors":"Luiz F. Stoppiglia, Luiz F. Rezende, Fabiano Ferreira, Eliane Filiputti, Everardo M. Carneiro, Antonio C. Boschero","doi":"10.1016/j.bbadis.2004.06.005","DOIUrl":null,"url":null,"abstract":"<div><div>B cell destruction during the onset of diabetes mellitus is associated with oxidative stress. In this work, we attempted to further trace the fate of H<sub>2</sub>O<sub>2</sub> inside the pancreatic islets and determine whether it is mediated by enzymatic (peroxidase) activity or by chemical reaction with thiols from any protein chain. Our results suggest that the islet cells have a very similar peroxidase activity at the hydrophilic (cytoplasm) and hydrophobic compartments (organelles and nucleus), independent of the catalase content of the samples. This activity is composed of sacrificial thiols and by proteins with Fe<sup>3+</sup>/Mn<sup>3+</sup> ions at non-heme catalytic sites. The capacity of the hydrophobic fraction to scavenge O<sub>2</sub><sup>−</sup> was increased in the presence of high concentrations of NADP<sup><img></sup> and RS<sup><img></sup> and was highly dependent on RSH. On the contrary, the hydrophilic fraction exhibited a low RSH-dependent activity where the O<sub>2</sub><sup>−</sup> scavenging is related to metal Cu<sup>2+</sup>/Fe<sup>3+</sup>/Mn<sup>3+</sup> ions attached to the protein molecules.</div></div>","PeriodicalId":8821,"journal":{"name":"Biochimica et biophysica acta. Molecular basis of disease","volume":"1690 2","pages":"Pages 159-168"},"PeriodicalIF":4.2000,"publicationDate":"2004-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Characterization of the peroxidase system at low H2O2 concentrations in isolated neonatal rat islets\",\"authors\":\"Luiz F. Stoppiglia, Luiz F. Rezende, Fabiano Ferreira, Eliane Filiputti, Everardo M. Carneiro, Antonio C. Boschero\",\"doi\":\"10.1016/j.bbadis.2004.06.005\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>B cell destruction during the onset of diabetes mellitus is associated with oxidative stress. In this work, we attempted to further trace the fate of H<sub>2</sub>O<sub>2</sub> inside the pancreatic islets and determine whether it is mediated by enzymatic (peroxidase) activity or by chemical reaction with thiols from any protein chain. Our results suggest that the islet cells have a very similar peroxidase activity at the hydrophilic (cytoplasm) and hydrophobic compartments (organelles and nucleus), independent of the catalase content of the samples. This activity is composed of sacrificial thiols and by proteins with Fe<sup>3+</sup>/Mn<sup>3+</sup> ions at non-heme catalytic sites. The capacity of the hydrophobic fraction to scavenge O<sub>2</sub><sup>−</sup> was increased in the presence of high concentrations of NADP<sup><img></sup> and RS<sup><img></sup> and was highly dependent on RSH. On the contrary, the hydrophilic fraction exhibited a low RSH-dependent activity where the O<sub>2</sub><sup>−</sup> scavenging is related to metal Cu<sup>2+</sup>/Fe<sup>3+</sup>/Mn<sup>3+</sup> ions attached to the protein molecules.</div></div>\",\"PeriodicalId\":8821,\"journal\":{\"name\":\"Biochimica et biophysica acta. Molecular basis of disease\",\"volume\":\"1690 2\",\"pages\":\"Pages 159-168\"},\"PeriodicalIF\":4.2000,\"publicationDate\":\"2004-10-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et biophysica acta. Molecular basis of disease\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0925443904000973\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et biophysica acta. Molecular basis of disease","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0925443904000973","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Characterization of the peroxidase system at low H2O2 concentrations in isolated neonatal rat islets
B cell destruction during the onset of diabetes mellitus is associated with oxidative stress. In this work, we attempted to further trace the fate of H2O2 inside the pancreatic islets and determine whether it is mediated by enzymatic (peroxidase) activity or by chemical reaction with thiols from any protein chain. Our results suggest that the islet cells have a very similar peroxidase activity at the hydrophilic (cytoplasm) and hydrophobic compartments (organelles and nucleus), independent of the catalase content of the samples. This activity is composed of sacrificial thiols and by proteins with Fe3+/Mn3+ ions at non-heme catalytic sites. The capacity of the hydrophobic fraction to scavenge O2− was increased in the presence of high concentrations of NADP and RS and was highly dependent on RSH. On the contrary, the hydrophilic fraction exhibited a low RSH-dependent activity where the O2− scavenging is related to metal Cu2+/Fe3+/Mn3+ ions attached to the protein molecules.
期刊介绍:
BBA Molecular Basis of Disease addresses the biochemistry and molecular genetics of disease processes and models of human disease. This journal covers aspects of aging, cancer, metabolic-, neurological-, and immunological-based disease. Manuscripts focused on using animal models to elucidate biochemical and mechanistic insight in each of these conditions, are particularly encouraged. Manuscripts should emphasize the underlying mechanisms of disease pathways and provide novel contributions to the understanding and/or treatment of these disorders. Highly descriptive and method development submissions may be declined without full review. The submission of uninvited reviews to BBA - Molecular Basis of Disease is strongly discouraged, and any such uninvited review should be accompanied by a coverletter outlining the compelling reasons why the review should be considered.