T Zanić-Grubisić, A Santini, I Cepelak, K Barisić, D Juretić, S Pepeljnjak
{"title":"Influence of ochratoxin A treatment on the activity of membrane bound enzymes in rat brain regions.","authors":"T Zanić-Grubisić, A Santini, I Cepelak, K Barisić, D Juretić, S Pepeljnjak","doi":"10.1515/bchm3.1996.377.2.121","DOIUrl":null,"url":null,"abstract":"<p><p>Ochratoxin A is a mycotoxin produced by Aspergillus ochraceus and is a natural contaminant of mouldy food. We examined the neuroactive potential of ochratoxin A by measuring the changes in the activities of several membrane bound, cytoplasmic and lysosomal enzymes in the brain of adult female rats, following subchronic application of ochratoxin A. The activities of both soluble and membrane bound fractions of ecto-5'nucleotidase, ecto-Ca2+/Mg2+ATPase, alanine aminopeptidase, gamma-glutamyl transferase, as well as activities of lactate dehydrogenase and of N-acetyl-beta-D-glucosaminidase were followed. Biochemical effects were examined in cerebral cortex, cerebellum and hippocampus. The results obtained showed physiologically significant alterations in the activity of enzymes tested. The changes were found to be time-dependent and regionally selective. Compared to controls, statistically significant increases in gamma-glutamyl transferase were observed in all three brain regions, while in the case of alanine aminopeptidase activities differed with regard to region, the highest increase being observed in hippocampus. Ecto-Ca2+/Mg2+ATPase and ecto-5'nucleotidase showed distinct changes lasting for 20 days of treatment, while increase in the activities of N-acetyl-beta-D-glucosaminidase and lactate dehydrogenase were visible only at the beginning of the treatment. By the end of the trial the activities of almost all enzymes returned back to normal values.</p>","PeriodicalId":8963,"journal":{"name":"Biological chemistry Hoppe-Seyler","volume":"377 2","pages":"121-7"},"PeriodicalIF":0.0000,"publicationDate":"1996-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm3.1996.377.2.121","citationCount":"10","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biological chemistry Hoppe-Seyler","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/bchm3.1996.377.2.121","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 10
Abstract
Ochratoxin A is a mycotoxin produced by Aspergillus ochraceus and is a natural contaminant of mouldy food. We examined the neuroactive potential of ochratoxin A by measuring the changes in the activities of several membrane bound, cytoplasmic and lysosomal enzymes in the brain of adult female rats, following subchronic application of ochratoxin A. The activities of both soluble and membrane bound fractions of ecto-5'nucleotidase, ecto-Ca2+/Mg2+ATPase, alanine aminopeptidase, gamma-glutamyl transferase, as well as activities of lactate dehydrogenase and of N-acetyl-beta-D-glucosaminidase were followed. Biochemical effects were examined in cerebral cortex, cerebellum and hippocampus. The results obtained showed physiologically significant alterations in the activity of enzymes tested. The changes were found to be time-dependent and regionally selective. Compared to controls, statistically significant increases in gamma-glutamyl transferase were observed in all three brain regions, while in the case of alanine aminopeptidase activities differed with regard to region, the highest increase being observed in hippocampus. Ecto-Ca2+/Mg2+ATPase and ecto-5'nucleotidase showed distinct changes lasting for 20 days of treatment, while increase in the activities of N-acetyl-beta-D-glucosaminidase and lactate dehydrogenase were visible only at the beginning of the treatment. By the end of the trial the activities of almost all enzymes returned back to normal values.