Immunochemical detection of covalently modified kidney proteins in S-(1,1,2,2,-tetrafluoroethyl)-L-cysteine-treated rats
| Autor: | M. W. Anders, Sally J. Hargus |
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| Rok vydání: | 1991 |
| Předmět: |
Time Factors
Hydrocarbons Fluorinated Metabolite Immunoblotting Cross Reactions Mitochondrion Biology Kidney Biochemistry Nephrotoxicity chemistry.chemical_compound Cytosol medicine Animals Cysteine Pharmacology Dose-Response Relationship Drug Aminooxyacetic Acid Proteins Glutathione Molecular biology Mitochondria Rats medicine.anatomical_structure chemistry Conjugate |
| Zdroj: | Biochemical Pharmacology. 42:R17-R20 |
| ISSN: | 0006-2952 |
| DOI: | 10.1016/0006-2952(91)90580-x |
| Popis: | The nephrotoxicity of several haloalkenes is associated with glutathione S -conjugate formation, metabolism of the glutathione S -conjugate to the corresponding cysteine S -conjugate and translocation to the kidney, and metabolism by renal cysteine conjugate β-lyase (β-lyase, EC 4.4.1.13) to electrophilic metabolites that cause cell damage and death in proximal tubular cells (1,2). S -(1,1,2,2-Tetrafluoroethyl)-L-cysteine (TFEC), the cysteine S -conjugate of tetrafluoroethene, is nephrotoxic (3), and covalent modification of cellular macromolecules has been implicated in the toxicity of S -conjugates (4,5) and other xenobiotics (6,7). The present study utilized immunochemical methods to demonstrate selective binding of the TFEC metabolites to renal proteins in TFEC-treated rats. Previous studies indicated that mitochondria are a primary target of toxic S -conjugates (8,9) and that β-lyase activity is present in both renal cytosolic and mitochondrial fractions (10). Therefore, renal mitochondrial and cytosolic fractions were examined for the presence of modified proteins, which were detected with polyclonal antibodies to trifluoroacetylated proteins that cross-react with protein-bound metabolites of TFEC. |
| Databáze: | OpenAIRE |
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