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  • 1
    Electronic Resource
    Electronic Resource
    Inhibition of 2,5-Hexanedione-Induced Protein Crosslinking by Biological Thiols: Chemical Mechanisms and Toxicological Implications (1995)
    s.l. : American Chemical Society
    Chemical research in toxicology 8 (1995), S. 764-771 
    Details
    ISSN: 1520-5010
    Source: ACS Legacy Archives
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/tx00047a017
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  • 2
    Electronic Resource
    Electronic Resource
    Formation and Structure of Crosslinking and Monomeric Pyrrole Autoxidation Products in 2,5-Hexanedione-Treated Amino Acids, Peptides, and Protein1 (1994)
    s.l. : American Chemical Society
    Chemical research in toxicology 7 (1994), S. 551-558 
    Details
    ISSN: 1520-5010
    Source: ACS Legacy Archives
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/tx00040a011
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of isothiocyanates, thioureas, and other lysine adduction products in carbon disulfide-treated peptides and protein (1992)
    s.l. : American Chemical Society
    Chemical research in toxicology 5 (1992), S. 496-504 
    Details
    ISSN: 1520-5010
    Source: ACS Legacy Archives
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/tx00028a007
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  • 4
    Electronic Resource
    Electronic Resource
    Multiple Forms of Glutamate Decarboxylase in Porcine Brain (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 40 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Three forms of glutamate decarboxylase from hog brain (termed α-, ß-, and γ-GAD) were separated by hydrophobic interaction chromatography on phenyl-Sepharose, by isoelectric focusing, and by polyacryl-amide gel electrophoresis. When rechromatographed on phenyl-Sepharose, each form migrated as a single entity, indicating that the forms are not readily interconvertible. The three forms are not different-sized aggregates of one form, since all three have the same approximate molecular weight (100,000) as determined by Sephadex G-200 chromatography. The pIs of the three forms separated by phenyl-Sepharose were determined by isoelectric focusing. The values obtained (5.3, 5.5, and 5.8 for α-, ß-, and γ-GAD, respectively) were comparable to the pIs of the three peaks of activity observed upon focusing of enzyme that had been subjected to phenyl-Sepharose chromatography. These results indicate that phenyl-Sepharose chromatography and isoelectric focusing separate the same three components. When synaptosomal extracts were analyzed by phenyl-Sepharose chromatography without intervening purification steps, all three forms were present, but the proportion of ß-GAD was somewhat higher and that of γ-GAD somewhat lower than in the usual preparations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb08101.x
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  • 5
    Electronic Resource
    Electronic Resource
    Effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin, 12-O-tetradecanoylphorbol-13-acetate and 17β-estradiol on estrogen receptor regulation in MCF-7 human breast cancer cells (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 60 (1996), S. 173-184 
    Details
    ISSN: 0730-2312
    Keywords: occupied nuclear estrogen receptors ; estrogen metabolism ; P450 ; environmental ; endocrine-modulating ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) exhibits remarkably potent antiestrogenic activity. To further elucidate the role of estrogen receptor (ER) regulation in this response, we examined the effects of exposure to TCDD in MCF-7 human breast cancer cells on ER mRNA levels by using an RNase protection assay, on ER accumulation by using an ER immunocytochemical essay (ER-ICA), and on ER function by competitive binding assays under conditions of saturating 17β-estradiol (E2). Comparative studies were conducted with E2 and 12-O-tetradecanoylphorbol-13-acetate (TPA), as both compounds are known to suppress ER expression. Our results indicate that 1 nM E2 and 100 nM TPA both suppress ER mRNA levels as early as 4 h after exposure and to 33.6% and 16.5% of control levels, respectively, after 72 h. In contrast, no significant effect on ER mRNA levels was attributed to exposure to 10 nM TCDD. A greater than 50% reduction in positive staining was observed by ER-ICA after 72 h exposure to 1 nM E2 and to 100 nM TPA, while only an 11% reduction in positive staining was observed with 10 nM TCDD. Specific binding of [3H]E2 under saturating conditions (10 nM E2) in whole cells was reduced by 50% in cultures exposed to 100 nM TPA, although no effect on binding was observed with exposure to 10 nM TCDD. In contrast, specific binding using subsaturating 1 nM [3H]E2 was depressed by 49% in MCF-7 cells exposed to 10 nM TCDD for 72 h. This depression was inhibited by a 1-h treatment with 5 μM α-naphthoflavone, which inhibits TCDD-induced, P450-mediated, E2 metabolism, and subsequent E2 depletion. In conclusion, while TPA and E2 effectively down-regulate ER expression, TCDD, under antiestrogenic conditions, has little if any effect on total ER levels in MCF-7 cells, and thus ER modulation is probably not necessary for the suppression of estrogenic activity in MCF-7 cells by TCDD. © 1996 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    12-O-tetradecanoylphorbol-13-acetate upregulates the Ah receptor and differentially alters CYP1B1 and CYP1A1 expression in MCF-7 breast cancer cells (1998)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 70 (1998), S. 289-296 
    Details
    ISSN: 0730-2312
    Keywords: cytochrome P450 ; estrogen metabolism ; estradiol 4-hydroxylation ; estrogen receptor ; 2,3,7,8-tetrachlorodibenzo-p- dioxin ; polymerase chain reaction ; cancer biomarkers ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Elevated expression of cytochrome P450 1B1 (CYP1B1) and estradiol 4-hydroxylation have been reported to be biomarkers of tumorigenesis in humans. The aromatic hydrocarbon receptor (AhR) regulates expression of human cytochrome P450 1A1 (CYP1A1) and CYP1B1, 17β-estradiol (E2) 2- and 4-hydroxylases, respectively. There is also evidence that expression of estrogen receptor α (ERα) potentiates CYP1A1 inducibility in breast cancer cells. To characterize these relationships further, we examined the effects of 12-O-tetradecanoylphorbol-13-acetate (TPA), which downregulates ERα, and the high-affinity AhR ligand, 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), on the expression of AhR, ERα, CYP1A1, and CYP1B1 in MCF-7 human breast cancer cells. Treatment with TPA, which suppressed ERα mRNA levels, caused a greater than fourfold elevation of AhR mRNA and protein levels, whereas treatment with TCDD caused a decrease in AhR protein but no change in ERα or AhR mRNA levels. In MCF-7 cells treated with TPA prior to treatment with TCDD, the AhR mRNA level was elevated, the ERα mRNA level remained suppressed, and the ratio of CYP1B1 to CYP1A1 mRNA was increased compared with treatment with TCDD alone. A corresponding increase in the ratio of the rates of 4- to 2-hydroxylation pathways of E2 metabolism was also observed in response to pretreatment with TPA prior to the addition of TCDD. These results demonstrate differential regulation of the human CYP1A1 and CYP1B1 genes and provide a cellular model to investigate further the mechanisms that may be involved in the elevated expression of CYP1B1 in tumorigenesis. J. Cell. Biochem. 70:289-296, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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