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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bockamp, Ernesto Oesch, Franz Huelster, Andrea Antoniou-lipfert, Patricia Oesch-bartlomowicz, Barbara Wiss, Oliver Arand, Michael Weiss, Carsten Dietrich, Cornelia |
| Description | Author Affiliation: Oesch-Bartlomowicz B ( Institute of Toxicology, University of Mainz, Obere Zahlbacher Strasse 67, 55131 Mainz, Germany. oeschb@uni-mainz.de); |
| Abstract | Even before the first vertebrates appeared on our planet, the aryl hydrocarbon receptor (AHR) gene was present to carry out one or more critical life functions. The vertebrate AHR then evolved to take on functions of detecting and responding to certain classes of environmental toxicants. These environmental pollutants include polycyclic aromatic hydrocarbons (e.g., benzo[a]pyrene), polyhalogenated hydrocarbons, dibenzofurans, and the most potent small-molecular-weight toxicant known, 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD or dioxin). After binding of these ligands, the activated AHR translocates rapidly from the cytosol to the nucleus, where it forms a heterodimer with aryl hydrocarbon nuclear translocator, causing cellular responses that lead to toxicity, carcinogenesis, and teratogenesis. The nuclear form of the activated AHR/aryl hydrocarbon nuclear translocator complex is responsible for alterations in immune, endocrine, reproductive, developmental, cardiovascular, and central nervous system functions whose mechanisms remain poorly understood. Here, we show that the second messenger, cAMP (an endogenous mediator of hormones, neurotransmitters, and prostaglandins), activates the AHR, moving the receptor to the nucleus in some ways that are similar to and in other ways fundamentally different from AHR activation by dioxin. We suggest that this cAMP-mediated activation may reflect the true endogenous function of AHR; disruption of the cAMP-mediated activation by dioxin, binding chronically to the AHR for days, weeks, or months, might be pivotal in the mechanism of dioxin toxicity. Understanding this endogenous activation of the AHR by cAMP may help in developing methods to counteract the toxicity caused by numerous environmental and food-borne toxic chemicals that act via the AHR. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 26 |
| Volume Number | 102 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2005-06-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cyclic AMP Metabolism Dioxins Chemistry Receptors, Aryl Hydrocarbon Signal Transduction Active Transport, Cell Nucleus Animals Bucladesine Cell Line, Tumor Cell Nucleus Colforsin Pharmacology Conservation Of Natural Resources Cyclic AMP-Dependent Protein Kinases Cytosol Dimerization Environmental Pollutants Fluorescent Antibody Technique, Indirect Genes, Reporter Genetic Vectors Green Fluorescent Proteins Immunoblotting Immunoprecipitation Ligands Mice Microscopy, Fluorescence Plasmids Prostaglandins Protein Binding Protein Transport Time Factors Transcription, Genetic Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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