The mammalian aryl hydrocarbon (Ah) receptor: from mediator of dioxin toxicity toward physiological functions in skin and liver
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Karl Walter Bock
Abstract
The mammalian Ah receptor (AhR) is a ligand-activated transcription factor with multiple functions in adaptive metabolism, development and dioxin toxicity in a variety of organs and cell systems. Phenotypes observed following sustained activation by dioxin or in AhR-null mice suggest organ-dependent physiological functions. These functions are probably deregulated following exposure to dioxin. We focus on skin and liver to facilitate discussion of mechanisms linking phenotypes and AhR-modulated genotypes. After a brief summary of currently discussed AhR ligand candidates, two groups of direct AhR target genes/proteins and associated functions are highlighted: (i) xenobiotic-metabolizing enzymes which are also involved in homeostasis of endogenous ligands and (ii) proteins controlling cell proliferation/apoptosis, differentiation and inflammation. Homeostatic feedback loops might not only include CYP1A1 but also Phase II enzymes such as UGT1A1 which controls the antioxidant AhR ligand bilirubin. The AhR is involved in extensive crosstalk with other transcription factors and multiple signaling pathways. Efforts elucidating the pathway toward identification of physiological functions of the AhR remain challenging and promising.
©2009 by Walter de Gruyter Berlin New York
Artikel in diesem Heft
- Reviews
- Chemokines in tumor-associated angiogenesis
- The mammalian aryl hydrocarbon (Ah) receptor: from mediator of dioxin toxicity toward physiological functions in skin and liver
- The mechanism of ATP-dependent RNA unwinding by DEAD box proteins
- Protein Structure and Function
- Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum
- Factors regulating tachyphylaxis triggered by N-terminal-modified angiotensin II analogs
- Cancer Osaka thyroid (Cot) phosphorylates Polo-like kinase (PLK1) at Ser137 but not at Thr210
- Coagulation factor XIII variants with altered thrombin activation rates
- Cell Biology and Signaling
- Stimulation of fibroblast proliferation by the plant cysteine protease CMS2MS2 is independent of its proteolytic activity and requires ERK activation
- EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in pancreatic carcinoma cells
- Identification of collagen IV derived danger/alarm signals in insect immunity by nanoLC-FTICR MS
- Proteolysis
- Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage
- Acknowledgment
- Acknowledgment
- Contents Volume 390, 2009
- Contents Biological Chemistry, Volume 390, 2009
- Author Index
- Author Index
- Subject Index
- Subject Index
Artikel in diesem Heft
- Reviews
- Chemokines in tumor-associated angiogenesis
- The mammalian aryl hydrocarbon (Ah) receptor: from mediator of dioxin toxicity toward physiological functions in skin and liver
- The mechanism of ATP-dependent RNA unwinding by DEAD box proteins
- Protein Structure and Function
- Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum
- Factors regulating tachyphylaxis triggered by N-terminal-modified angiotensin II analogs
- Cancer Osaka thyroid (Cot) phosphorylates Polo-like kinase (PLK1) at Ser137 but not at Thr210
- Coagulation factor XIII variants with altered thrombin activation rates
- Cell Biology and Signaling
- Stimulation of fibroblast proliferation by the plant cysteine protease CMS2MS2 is independent of its proteolytic activity and requires ERK activation
- EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in pancreatic carcinoma cells
- Identification of collagen IV derived danger/alarm signals in insect immunity by nanoLC-FTICR MS
- Proteolysis
- Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage
- Acknowledgment
- Acknowledgment
- Contents Volume 390, 2009
- Contents Biological Chemistry, Volume 390, 2009
- Author Index
- Author Index
- Subject Index
- Subject Index
