scholarly journals Responsiveness of a Xenopus laevis cell line to the aryl hydrocarbon receptor ligands 6-formylindolo[3,2-b]carbazole (FICZ) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)

2010 ◽  
Vol 183 (1) ◽  
pp. 202-211 ◽  
Author(s):  
Leo B. Laub ◽  
Brian D. Jones ◽  
Wade H. Powell
2012 ◽  
Vol 362 (1-2) ◽  
pp. 39-47 ◽  
Author(s):  
Elin Swedenborg ◽  
Maria Kotka ◽  
Martin Seifert ◽  
Jun Kanno ◽  
Ingemar Pongratz ◽  
...  

2004 ◽  
Vol 50 (5) ◽  
pp. 530-536 ◽  
Author(s):  
Masashi Sekimoto ◽  
Miho Iwamoto ◽  
Shoji Miyajima ◽  
Kiyomitsu Nemoto ◽  
Masakuni Degawa

1993 ◽  
Vol 294 (1) ◽  
pp. 95-101 ◽  
Author(s):  
E C Henry ◽  
T A Gasiewicz

The binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) to the aryl hydrocarbon receptor (AhR) elicits a sequence of poorly defined molecular events that ultimately yield a heteromeric transformed AhR that is active as a transcription factor. We have previously developed a model of the ligand-initiated transformation of the AhR to the DNA-binding state based on characterization of several forms of the AhR with respect to their physicochemical properties and DNA-binding affinities. The present studies were designed to determine whether, and at what stage, this process of transformation alters the receptor's affinity for TCDD. In rat hepatic cytosol, approx. 10% of the TCDD specifically bound to the AhR rapidly dissociated (t1/2 approximately 1 h), while the remainder was only slowly dissociable (t1/2 approximately 70 h). The isolated DNA-binding forms of the receptor (monomeric and transformed) bound TCDD very tightly (t1/2 > 100 h), whereas TCDD was dissociable from the non-DNA-binding receptor form(s). A lower incubation temperature (0-4 degrees C) and the presence of molybdate partially stabilized the non-DNA-binding fraction of the TCDD.receptor complex and also enhanced TCDD dissociation in crude cytosol. Immunoprecipitation of the different AhR forms with an anti-AhR antibody and immunoblotting with antibody to the 90 kDa heat-shock protein (hsp90) demonstrated that hsp90 was associated with the unoccupied receptor complex as well as with a fraction of the non-DNA-binding TCDD.receptor complex; isolated DNA-binding forms did not contain detectable hsp90. We conclude that while hsp90 remains associated with the AhR, TCDD is readily dissociable; following release of hsp90, however, TCDD becomes very tightly bound, and remains so upon completion of transformation.


2013 ◽  
Vol 48 (2) ◽  
pp. 145-151 ◽  
Author(s):  
Soledad Chamorro ◽  
Elizabeth Monsalvez ◽  
Benjamín Piña ◽  
Alba Olivares ◽  
Víctor Hernández ◽  
...  

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