Association of the thyroid hormone receptor with rat liver chromatin

Biochemistry ◽  
1981 ◽  
Vol 20 (24) ◽  
pp. 6781-6789 ◽  
Author(s):  
Donald B. Jump ◽  
Steven Seelig ◽  
Harold L. Schwartz ◽  
Jack H. Oppenheimer
1989 ◽  
Vol 120 (2) ◽  
pp. 237-243 ◽  
Author(s):  
K. Ichikawa ◽  
J. Brtko ◽  
L. J. DeGroot ◽  
K. Hashizume ◽  
T. Yamada

ABSTRACT Rat liver nuclear thyroid hormone receptor lost 3,5,3′-tri-iodo-l-thyronine (T3)-binding activity with a half-life of 14 days, 4 h, 139 min, 62 min, 16 min or 6 min at 0, 36, 38, 40, 43 or 45 °C respectively, when present in crude nuclear extracts. Glycerol increased the half-life of the receptor during heat inactivation. Protection was reversible by removing the glycerol. The receptor was unstable at a pH below 6·0 or above 10·0. We also found a loss of the receptor activity during the separation of bound and free hormone using the resin test. Of several conditions tested for the separation of bound and free hormone, the addition of heated nuclear extract gave the most accurate estimation of bound hormone when using the resin test. Using these characteristics of the receptor, we purified the receptor to 1220 pmol T3-binding capacity/mg protein with a final yield of 14·6 μg/4 kg rat liver. Journal of Endocrinology (1989) 120, 237–243


Life Sciences ◽  
2006 ◽  
Vol 78 (22) ◽  
pp. 2584-2594 ◽  
Author(s):  
M.M. Montesinos ◽  
C.G. Pellizas ◽  
M.L. Vélez ◽  
S. Susperreguy ◽  
A.M. Masini-Repiso ◽  
...  

Endocrinology ◽  
2006 ◽  
Vol 147 (7) ◽  
pp. 3211-3218 ◽  
Author(s):  
Amedeo Columbano ◽  
Monica Pibiri ◽  
Manuela Deidda ◽  
Costanza Cossu ◽  
Thomas S. Scanlan ◽  
...  

Endocrinology ◽  
1982 ◽  
Vol 111 (5) ◽  
pp. 1758-1760 ◽  
Author(s):  
Yvonne David-Inouye ◽  
Ralph SomacK ◽  
Steven K. Nordeen ◽  
James W. Apriletti ◽  
John D. Baxter ◽  
...  

2003 ◽  
Vol 179 (3) ◽  
pp. 379-385 ◽  
Author(s):  
B Zandieh-Doulabi ◽  
E Dop ◽  
M Schneiders ◽  
MP Schiphorst ◽  
A Mansen ◽  
...  

Many metabolic processes occur simultaneously in the liver in different locations along the porto-central axis of the liver units. These processes are often regulated by hormones, one of which is thyroid hormone which for its action depends on the presence of the different isoforms of the thyroid hormone receptor (TR). These are encoded by two genes: c-erbA-alpha encoding TRalpha1 and TRalpha2 and their respective Delta isoforms, and c-erbA-beta which encodes TRbeta1, TRbeta2 and TRbeta3. We recently found a zonal (pericentral) expression of and a diurnal variation in the TRbeta1 isoform in rat liver. We were therefore also interested to see whether TRalpha1 and TRalpha2 expression showed similar characteristics. For this reason we raised both polyclonal and monoclonal antibodies against TRalpha1 and TRalpha2 isoforms and characterised these. Antibody specificity was tested using Western blots and immunohistochemistry in liver of TR isoform-specific knockout animals. Using these antibodies we found that the TRalpha1 and TRalpha2 isoforms are zonally expressed around the central vein in rat liver. The experiments show that the portal to central gradient of TRalpha1 is broader than that of TRbeta1. Moreover, the expression of the TRalpha2 protein showed a diurnal variation with a peak in the afternoon when the animals are least active whereas no such variation was found for the TRalpha1 protein.From our data it appears that both the TRalpha1 and TRalpha2 isoforms show a zonal distribution in liver. This finding, together with the observed diurnal rhythm, has major implications for interpreting and timing experiments concerning the TR and its downstream actions in liver.


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