Polychlorinated biphenyls and related compound interactions with specific binding sites for thyroxine in rat liver nuclear extracts

1987 ◽  
Vol 30 (1) ◽  
pp. 79-86 ◽  
Author(s):  
J. McKinney ◽  
R Fannin ◽  
S. Jordan ◽  
K. Chae ◽  
U. Rickenbacher ◽  
...  
Keyword(s):  
Polychlorinated Biphenyls ◽  
Rat Liver ◽  
Related Compound ◽  
Binding Sites ◽  
Specific Binding ◽  
Specific Binding Sites ◽  
Nuclear Extracts

scholarly journals Characterization of a thyroid-hormone-binding site on nuclear envelopes and nuclear matrices of the male-rat liver

1984 ◽  
Vol 219 (3) ◽  
pp. 1001-1007 ◽  
Author(s):  
Y A Lefebvre ◽  
J T Venkatraman
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Intact Animal ◽  
Binding Capacity ◽  
Specific Binding ◽  
Male Rat ◽  
Scatchard Analysis ◽  
Specific Binding Sites ◽  
Number Of Binding Sites

Nuclear envelopes and nuclear matrices were isolated from the male-rat liver. Incubation of 125I-labelled 3,3′,5-tri-iodothyronine (T3) with the nuclear-envelope fraction resulted in specific binding of T3 to the membranes. Maximum specific binding occurred at 30 degrees C after 2h incubation. Storage for 1 week at -80 degrees C resulted in no loss of binding. Scatchard analysis revealed a class of binding sites with KD 86 nM. 3,3′,5′-Tri-iodothyronine was as effective a competitor of [125I]T3 binding to nuclear envelopes as was L-T3 itself, and tri-iodothyroacetic acid was 70% as potent as T3. L- and D-thyronine did not compete for [125I]T3 binding. Incubation of nuclear envelopes with 0.6 M-NaCl before addition of T3 resulted in the complete loss of specific binding sites, whereas exposure of the membranes to 2.0 M-NaCl after incubation with T3 did not extract binding sites. Nuclear matrices, after incubation with [125I]T3 under the same conditions, were shown to possess a class of binding sites with a similar KD but with approx. 30% of the maximum binding capacity. Nuclear envelopes from hypothyroid animals may possess slightly lower numbers of binding sites compared with nuclear envelopes from the intact animal, whereas nuclear matrices from hypothyroid animals have the same number of binding sites as do nuclear envelopes from the intact animal. In conclusion, nuclear envelopes and nuclear matrices have a class of binding sites with relatively high affinity for T3. It is distinct from nuclear and cytosolic binding sites.

SPECIFIC BINDING SITES FOR L-TRIIODOTHYRONINE IN RAT LIVER AND KIDNEY CYTOSOL

1976 ◽  
Vol 82 (1) ◽  
pp. 98-104 ◽  
Author(s):  
T. J. Visser ◽  
H. F. Bernard ◽  
R. Docter ◽  
G. Hennemann
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Specific Binding ◽  
Specific Binding Sites ◽  
Liver And Kidney

Interactions of rutaecarpine alkaloids with specific binding sites for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver

1989 ◽  
Vol 10 (4) ◽  
pp. 651-654 ◽  
Author(s):  
Mikael Gillner ◽  
Jan Bergman ◽  
Christian Cambillau ◽  
Jan-Åke Gustafsson
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Specific Binding ◽  
Specific Binding Sites ◽  
Tetrachlorodibenzo P Dioxin

Specific binding sites for 3,3′-diiodo-l -thyronine (3,3′-T2 ) in rat liver mitochondria

FEBS Letters ◽  
1994 ◽  
Vol 351 (2) ◽  
pp. 237-240 ◽  
Author(s):  
Antonia Lanni ◽  
Maria Moreno ◽  
Claus Horst ◽  
Assunta Lombardi ◽  
Goglia Fernando
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Specific Binding ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Specific Binding Sites

A novel class of inactive steroid-binding sites in female rat liver nuclei

1986 ◽  
Vol 110 (1) ◽  
pp. 27-36 ◽  
Author(s):  
D. M. Bechet ◽  
B. N. Perry
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Specific Binding ◽  
Gel Filtration ◽  
Nuclear Extract ◽  
Female Rat ◽  
Rat Liver Nuclei ◽  
Heat Stable ◽  
Nuclear Extracts ◽  
Liver Nuclei

ABSTRACT Nuclear salt extracts from intact female rat liver showed insignificant levels of progesterone-, oestradiol-, testosterone- or dexamethasone-specific binding. However, brief exposure of nuclear extracts to dextran-coated charcoal (DCC) induced binding for all the above classes of steroids. This 'DCC-effect', which was reproduced neither by gel filtration nor by extensive dialysis of the nuclear extract, could not be ascribed to removal of endogenous free or loosely bound steroids. We show that rat liver nuclei contain a class of secondary binding sites (BsII), which exhibit moderate or low affinity for steroid ligands, positive co-operativity, and cross-reaction between classes of steroids. The capacity of BsII sites to bind steroids depends strictly on prior neutralization by DCC of endogenous heat-stable non-dialysable inhibitor(s). The putative roles of these BsII binding sites are discussed in relation to component(s) probably responsible for inhibitory activity. J. Endocr. (1986) 110, 27–36

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