scholarly journals Stimulation of hepatic mitochondrial alpha-glycerophosphate dehydrogenase and malic enzyme by L-triiodothyronine. Characteristics of the response with specific nuclear thyroid hormone binding sites fully saturated.

1977 ◽  
Vol 59 (3) ◽  
pp. 517-527 ◽  
Author(s):  
J H Oppenheimer ◽  
E Silva ◽  
H L Schwartz ◽  
M I Surks
Keyword(s):  
Thyroid Hormone ◽  
Binding Sites ◽  
Malic Enzyme ◽  
Hormone Binding ◽  
Glycerophosphate Dehydrogenase ◽  
Stimulation Of

scholarly journals A spin label study of the thyroid hormone-binding sites in human plasma thyroxine transport proteins.

1981 ◽  
Vol 256 (2) ◽  
pp. 831-836
Author(s):  
S.Y. Cheng ◽  
G. Rakhit ◽  
F. Erard ◽  
J. Robbins ◽  
C.F. Chignell
Keyword(s):  
Thyroid Hormone ◽  
Human Plasma ◽  
Spin Label ◽  
Binding Sites ◽  
Transport Proteins ◽  
Hormone Binding ◽  
Label Study

Recombinant Human Growth Hormone Increases Thyroid Hormone-Binding Sites in Recovering Severely Burned Children

Shock ◽  
2003 ◽  
Vol 19 (5) ◽  
pp. 399-403 ◽  
Author(s):  
Cara M. Connolly ◽  
Robert E. Barrow ◽  
David L. Chinkes ◽  
Jose A. Martinez ◽  
David N. Herndon
Keyword(s):  
Growth Hormone ◽  
Thyroid Hormone ◽  
Human Growth Hormone ◽  
Binding Sites ◽  
Recombinant Human Growth Hormone ◽  
Human Growth ◽  
Hormone Binding

Thyroid Hormone Binding to Isolated Human Apolipoproteins A-II, C-I, C-II, and C-III: Homology in Thyroxine Binding Sites

Thyroid ◽  
1994 ◽  
Vol 4 (3) ◽  
pp. 261-267 ◽  
Author(s):  
SALVATORE BENVENGA ◽  
HANS J. CAHNMANN ◽  
DAN RADER ◽  
MARIE KINDT ◽  
ANTONIO FACCHIANO ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Binding Sites ◽  
Hormone Binding

THYROID HORMONE-BINDING INTERACTIONS IN CYTOSOL OF RAT ANTERIOR PITUITARY

1977 ◽  
Vol 85 (2) ◽  
pp. 256-266 ◽  
Author(s):  
Valerie Anne Galton
Keyword(s):  
Thyroid Hormone ◽  
Binding Sites ◽  
Anterior Pituitary ◽  
Binding Capacity ◽  
Relative Effectiveness ◽  
Binding Activity ◽  
Rat Tissues ◽  
Hormone Binding ◽  
Cytosol Fraction ◽  
Binding Interactions

ABSTRACT Thyroxine (T4) and triiodothyronine (T3)-binding interactions in preparations of rat anterior pituitary gland have been studied. T4 is bound primarily to extranuclear binding sites located in the cytosol fraction of the cell. These sites have a medium affinity for T4: Ka = 2.5 × 108 1/mol and a maximum binding capacity (MBC) of 1.15 pmol/mg tissue (wet weight). Binding of T3 to these sites is minimal. The extent of binding of T4 is influenced by the pH of the system and the temperature of incubation. The relative effectiveness of T4 analogues in displacing bound T4 is tetrac > T4 > triac > D-T4 > T3. Similar T4-binding sites are present in other rat tissues, but in all except serum, binding activity is lower than in the pituitary. T4-binding by serum contaminating the pituitary preparations contributed only partially to the total activity observed. Concomitant assessment of T4-binding activity and T4 metabolism in pituitary homogenates prepared at different pH values indicated an inverse relationship between the two processes. The possible role of thyroid hormone binding in cytosol in influencing the intracellular distribution of thyroid hormones is discussed.

scholarly journals The changes in hepatic enzyme expression caused by selenium deficiency and hypothyroidism in rats are produced by independent mechanisms

1990 ◽  
Vol 266 (3) ◽  
pp. 743-747 ◽  
Author(s):  
G J Beckett ◽  
F Nicol ◽  
D Proudfoot ◽  
K Dyson ◽  
G Loucaides ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Malic Enzyme ◽  
Selenium Deficiency ◽  
Hepatic Enzyme ◽  
Enzyme Expression ◽  
Glutathione S Transferase ◽  
Plasma Enzymes ◽  
Glycerophosphate Dehydrogenase ◽  
Se Deficiency ◽  
Gst Activity

Selenium (Se) deficiency for 5 weeks in rats produced changes in the activity of a number of hepatic, renal and plasma enzymes. In animals whose food intake was restricted to 75% of normal for 2 weeks, Se deficiency produced significant increases in the activity of hepatic cytosolic ‘malic’ enzyme and mitochondrial alpha-glycerophosphate dehydrogenase (GPD), two enzymes that are particular sensitive to the thyroid-hormone concentrations in tissue. Propylthiouracil-induced hypothyroidism produced significant decreases in ‘malic’ enzyme and GPD activities. The effect of hypothyroidism on the activity of ‘malic’ enzyme, GPD and other enzymes studied in liver and plasma was often opposite to that seen in Se deficiency. Glutathione S-transferase (GST) activity was increased by both Se deficiency and hypothyroidism, but in hypothyroid animals further significant increases in GST were produced by Se deficiency. These data suggest that the changes in enzyme expression observed in Se deficiency are not caused by decreased tissue exposure to thyroid hormones.

scholarly journals Rapid stimulation of hepatic oxygen consumption by 3,5-di-iodo-l-thyronine

1989 ◽  
Vol 261 (3) ◽  
pp. 945-950 ◽  
Author(s):  
C Horst ◽  
H Rokos ◽  
H J Seitz
Keyword(s):  
Oxygen Consumption ◽  
Thyroid Hormone ◽  
Malic Enzyme ◽  
Mitochondrial Pathway ◽  
Mitochondrial Activity ◽  
O2 Consumption ◽  
Hepatic Oxygen Consumption ◽  
Rapid Stimulation ◽  
Stimulation Of

Tri-iodothyronine (T3) and thyroxine (T4) as well as 3,5-di-iodothyronine (T2) stimulated O2 consumption by isolated perfused livers from hypothyroid rats at a concentration as low as 1 pM by about 30% within 90 min. Application of T2 resulted in a faster stimulation than with application of T3 or T4. Inhibition of iodothyronine monodeiodinase by propylthiouracil, thereby blocking the degradation of T4 to T3 and of T3 to T2, demonstrated that only T2 is the active hormone for the rapid stimulation of hepatic O2 consumption: T3 and T4 lost all of their stimulative activity, whereas T2 was as potent as in the absence of propylthiouracil. Perfusion experiments with thyroid-hormone analogues confirmed the specificity of the T2 effect. The nucleus is unlikely to contribute to the rapid T2 effect, as can be deduced from perfusion experiments with cycloheximide and lack of induction of malic enzyme by T2. In conclusion, a new scheme of regulation of mitochondrial activity is proposed: T2 acts rapidly and directly via a mitochondrial pathway, whereas T3 exerts its long-term action indirectly by induction of specific enzymes.

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