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

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 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.

DIAGNOSIS TIROID

2016 ◽  
Vol 21 (3) ◽  
pp. 304
Author(s):  
Liong Boy Kurniawan ◽  
Mansyur Arif
Keyword(s):  
Thyroid Hormone ◽  
Laboratory Tests ◽  
Thyroid Disorder ◽  
Functional Tests ◽  
Hormone Binding ◽  
Functional Diagnosis ◽  
Underlying Condition ◽  
Unusual Combination ◽  
The Right ◽  
Underlying Diseases

Thyroid disease often causes unspecific or mild symptoms, so laboratory tests are needed to confirm the functional diagnosis of the thyroid disorder. The laboratory tests which are important to establish the diagnosis of thyroid disorder include: total and free thyroidhormones, its related (thyroid) hormone binding proteins and auto antibodies. The thyroid hormone tests are mostly measured with competitive or sandwich immunoassays and each method can be interfered by several factors. Some drugs may increase or decrease thethyroid functional tests and several factors such as: underlying diseases, age, pregnancy, occurrence of heterophil antibody and auto antibodies may also interfere the thyroid tests results. The interpretation of an unusual combination from thyroid stimulating hormonesuch as free thyroxin and tri-iodothyronine results needs confirmation of underlying condition for establishing the right diagnosis. This review is aimed to evaluate several factors which may influence the thyroid tests and interpretation.

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