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Characteristics of anti-TSH antibody and its relationship with TSH receptor antibody.

Cho BY, Shong YK, Lee HK, Koh CS, Min HK, Lee M - Korean J. Intern. Med. (1988)

View Article: PubMed Central - PubMed

ABSTRACT

Using the TSH binding inhibition IgG (TBII) assay three patients with Graves’ disease were discovered to have serum TSH-binding immunoglobulins of high affinity. These IgGs bound 61%, 33% and 60% of radiolabeled TSH, respectively, higher than the maximal specific binding (25%) in the TBII assay. Such binding was detected even in the absence of TSH receptor with only small differences in the precipitable radioactivity (61 %, 28%, and 61 %, respectively) compared with non-specific binding (11.3%). The 125I-bTSH binding of IgGs was competitively inhibited by the addition of bTSH. The 7s fraction was found to be a major binding component by gel filtration chromatography. Myxedema sera with high TSH levels did not affect the reaction. Moreover IgG binding to bTSH was not inhibited by the addition of serial dilutions of TBII positive pooled Graves’ IgG (0.1–10mg/ml) from a different untreated patient. The titers of these TSH binding antibodies were not changed during the treatment of Graves’ disease. Following guinea pig fat cell membrane receptor purification, the IgG of one patient with Graves’ disease revealed TBII activity of 46.3%. However, no binding of 125I-bTSH in the absence of the TSH receptor was evident.

These studies suggest that 1) anti-TSH antibodies and TSH receptor antibodies are present independent of one another in the sera of some patients with Graves’ disease, and 2) TSH receptor antibodies do not affect the binding of anti-TSH antibodies to TSH.

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Displacement of PEG-precipitable 125I-bTSH binding by IgGs from patient 1 by bTSH. Incubation was carried out in 100 μl IgG (10mg/ml) and 100μl 125I-bTSH in addition to 100 μl of 10mM Tris/50mM NaCl/0.1% BSA, pH 7.4, containing 1–10 μU/ml bTSH. The insert shows the Scatchard plot of bTSH binding to patient’s IgGs.
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f1-kjim-3-1-1-1: Displacement of PEG-precipitable 125I-bTSH binding by IgGs from patient 1 by bTSH. Incubation was carried out in 100 μl IgG (10mg/ml) and 100μl 125I-bTSH in addition to 100 μl of 10mM Tris/50mM NaCl/0.1% BSA, pH 7.4, containing 1–10 μU/ml bTSH. The insert shows the Scatchard plot of bTSH binding to patient’s IgGs.

Mentions: Addition of unlabelled bTSH produced a concentration-dependent inhibition of the binding of 125I-bTSH by IgGs of all three patients. Scatchand analysis revealed that the IgG of patient 1 bound 125I-bTSH with an association constant of 1.2 × 1010 M−1 and a maximum binding capacity of 6.9 × 10−12M/mg IgG. The binding affinity did not change during antithyroid drug treatment (Fig. 1). Association constants of patients 2 and 3 IgGs were 6.7 × 107 M−1 1.9 × 1010 M−1, respectively, and maximum binding capacities were 5.4 × 10−10, 4.9 × 10−2M/mg IgG, respectively (Table 3).


Characteristics of anti-TSH antibody and its relationship with TSH receptor antibody.

Cho BY, Shong YK, Lee HK, Koh CS, Min HK, Lee M - Korean J. Intern. Med. (1988)

Displacement of PEG-precipitable 125I-bTSH binding by IgGs from patient 1 by bTSH. Incubation was carried out in 100 μl IgG (10mg/ml) and 100μl 125I-bTSH in addition to 100 μl of 10mM Tris/50mM NaCl/0.1% BSA, pH 7.4, containing 1–10 μU/ml bTSH. The insert shows the Scatchard plot of bTSH binding to patient’s IgGs.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4532127&req=5

f1-kjim-3-1-1-1: Displacement of PEG-precipitable 125I-bTSH binding by IgGs from patient 1 by bTSH. Incubation was carried out in 100 μl IgG (10mg/ml) and 100μl 125I-bTSH in addition to 100 μl of 10mM Tris/50mM NaCl/0.1% BSA, pH 7.4, containing 1–10 μU/ml bTSH. The insert shows the Scatchard plot of bTSH binding to patient’s IgGs.
Mentions: Addition of unlabelled bTSH produced a concentration-dependent inhibition of the binding of 125I-bTSH by IgGs of all three patients. Scatchand analysis revealed that the IgG of patient 1 bound 125I-bTSH with an association constant of 1.2 × 1010 M−1 and a maximum binding capacity of 6.9 × 10−12M/mg IgG. The binding affinity did not change during antithyroid drug treatment (Fig. 1). Association constants of patients 2 and 3 IgGs were 6.7 × 107 M−1 1.9 × 1010 M−1, respectively, and maximum binding capacities were 5.4 × 10−10, 4.9 × 10−2M/mg IgG, respectively (Table 3).

View Article: PubMed Central - PubMed

ABSTRACT

Using the TSH binding inhibition IgG (TBII) assay three patients with Graves’ disease were discovered to have serum TSH-binding immunoglobulins of high affinity. These IgGs bound 61%, 33% and 60% of radiolabeled TSH, respectively, higher than the maximal specific binding (25%) in the TBII assay. Such binding was detected even in the absence of TSH receptor with only small differences in the precipitable radioactivity (61 %, 28%, and 61 %, respectively) compared with non-specific binding (11.3%). The 125I-bTSH binding of IgGs was competitively inhibited by the addition of bTSH. The 7s fraction was found to be a major binding component by gel filtration chromatography. Myxedema sera with high TSH levels did not affect the reaction. Moreover IgG binding to bTSH was not inhibited by the addition of serial dilutions of TBII positive pooled Graves’ IgG (0.1–10mg/ml) from a different untreated patient. The titers of these TSH binding antibodies were not changed during the treatment of Graves’ disease. Following guinea pig fat cell membrane receptor purification, the IgG of one patient with Graves’ disease revealed TBII activity of 46.3%. However, no binding of 125I-bTSH in the absence of the TSH receptor was evident.

These studies suggest that 1) anti-TSH antibodies and TSH receptor antibodies are present independent of one another in the sera of some patients with Graves’ disease, and 2) TSH receptor antibodies do not affect the binding of anti-TSH antibodies to TSH.

Show MeSH