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Specific binding of thyroid-stimulating hormone by human serum globulins
The Journal of Endocrinology
|March 1, 1981
Summary
Thyroid stimulating immunoglobulins (TSI) in Graves' disease patients exhibit distinct thyrotropin (TSH) binding properties. Some TSI-positive globulins show similar TSH binding to controls, while others display significantly different binding characteristics.
Area of Science:
- Endocrinology
- Immunology
- Biochemistry
Background:
- Graves' disease is an autoimmune disorder characterized by elevated thyroid stimulating immunoglobulins (TSI).
- Understanding the interaction between TSI and thyrotropin (TSH) is crucial for elucidating disease mechanisms.
Purpose of the Study:
- To investigate the specific thyrotropin (TSH)-binding properties of globulin preparations from patients with Graves' disease and healthy individuals.
- To characterize the nature and affinity of TSH binding sites associated with TSI.
Main Methods:
- Testing globulin preparations from TSI-positive (Graves' disease) and TSI-negative (healthy) individuals for 131I-labelled TSH binding.
- Characterizing binding kinetics, affinity (Kd), maximum binding capacity (Bmax), and influencing factors (pH, incubation time).
- Utilizing chromatography (Sephadex G-200) and electrophoresis (paper electrophoresis) to identify the nature of binding macromolecules.
Main Results:
- Globulins from both patient and control groups demonstrated TSH binding sites.
- TSI-positive globulins exhibited two distinct binding patterns: A-type (similar to controls) and B-type (different affinity and capacity).
- TSH binding was associated with macromolecules migrating with immunoglobulin G (IgG) and was reversible.
Conclusions:
- Specific TSH binding sites are present in globulins from both Graves' disease patients and healthy individuals.
- A subset of Graves' disease patients possesses globulins with unique TSH-binding characteristics, potentially contributing to disease pathogenesis.
- The identified TSH binding sites are linked to immunoglobulin G, suggesting an autoimmune basis for this interaction.