Thyroid hormone binding in serum of 15 vertebrate species: isolation of thyroxine-binding globulin and prealbumin analogs.
Abstract: The binding of [125I]T4 to serum proteins was studied in human, monkey, cattle, sheep, goat, water buffalo, horse, swine, dog, cat, rabbit, rat, chicken, frog, and salmon. Attempts were made to isolate thyroxine-binding globulin (TBG) and thyroxine-binding prealbumin (TBPA) from serum of all species, utilizing purification methods based on the specific properties of these proteins. TBPA was found to exist in all species examined. The protein was found anodal to albumin only in human, monkey, horse, and chicken. In cattle, swine, dog, cat, rabbit, frog, and salmon, TBPA was found cathodal to albumin, while sheep, goat, water buffalo, and rat had identical mobility of albumin and TBPA. The presence of TBG was demonstrated in larger mammals. In cat, rabbit, rat, chicken, frog, and salmon, TBG could not be demonstrated. The thyroxine-binding capacity of TBPA in serum varied from 1000 to greater than 6000 nmol/l and that of TBG between 150 and 600 nmol/l. TBPA from all species except salmon showed affinity to human retinol-binding protein. The presence of TBPA in all vertebrates suggests prealbumin to be a far more important thyroxine carrier than earlier anticipated.
Publication Date: 1985-06-01 PubMed ID: 3924724DOI: 10.1016/0016-6480(85)90108-xGoogle Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research studied the binding of a specific thyroid hormone to serum proteins in 15 different vertebrate species. The researchers additionally attempted to isolate specific types of thyroid hormone-binding proteins, presenting new understandings on the importance of prealbumin as these proteins appeared to be present in all the species studied.
Thyroid Hormone Binding Study
- The main focus of the research was to investigate how the thyroid hormone, specifically thyroxine (T4), binds to serum proteins in a wide range of vertebrates, including humans, monkeys, various types of livestock and domestic animals, as well as reptiles and fish.
- The rationale was to gain a better understanding of how thyroid hormones are carried in the blood across different species, an important aspect of endocrine physiology that could shed light on evolutionary adaptations and implications for disease.
Isolation of Thyroid Hormone Binding Proteins
- Two types of proteins capable of binding thyroxine were targeted for isolation from the serum of each species: thyroxine-binding globulin (TBG) and thyroxine-binding prealbumin (TBPA).
- The isolation process was designed around the specific properties of these proteins, with TBPA found to exist in all species studied. However, where TBPA was found in relation to albumin—a commonly used protein marker in such studies—varied.
- In humans, monkeys, horses, and chickens, TBPA was located anodal to albumin, meaning it migrated towards the positive electrode in the electrophoretic separation, a method used to tell proteins apart in a complex mixture.
- In contrast, TBPA was found cathodal to albumin, moving towards the negative electrode, in cattle, swine, dogs, cats, rabbits, frogs, and salmon. Identical mobility of albumin and TBPA was observed in sheep, goats, water buffaloes, and rats.
Different Findings for TBG
- The presence of TBG was confirmed in larger mammals but could not be demonstrated in cats, rabbits, rats, chickens, frogs, and salmon, suggesting variations in thyroid hormone transport mechanisms between these groups of species.
- The capacity of the serum protein TBPA to bind thyroxine varied widely from 1,000 to over 6,000 nmol/l, while that of TBG was lower, ranging between 150 and 600 nmol/l, indicating that TBPA plays a more substantial role in thyroxine transport.
Significance of the Findings
- The research highlighted the crucial role of TBPA in thyroid hormone transport, suggesting that prealbumin is a more important thyroxine carrier than previously thought based on its presence in all species studied.
- The differences observed in the positioning of TBPA relative to albumin and the inability to demonstrate TBG in certain species provide interesting insights and raise questions about evolutionary adaptations in endocrine transport mechanisms across different groups of vertebrates.
Cite This Article
APA
Larsson M, Pettersson T, Carlström A.
(1985).
Thyroid hormone binding in serum of 15 vertebrate species: isolation of thyroxine-binding globulin and prealbumin analogs.
Gen Comp Endocrinol, 58(3), 360-375.
https://doi.org/10.1016/0016-6480(85)90108-x Publication
Researcher Affiliations
MeSH Terms
- Animals
- Blood Proteins / metabolism
- Buffaloes
- Bufonidae
- Cats
- Cattle
- Chickens
- Chromatography, Affinity
- Dogs
- Electrophoresis
- Female
- Goats
- Horses
- Humans
- Macaca mulatta
- Male
- Prealbumin / isolation & purification
- Prealbumin / metabolism
- Protein Binding
- Rabbits
- Rats
- Salmon
- Sheep
- Species Specificity
- Swine
- Thyroxine / blood
- Thyroxine-Binding Proteins / isolation & purification
- Thyroxine-Binding Proteins / metabolism
Citations
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