Thyroxine Binding Prealbumin, also known as transthyretin (TTR), is a protein synthesized primarily in the liver and secreted into the bloodstream. It plays a crucial role in the transport of the thyroid hormones, thyroxine (T4) and triiodothyronine (T3), through the circulation.
The function of Thyroxine Binding Prealbumin is to bind with high affinity to thyroxine, thereby preventing its degradation and enhancing its stability. It ensures the proper distribution of thyroid hormones throughout the body, as these hormones are vital for various physiological processes, including metabolism, growth, development, and thermoregulation.
The name "prealbumin" stems from the fact that it migrates slightly ahead of albumin during electrophoresis techniques, despite its smaller size. This protein consists of four identical subunits that form a globular structure, providing a stable environment for the binding of thyroxine molecules.
Apart from its role in thyroid hormone transport, Thyroxine Binding Prealbumin also binds with retinol-binding protein, aiding in the transport of vitamin A throughout the body. Additionally, it has been implicated in several pathological conditions, including amyloidosis and certain inherited diseases due to mutations in the TTR gene.
Measuring the levels of Thyroxine Binding Prealbumin in blood can provide valuable information about the binding capacity of thyroid hormones and can be useful in diagnosing thyroid-related disorders. Overall, Thyroxine Binding Prealbumin plays a crucial role in maintaining appropriate levels of thyroid hormones in the body, ensuring their effective transport and utilization.
