Transthyretin properties

Meerts lA, van Zanden JJ, Luijks EA, van Leeuwen-Bol I, Marsh G, Jakobsson E, Bergman A, Brouwer A (2000) Potent competitive interaction of some brominated flame retardants and related compounds with human transthyretin in vitro. Toxicol Sci 56 95-104 Mengel K (1985) Dynamics and availability of major nutrients in soils. Adv Soil Sci 2 67-134 Mercer JW, Cohen RM (1990) A review of immiscible fluids in the subsurface Properties, models, characterization, and remediation. J Contam Hydrol 6 107-163 Mertens JA (2000) Trichloroethylene. In Kirk-Othmer Encyclopedia of Chemical Technology. Wiley New York. Available at http //www.mrw.interscience.wiley.com/emrw/9780471238966/ kirk/article/tricmert.aOl/current/pdf... 

Measurements of the levels of semm proteins such as albumin, transthyretin (also known as prealbumin), transferrin and retinol-binding protein are used as biochemical parameters in the assessment of protein energy malnutrition (Table 17-1). An ideal protein marker should have rapid turnover and present in sufficiently high concentrations in semm to be measured accurately. Transthyretin has these properties it is a sensitive indicator of protein deficiency and is effective in assessing improvement with refeeding. 

Vitamin A is transported m the plasma as retinol bound to a carrier protein, called retinol-binding protein (RBP), which itself forms a complex with the thyroxine-binding protein, known as transthyretin (TTR). This complex exists in equilibrium with free holo-RBP, which can then interact with a specific cell-surface receptor, thereby inducing the release of its retinol to the target cell. Thus, RBP possesses at least three molecular-recognition properties it binds retinol and it interacts with both TTR and the cell-surface receptor (for reviews, see refs. I and 2). 

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