Transthyretin: the servant of many masters |
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Authors: | Joel N Buxbaum Natàlia Reixach |
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Institution: | (1) Molecular and Experimental Medicine Department, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA |
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Abstract: | Transthyretin (TTR) (formerly, thyroxine binding prealbumin) is an evolutionarily conserved serum and cerebrospinal fluid
protein that transports holo-retinol-binding protein and thyroxine. Its serum concentration has been widely used to assess
clinical nutritional status. It is also well known that wild-type transthyretin and approximately 100 different mutants give
rise to a variety of forms of systemic amyloid deposition. It has been suspected and recently established that TTR can suppress
the Alzheimer’s disease phenotype in transgenic animal models of cerebral Aβ deposition. Thus, while TTR is a systemic amyloid
precursor, in the brain it seems to have an anti-amyloidogenic effect. TTR is found in other organs as a result of local synthesis
or transport, suggesting that it may have other, as yet undiscovered, functions. It is possible that its capacity to bind
many classes of compounds allows it to serve as an endogenous detoxifier of molecules with potential pathologic effects. |
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