Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 66, Issue 19, Pages 3095-3101Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-009-0109-0
Keywords
Transthyretin; Amyloidosis; Alzheimer's disease; Retinol binding protein; Albumin; Detoxification
Categories
Funding
- National Institute on Aging [R01 AG30027, R01 AG19259]
- W. M. Keck Foundation
- American Heart Association BGIA award [0865061F]
- NATIONAL INSTITUTE ON AGING [R01AG030027, R01AG019259] Funding Source: NIH RePORTER
Ask authors/readers for more resources
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 A beta 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available