Abstract:
:The deposition of amyloid beta protein (Abeta), a proteolytic cleavage product of amyloid precursor protein (APP), is an invariable pathological feature of the Alzheimer's disease brain, while APP gene is widely expressed in all neuronal and non-neuronal tissues with the highest levels of expression in the brain, and kidney. To understand the role transthyretin (TTR) plays in the sequestration mechanism of Abeta in the kidney, we have investigated interactions of TTR with Abeta1-40 and Abeta1-42 molecules by an immunoprecipitation method, in vitro binding studies, and overlay assay. These in vivo and in vitro biochemical experiments showed that TTR bound Abeta1-42 preferentially, and Abeta1-40 only to a limited extent, to form TTR-monomer and -dimer-Abeta complexes in the normal human kidney. We provide new evidence supporting the hypothesis that TTR, an Abeta binding protein, plays an important role in the sequestration of Abeta and prevents amyloid formation in the kidney.
journal_name
Neurosci Lettjournal_title
Neuroscience lettersauthors
Tsuzuki K,Fukatsu R,Yamaguchi H,Tateno M,Imai K,Fujii N,Yamauchi Tdoi
10.1016/s0304-3940(00)00834-xkeywords:
subject
Has Abstractpub_date
2000-03-10 00:00:00pages
171-4issue
2-3eissn
0304-3940issn
1872-7972pii
S030439400000834Xjournal_volume
281pub_type
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