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P2‐348: Estrogen exhibits anti‐amyloidogenicity for β‐amyloid fibrils in vitro
Author(s) -
Morinaga Akiyoshi,
Hirohata Mie,
Ono Kenjiro,
Yamada Masahito
Publication year - 2008
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2008.05.1425
Subject(s) - estrogen , estriol , in vitro , chemistry , amyloid (mycology) , estrone , testosterone (patch) , fibril , thioflavin , medicine , endocrinology , pharmacology , biochemistry , alzheimer's disease , disease , inorganic chemistry
HPLC followed by mass spec was employed to evaluate human CSF. Results: The 23 amino acid peptide, Bri2-23, released from BRI2 by normal processing inhibits A aggregation in vitro and markedly suppresses cerebral A deposition in AD mouse models. Further analysis demonstrated the presence of Bri2-23 peptide in human CSF suggesting physiologic relevance to human disease as did a separate case control study (see abstract by Fanggeng Zou et al) linking several rare single nucleotide polymorphism (SNP) haplotypes in ITM2b to cases of sporadic AD. Conclusions: Taken together, these studies support the notion that BRI2 functions as part of a novel extracellular protein quality control system that inhibits amyloid formation and identify BRI2 as a novel risk factor and therapeutic target in AD.

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