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O4–06–07: MMP–9 degrades fibrilllar abeta in vitro and compact plaques In situ
Author(s) -
Lee Jin-Moo,
Hu Xiaoyan,
Crick Scott,
Song Haowei,
Yin Kejie,
Cirrito John,
Bateman Randy,
Hsu Chung Y.,
Xu Jan,
Hsu Fong F.,
Turk John,
Pappu Rohit,
Holtzman David M.,
Yan Ping
Publication year - 2006
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.2006.05.342
Subject(s) - proteases , chemistry , matrix metalloproteinase , protease , enzyme , senile plaques , staining , in vivo , metalloproteinase , in vitro , fluorescence microscope , proteolysis , paraformaldehyde , microbiology and biotechnology , biophysics , biochemistry , fluorescence , pathology , biology , alzheimer's disease , medicine , physics , disease , organic chemistry , quantum mechanics
null background. We are performing A ELISAs, immunoblotting, and immunohisto-chemistry on brains from these mice and their APP transgenic controls collected at 3, 6, and 13 months of age. Results: The absence of NEP results in: a) elevations in the TBS-, NP40-, and guanidine HCl-soluble pools of brain A ; b) marked elevations in hippocampal amyloid plaque burden; and c) a dramatic increase in amyloid angiopathy. We will report further on plasma A levels, A monomer, dimer, and oligomer levels, and the possibility of a NEP gene-dose response. Conclusions: The absence of endogenous NEP in human APP transgenic mice results in elevated levels of brain A , an increased amyloid plaque burden, and the development of amyloid angiopathy.