Premium
Effects of different anti‐tau antibodies on tau fibrillogenesis: RTA‐1 and RTA‐2 counteract tau aggregation
Author(s) -
Taniguchi Taizo,
Sumida Miho,
Hiraoka Shuko,
Tomoo Koji,
Kakehi Tomoko,
Minoura Katsuhiko,
Sugiyama Shigeru,
Inaka Koji,
Ishida Toshimasa,
Saito Naoaki,
Tanaka Chikako
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.01.039
Subject(s) - tauopathy , fibrillogenesis , chemistry , tau protein , microtubule , fibril , biophysics , monoclonal antibody , microtubule associated protein , microbiology and biotechnology , biochemistry , antibody , alzheimer's disease , biology , disease , neurodegeneration , medicine , pathology , immunology
Tau is the major antigenic component of neurofibrillary pathology in tauopathy, including Alzheimer's disease. Although conversion of soluble tau to an insoluble polymerized fibrillar form is a key factor in the pathogenesis of tauopathy, the mechanism of the change is unclear and no inhibitors of fibril formation are available. Monoclonal antibodies against the 1st or 2nd repeat of the microtubule binding domain, but not the C‐terminal 16 residues, completely inhibited tau aggregation into PHF. Furthermore, they did not inhibit tau‐induced tubulin assembly. Thus, they are useful to investigate tau protein conversion and will be useful therapeutic lead materials.