IMMUNOLOGICAL CHARACTERIZATION OF THE REGION OF TAU-PROTEIN THAT IS BOUND TO ALZHEIMER PAIRED HELICAL FILAMENTS

被引：32

作者：

CAPUTO, CB ^{[1
]}

WISCHIK, C ^{[1
]}

NOVAK, M ^{[1
]}

SCOTT, CW ^{[1
]}

BRUNNER, WF ^{[1
]}

DEGARCINI, EM ^{[1
]}

LO, MMS ^{[1
]}

NORRIS, TE ^{[1
]}

SALAMA, AI ^{[1
]}

机构：

[1] MRC, MOLEC BIOL LAB, CAMBRIDGE, ENGLAND

来源：

NEUROBIOLOGY OF AGING | 1992年 / 13卷 / 02期

关键词：

ALZHEIMERS DISEASE; TAU-PROTEIN; PAIRED HELICAL FILAMENT;

D O I：

10.1016/0197-4580(92)90039-Z

中图分类号：

R592 [老年病学]; C [社会科学总论];

学科分类号：

03 ; 0303 ; 100203 ;

摘要：

Tau protein is known to be present in the paired helical filaments (PHFs) of Alzheimer brains. This study investigated the fragments of tau protein that remain bound to pronase-treated PHFs and conditions that lead to the release of these tau fragments from the core structure of the PHF. Antibody 423 reacted with PHFs and with fetal rat tau but not with adult rat tau, pig tau, or recombinant human tau. Three other antibodies that react with the tubulin binding region of tau only reacted with PHFs after they were disrupted with formic acid or guanidine. Other antibodies that recognize tau sequences C terminal to the tubulin binding region also recognized pronase-treated PHFs. Antibodies SM134 and T3P that recognize phosphorylated epitopes were reactive with pronase-treated PHFs. Tau fragments from the PHF were solubilized by acid or guanidine treatment. These findings suggest that the fragments of tau that are bound to PHFs and protected from pronase digestion include sequences from the tubulin binding region to the C terminus of tau. In addition, some of these sequences appear to be conformationally or post-translationally modified.

引用

页码：267 / 274

页数：8

共 36 条

[31] ABERRANT NEUROFILAMENT PHOSPHORYLATION IN ALZHEIMER-DISEASE [J].