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The τ Protein in Human Cerebrospinal Fluid in Alzheimer's Disease Consists of Proteolytically Derived Fragments
Author(s) -
Johnson Gail V. W.,
Seubert Peter,
Cox Teresa M.,
Motter Ruth,
Brown Jason P.,
Galasko Douglas
Publication year - 1997
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1997.68010430.x
Subject(s) - cerebrospinal fluid , immunoprecipitation , alzheimer's disease , phosphatase , biology , pathology , disease , tau protein , microbiology and biotechnology , medicine , endocrinology , biochemistry , gene , phosphorylation
Previous studies have shown that the levels of the microtubule‐associated protein τ in the CSF of patients with Alzheimer's disease (AD) are elevated compared with age‐matched controls. In spite of these findings, the nature of τ in CSF has not been well documented. In the present study, τ was immunoprecipitated from CSF of patients with AD or acute stroke, as well as normal elderly controls, followed by immunoblot analysis. In all cases, CSF τ consisted primarily of a band migrating at 26–28 kDa. In AD and stroke patients, several smaller τ fragments were also detected. No intact τ was detected in any of the CSF samples examined. Further immunoprecipitation studies showed that the majority of the τ fragments contained the amino terminus of the molecule. Treatment of CSF τ with alkaline phosphatase did not alter the electrophoretic properties of the fragments. These studies clearly demonstrate that CSF τ is truncated rather than intact.