Proteolytic Degradation of Microtubule-Associated Protein τ by Thrombin
Research output: Contribution to journal › Journal article › Research › peer-review
Deposits in the brain of β-amyloid and tau proteins constitute the two major characteristics of Alzheimer′s disease. It is unknown how the deposits are formed, but several studies have suggested that proteases might play a crucial role. Consequently, the search for proteases responsible for processing tau and amyloid precursor protein has become relevant. Here, the ability of thrombin to process tau in vitro is examined. Thrombin, which is found in blood but presumably also in the nervous system, cleaves tau and generates a stable 25 kDa fragment. Immunoblot and amino acid sequencing reveals that the fragment is derived from the C-terminal of tau, and a microtubule assembly assay shows that it has a reduced capacity to promote microtubule assembly compared with full length tau. © 1994 Academic Press. All rights reserved.
Original language | English |
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Journal | Biochemical and Biophysical Research Communications |
Volume | 201 |
Issue number | 2 |
Pages (from-to) | 716-721 |
Number of pages | 6 |
ISSN | 1522-4724 |
DOIs | |
Publication status | Published - 15 Jun 1994 |
ID: 252063997