AI Article Synopsis
- - The key difference between human and mouse tau proteins lies in the N-terminal region, with human tau having additional residues (17 to 28) that mouse tau lacks.
- - Research revealed that these human tau residues can bind to certain proteins, specifically identifying strong interactions with enolase, glyceraldehyde 3 phosphate dehydrogenase, and creatine kinase B.
- - Notably, creatine kinase B did not bind to tau extracted from Alzheimer's disease patients, possibly due to oxidative modifications affecting its interaction in those cases.
Article Abstract
The main difference between the primary structures of human and mouse tau can be found at the N-terminal end of the protein. Residues 17 to 28 in human tau are not present in the mouse form of the molecule. Here we tested the capacity of these human tau residues to bind to specific proteins. Several proteins were observed to bind to these residues. Among those that showed the greatest binding were three related to energetic processes: enolase, glyceraldehyde 3 phosphate dehydrogenase and creatine kinase B. The latter did not bind to tau from brain extracts taken from patients with Alzheimer's disease (AD). This lack of binding could be due to the modification of CKB by oxidation in AD.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.bbadis.2018.08.010 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!