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Differences in structure and function between human and murine tau.

Félix Hernández1, Raquel Cuadros1, Ivanna Ollá1

  • 1Department of Molecular Neuropathology, Centro de Biología Molecular "Severo Ochoa" (CBMSO), CSIC-UAM, Madrid, Spain; Network Center for Biomedical Research on Neurodegenerative Diseases (CIBERNED), Madrid, Spain.

Biochimica Et Biophysica Acta. Molecular Basis of Disease
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PubMed
Summary
This summary is machine-generated.

Human tau protein residues 17-28 bind to energy-related proteins like enolase and creatine kinase B. This binding is impaired in Alzheimer's disease (AD) brain extracts, possibly due to creatine kinase B oxidation.

Keywords:
Alzheimer diseaseCreatine kinaseTau

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Area of Science:

  • Neuroscience
  • Protein Biochemistry

Background:

  • Human and mouse tau proteins differ in N-terminal residues (17-28).
  • Tau protein is implicated in neurodegenerative diseases like Alzheimer's disease (AD).

Purpose of the Study:

  • To investigate the binding capacity of human tau residues 17-28 to other proteins.
  • To determine if Alzheimer's disease (AD) affects the binding of these proteins to tau.

Main Methods:

  • Peptide-based protein binding assays using specific human tau N-terminal residues.
  • Analysis of tau protein interactions in brain extracts from AD patients.

Main Results:

  • Human tau residues 17-28 bind to several proteins, notably enolase, glyceraldehyde 3 phosphate dehydrogenase, and creatine kinase B (CKB).
  • CKB binding to tau was significantly reduced in brain extracts from AD patients compared to controls.
  • Oxidative modification of CKB may explain the reduced binding in AD.

Conclusions:

  • The N-terminal region of human tau (residues 17-28) interacts with key metabolic enzymes.
  • Altered tau-protein interactions, specifically with CKB, may contribute to the pathophysiology of Alzheimer's disease (AD).
  • CKB oxidation is a potential mechanism for impaired tau binding in AD.