Proteolysis of tau by calpain

Gail V.W. Johnson, Richard S. Jope, Lester I. Binder

Research output: Contribution to journalArticle

145 Scopus citations

Abstract

The calpain-induced proteolysis of tau associated with twice-cycled microtubules or from a total brain heat-stable fraction was studied. Twice-cycled microtubule tau was rapidly hydrolyzed by calpain. In contrast, tau purified from the total brain heat-stable fraction was very resistant to degradation by calpain. These results clearly demonstrate that there are at least 2 populations of tau in the brain based on calpain-sensitivity, a calpain-sensitive form that is associated with microtubules and a calpain-resistant form that may represent another population of tau in the brain.

Original languageEnglish (US)
Pages (from-to)1505-1511
Number of pages7
JournalBiochemical and biophysical research communications
Volume163
Issue number3
DOIs
StatePublished - Sep 29 1989
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Proteolysis of tau by calpain'. Together they form a unique fingerprint.

  • Cite this