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PMID: 2551295 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Proteolysis of tau by calpain.

Biochemical and biophysical research communications ·Vol. 163 ·No. 3 ·1989-09-29 ·Pages 1505-11

Johnson GV, Jope RS, Binder LI

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.

MeSH Terms
Animals Brain/metabolism Calpain/metabolism Cattle Immunoblotting Kinetics Microtubule-Associated Proteins/isolation & purification,metabolism Microtubules/metabolism Nerve Tissue Proteins/metabolism tau Proteins
Chemicals
Microtubule-Associated Proteins Nerve Tissue Proteins tau Proteins Calpain
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Johnson G V
Department of Neurology, University of Alabama, Birmingham 35294.
Jope R S
Binder L I
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1989-09-29
Pages
1505-11
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Grants
NIA NIH HHS · P01-AG06569 · United States
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