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Mitochondrial aconitase is a transglutaminase 2 substrate: transglutamination is a probable mechanism contributing to high-molecular-weight aggregates of aconitase and loss of aconitase activity in Huntington disease brain.

Authors: Kim, SY  Marekov, L  Bubber, P  Browne, SE  Stavrovskaya, I  Lee, J  Steinert, PM  Blass, JP  Beal, MF  Gibson, GE  Cooper, AJ 
Citation: Kim SY, etal., Neurochem Res. 2005 Oct;30(10):1245-55.
Pubmed: (View Article at PubMed) PMID:16341586
DOI: Full-text: DOI:10.1007/s11064-005-8796-x

Transglutaminase activity was found to be present in highly purified non-synaptosomal rat brain mitochondria. A 78-kDa protein in these organelles was shown to be a transglutaminase 2 substrate, and incubation of a non-synaptosomal mitochondrial lysate with transglutaminase 2 yielded high-Mr proteins. The 78-kDa protein was identified as mitochondrial aconitase by MALDI-TOF analysis. Aconitase activity was decreased in a dose-dependent manner when non-synaptosomal rat brain mitochondria were incubated with transglutaminase 2. Transglutaminase activity is increased about 2-fold in the mitochondrial fraction of HD caudate. Moreover, Western blotting of the mitochondrial fraction revealed that most of the mitochondrial aconitase in HD caudate is present as high-Mr aggregates. Aconitase activity was previously shown to be decreased in Huntington disease (HD) caudate (a region severely damaged by the disease). The present findings suggest that an increase of transglutaminase activity in HD caudate may contribute to mitochondrial dysfunction by incorporating aconitase into inactive polymers.


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CRRD Object Information
CRRD ID: 1579955
Created: 2006-06-02
Species: All species
Last Modified: 2006-06-02
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.