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.

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Abstrakt

Tytuł:: 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.
Autorzy:: Kim SY; Department of Neurology and Neuroscience, Weill Medical College of Cornell University, New York, NY 10021, USA.
Marekov L
Bubber P
Browne SE
Stavrovskaya I
Lee J
Steinert PM
Blass JP
Beal MF
Gibson GE
Cooper AJ
Źródło:: Neurochemical research [Neurochem Res] 2005 Oct; Vol. 30 (10), pp. 1245-55.
Typ publikacji:: Journal Article; Research Support, N.I.H., Extramural
Język:: English
Imprint Name(s):: Publication: 1999- : New York, NY : Kluwer Academic/Plenum Publishers
Original Publication: New York, Plenum Press
MeSH Terms:: Aconitate Hydratase*/chemistry
Aconitate Hydratase*/metabolism
Brain/*enzymology
GTP-Binding Proteins/*metabolism
Huntington Disease/*metabolism
Mitochondria/*enzymology
Transglutaminases/*metabolism
Animals ; Brain/anatomy & histology ; Brain/pathology ; Humans ; Huntington Disease/pathology ; Mice ; Molecular Weight ; Peptides/genetics ; Peptides/metabolism ; Protein Glutamine gamma Glutamyltransferase 2 ; Rats ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Subcellular Fractions/metabolism
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Grant Information:: AG19589 United States AG NIA NIH HHS; P01 AG14930 United States AG NIA NIH HHS; R24-MH 068855 United States MH NIMH NIH HHS
Substance Nomenclature:: 0 (Peptides)
0 (Tgm2 protein, rat)
EC 2.3.2.13 (Protein Glutamine gamma Glutamyltransferase 2)
EC 2.3.2.13 (Transglutaminases)
EC 3.6.1.- (GTP-Binding Proteins)
EC 4.2.1.3 (Aconitate Hydratase)
Entry Date(s):: Date Created: 20051213 Date Completed: 20060223 Latest Revision: 20220309
Update Code:: 20240104
DOI:: 10.1007/s11064-005-8796-x
PMID:: 16341586
: Czasopismo naukowe

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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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