Transglutaminase 6 Is Colocalized and Interacts with Mutant Huntingtin in Huntington Disease Rodent Animal Models.

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Abstrakt

Tytuł:: Transglutaminase 6 Is Colocalized and Interacts with Mutant Huntingtin in Huntington Disease Rodent Animal Models.
Autorzy:: Schulze-Krebs A; Experimental Therapy, Preclinical Experimental Center, University Hospital Erlangen (UKEr), Friedrich-Alexander-University Erlangen-Nürnberg (FAU), 91054 Erlangen, Germany.
Canneva F; Experimental Therapy, Preclinical Experimental Center, University Hospital Erlangen (UKEr), Friedrich-Alexander-University Erlangen-Nürnberg (FAU), 91054 Erlangen, Germany.
Stemick J; Department of Molecular Neurology, University Hospital Erlangen (UKEr), Friedrich-Alexander-University Erlangen-Nürnberg (FAU), 91054 Erlangen, Germany.
Plank AC; Experimental Therapy, Preclinical Experimental Center, University Hospital Erlangen (UKEr), Friedrich-Alexander-University Erlangen-Nürnberg (FAU), 91054 Erlangen, Germany.
Harrer J; Experimental Therapy, Preclinical Experimental Center, University Hospital Erlangen (UKEr), Friedrich-Alexander-University Erlangen-Nürnberg (FAU), 91054 Erlangen, Germany.
Bates GP; Huntington's Disease Centre, Department of Neurodegenerative Disease and UK Dementia Research Institute at UCL, Queen Square Institute of Neurology, University College London, London WC1N 3BG, UK.
Aeschlimann D; Matrix Biology and Tissue Repair Research Unit, College of Biomedical and Life Sciences, School of Dentistry, Cardiff University, Cardiff CF14 4XY, UK.
Steffan JS; Institute of Memory Impairments and Neurological Disorders, University of California, Irvine, CA 92697, USA.; Department of Psychiatry and Human Behavior, University of California, Irvine, CA 92697, USA.
von Hörsten S; Experimental Therapy, Preclinical Experimental Center, University Hospital Erlangen (UKEr), Friedrich-Alexander-University Erlangen-Nürnberg (FAU), 91054 Erlangen, Germany.
Źródło:: International journal of molecular sciences [Int J Mol Sci] 2021 Aug 18; Vol. 22 (16). Date of Electronic Publication: 2021 Aug 18.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Original Publication: Basel, Switzerland : MDPI, [2000-
MeSH Terms:: Disease Models, Animal*
Mutation*
Huntingtin Protein/*metabolism
Huntington Disease/*pathology
Mutant Proteins/*metabolism
Neurons/*metabolism
Transglutaminases/*metabolism
Animals ; Huntingtin Protein/genetics ; Huntington Disease/genetics ; Huntington Disease/metabolism ; Mice ; Mice, Transgenic ; Mutant Proteins/genetics ; Rats ; Transglutaminases/genetics
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Grant Information:: 01ED1501C Bundesministerium für Bildung und Forschung
Contributed Indexing:: Keywords: Huntington disease; neurodegeneration; rodent transgenic animal models; transglutaminase isoform 6
Substance Nomenclature:: 0 (Huntingtin Protein)
0 (Mutant Proteins)
EC 2.3.2.13 (Transglutaminases)
Entry Date(s):: Date Created: 20210827 Date Completed: 20210920 Latest Revision: 20240403
Update Code:: 20240403
PubMed Central ID:: PMC8396294
DOI:: 10.3390/ijms22168914
PMID:: 34445621
: Czasopismo naukowe

Pełny tekst

Mammalian transglutaminases (TGs) catalyze calcium-dependent irreversible posttranslational modifications of proteins and their enzymatic activities contribute to the pathogenesis of several human neurodegenerative diseases. Although different transglutaminases are found in many different tissues, the TG6 isoform is mostly expressed in the CNS. The present study was embarked on/undertaken to investigate expression, distribution and activity of transglutaminases in Huntington disease transgenic rodent models, with a focus on analyzing the involvement of TG6 in the age- and genotype-specific pathological features relating to disease progression in HD transgenic mice and a tgHD transgenic rat model using biochemical, histological and functional assays. Our results demonstrate the physical interaction between TG6 and (mutant) huntingtin by co-immunoprecipitation analysis and the contribution of its enzymatic activity for the total aggregate load in SH-SY5Y cells. In addition, we identify that TG6 expression and activity are especially abundant in the olfactory tubercle and piriform cortex, the regions displaying the highest amount of mHTT aggregates in transgenic rodent models of HD. Furthermore, mHTT aggregates were colocalized within TG6-positive cells. These findings point towards a role of TG6 in disease pathogenesis via mHTT aggregate formation.

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