scholarly journals Full length mutant huntingtin is required for altered Ca2+ signaling and apoptosis of striatal neurons in the YAC mouse model of Huntington's disease

2008 ◽  
Vol 31 (1) ◽  
pp. 80-88 ◽  
Author(s):  
Hua Zhang ◽  
Qin Li ◽  
Rona K. Graham ◽  
Elizabeth Slow ◽  
Michael R. Hayden ◽  
...  
Keyword(s):  
Mouse Model ◽  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Full Length ◽  
Mutant Huntingtin ◽  
Striatal Neurons

scholarly journals A YAC Mouse Model for Huntington’s Disease with Full-Length Mutant Huntingtin, Cytoplasmic Toxicity, and Selective Striatal Neurodegeneration

Neuron ◽  
1999 ◽  
Vol 23 (1) ◽  
pp. 181-192 ◽  
Author(s):  
J.Graeme Hodgson ◽  
Nadia Agopyan ◽  
Claire-Anne Gutekunst ◽  
Blair R Leavitt ◽  
Fred LePiane ◽  
...  
Keyword(s):  
Mouse Model ◽  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Full Length ◽  
Mutant Huntingtin

N-type Ca2+ channels are affected by full-length mutant huntingtin expression in a mouse model of Huntington's disease

2017 ◽  
Vol 55 ◽  
pp. 1-10 ◽  
Author(s):  
Flavia R. Silva ◽  
Artur S. Miranda ◽  
Rebeca P.M. Santos ◽  
Isabella G. Olmo ◽  
Gerald W. Zamponi ◽  
...  
Keyword(s):  
Mouse Model ◽  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Full Length ◽  
Mutant Huntingtin ◽  
Ca2 Channels

scholarly journals Identification of Full-Length Wild-Type and Mutant Huntingtin Interacting Proteins by Crosslinking Immunoprecipitation in Mice Brain Cortex

2021 ◽  
pp. 1-13
Author(s):  
Karen A. Sap ◽  
Arzu Tugce Guler ◽  
Aleksandra Bury ◽  
Dick Dekkers ◽  
Jeroen A.A. Demmers ◽  
...  
Keyword(s):  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Brain Cortex ◽  
Full Length ◽  
Biological Processes ◽  
Interacting Proteins ◽  
Mutant Huntingtin ◽  
Wild Type ◽  
Mutant Huntingtin Protein ◽  
Mice Brain

Background: Huntington’s disease is a neurodegenerative disorder caused by a CAG expansion in the huntingtin gene, resulting in a polyglutamine expansion in the ubiquitously expressed mutant huntingtin protein. Objective: Here we set out to identify proteins interacting with the full-length wild-type and mutant huntingtin protein in the mice cortex brain region to understand affected biological processes in Huntington’s disease pathology. Methods: Full-length huntingtin with 20 and 140 polyQ repeats were formaldehyde-crosslinked and isolated via their N-terminal Flag-tag from 2-month-old mice brain cortex. Interacting proteins were identified and quantified by label-free liquid chromatography-mass spectrometry (LC-MS/MS). Results: We identified 30 interactors specific for wild-type huntingtin, 14 interactors specific for mutant huntingtin and 14 shared interactors that interacted with both wild-type and mutant huntingtin, including known interactors such as F8a1/Hap40. Syt1, Ykt6, and Snap47, involved in vesicle transport and exocytosis, were among the proteins that interacted specifically with wild-type huntingtin. Various other proteins involved in energy metabolism and mitochondria were also found to associate predominantly with wild-type huntingtin, whereas mutant huntingtin interacted with proteins involved in translation including Mapk3, Eif3h and Eef1a2. Conclusion: Here we identified both shared and specific interactors of wild-type and mutant huntingtin, which are involved in different biological processes including exocytosis, vesicle transport, translation and metabolism. These findings contribute to the understanding of the roles that wild-type and mutant huntingtin play in a variety of cellular processes both in healthy conditions and Huntington’s disease pathology.

scholarly journals Msh2 Acts in Medium-Spiny Striatal Neurons as an Enhancer of CAG Instability and Mutant Huntingtin Phenotypes in Huntington’s Disease Knock-In Mice

PLoS ONE ◽  
2012 ◽  
Vol 7 (9) ◽  
pp. e44273 ◽  
Author(s):  
Marina Kovalenko ◽  
Ella Dragileva ◽  
Jason St. Claire ◽  
Tammy Gillis ◽  
Jolene R. Guide ◽  
...  
Keyword(s):  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Mutant Huntingtin ◽  
Striatal Neurons

scholarly journals Caspase-6 does not contribute to the proteolysis of mutant huntingtin in the HdhQ150 knock-in mouse model of Huntington’s disease

PLoS Currents ◽  
2012 ◽  
Vol 4 ◽  
pp. e4fd085bfc9973 ◽  
Author(s):  
Christian Landles ◽  
Andreas Weiss ◽  
Sophie Franklin ◽  
David Howland ◽  
Gill Bates
Keyword(s):  
Mouse Model ◽  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Mutant Huntingtin ◽  
Caspase 6

scholarly journals Loss of huntingtin function slows synaptic vesicle endocytosis in striatal neurons from the httQ140/Q140 mouse model of Huntington's disease

2020 ◽  
Vol 134 ◽  
pp. 104637 ◽  
Author(s):  
Robyn L. McAdam ◽  
Andrew Morton ◽  
Sarah L. Gordon ◽  
Julia F. Alterman ◽  
Anastasia Khvorova ◽  
...  
Keyword(s):  
Mouse Model ◽  
Huntington's Disease ◽  
Synaptic Vesicle ◽  
Huntington’S Disease ◽  
Striatal Neurons

scholarly journals Loss of the thyroid hormone-binding protein Crym renders striatal neurons more vulnerable to mutant huntingtin in Huntington's disease

2014 ◽  
Vol 24 (6) ◽  
pp. 1563-1573 ◽  
Author(s):  
Laetitia Francelle ◽  
Laurie Galvan ◽  
Marie-Claude Gaillard ◽  
Martine Guillermier ◽  
Diane Houitte ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Binding Protein ◽  
Mutant Huntingtin ◽  
Striatal Neurons ◽  
Hormone Binding ◽  
Hormone Binding Protein

scholarly journals Exaggerated mitophagy: a weapon of striatal destruction in the brain?

2020 ◽  
Vol 48 (2) ◽  
pp. 709-717
Author(s):  
Srinivasa Subramaniam
Keyword(s):  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Mutant Huntingtin ◽  
Striatal Neurons ◽  
Mitochondrial Complex ◽  
Complex Ii ◽  
Nitropropionic Acid ◽  
Striatal Lesion ◽  
The Brain ◽  
3 Nitropropionic Acid

Mechanisms responsible for neuronal vulnerability in the brain remain unclear. Striatal neurons are preferentially damaged by 3-nitropropionic acid (3-NP), a mitochondrial complex-II inhibitor, causing striatal damage reminiscent of Huntington's disease (HD), but the mechanisms of the selectivity are not as well understood. We have discovered that Rhes, a protein enriched in the striatum, removes mitochondria via the mitophagy process. The process becomes intensified in the presence of 3-NP, thereby eliminating most of the mitochondria from the striatum. We put forward the hypothesis that Rhes acts as a ‘mitophagy ligand' in the brain and promotes mitophagy via NIX, a mitophagy receptor. Since Rhes interacts and promotes toxicity in association with mutant huntingtin (mHTT), the genetic cause of HD, it is tempting to speculate on whether the exaggerated mitophagy may be a contributing factor to the striatal lesion found in HD. Thus, Rhes-mediated exaggerated mitophagy may act as a weapon of striatal destruction in the brain.

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