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Articles by Ellen Sapp
Blocking somatic repeat expansion and lowering huntingtin by RNAi synergize to attenuate Huntington’s disease pathogenesis in mice
Editor’s summary Abstract Supplementary Materials REFERENCES AND NOTES Information & Authors Metrics & Citations Check Access References Figures Tables Media Share Editor’s summary The DNA repair protein MSH3 drives somatic CAG repeat expansion in the huntingtin gene (HTT), and both MSH3 and HTT are key of RNA therapeutics for Huntington’s disease (HD). In a series of experiments in a mouse model of HD, Belgrad et al.
Intrastriatal delivery of a zinc finger protein targeting the mutant HTT gene obviates lipid phenotypes in zQ175DN HD mice
Abstract Abstract: Reducing the burden of mutant Huntingtin (mHTT) protein in brain cells is a strategy for treating Huntington's disease (HD). However, it is still unclear what pathological changes can be reproducibly reversed by mHTT lowering. We previously found that lipid changes that occur with HD progression could be prevented by attenuating HTT transcription of the mutant allele in a genetic mouse model (LacQ140) with inducible whole body lowering.
Chronic pharmacologic manipulation of dopamine transmission ameliorates metabolic disturbance in trappc9-linked brain developmental syndrome
ResearchMetabolismNeuroscience Open Access | 10.1172/jci.insight.181339 JCI Insight. https://doi.org/10.1172/jci.insight.181339. Copyright © 2024, Li et al. This work is licensed under the Creative Commons Attribution 4.0 International License. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
mRNA nuclear clustering leads to a difference in mutant huntingtin mRNA and protein silencing by siRNAs in vivo
Abstract Huntington's disease (HD) is an autosomal dominant neurodegenerative disease caused by CAG repeat expansion in the first exon of the huntingtin gene (HTT). Oligonucleotide therapeutics, such as short interfering RNA (siRNA), reduce levels of huntingtin mRNA and protein in vivo and are considered a viable therapeutic strategy. However, the extent to which they silence HTT mRNA in the nucleus is not established.
Chronic pharmacologic manipulation of dopamine transmission ameliorates metabolic disturbance in syndrome caused by mutated trappc9
Abstract Loss-of-function mutations of the gene encoding the trafficking protein particle complex subunit 9 (trappc9) cause intellectual disability and obesity by unknown mechanisms. Genome-wide analysis links trappc9 to non-alcoholic fatty liver disease (NAFLD). The abrogation of trappc9 in mice has been shown to alter the density of neurons containing dopamine receptor D2 (DRD2) and/or DRD1 in the striatum.
Nacc1 mutation in mice models rare neurodevelopmental disorder with underlying synaptic dysfunction
Nacc1 mutation in mice models rare neurodevelopmental disorder with underlying synaptic dysfunction Mark A. Deehan, Josine M. Kothuis, Ellen Sapp, Kathryn Chase, Yuting Ke, Connor Seeley, Maria Iuliano, Emily Kim, Lori Kennington, Rachael Miller, Adel Boudi, Kai Shing, Xueyi Li, Edith Pfister, Christelle Anaclet, Michael Brodsky, Kimberly Kegel-Gleason, Neil Aronin, Marian DiFiglia Journal of Neuroscience 22 February 2024, e1610232024; DOI: 10.1523/JNEUROSCI.1610-23.2024
Trappc9 deficiency causes obesity and fatty liver disease by constraining dopamine neurotransmission
Abstract Loss-of-function mutations of the gene encoding the trafficking protein particle complex subunit 9 (trappc9) cause intellectual disability and obesity by unknown mechanisms. Genome-wide analysis links trappc9 to non-alcoholic fatty liver disease (NAFLD). Trappc9-deficient mice gain body weight normally in early developmental periods but become overweight shortly after being weaned.
Early whole-body mutant huntingtin lowering averts changes in proteins and lipids important for synapse function and white matter maintenance in the LacQ140 mouse model
Abstract Expansion of a triplet repeat tract in exon1 of the HTT gene causes Huntington's disease (HD). The mutant HTT protein (mHTT) has numerous aberrant interactions with diverse, pleiomorphic effects. No disease modifying treatments exist but lowering mutant huntingtin (mHTT) by gene therapy is a promising approach to treat Huntington's disease (HD). It is not clear when lowering should be initiated, how much lowering is necessary and for what duration lowering should occur to achieve benefits.
Early whole-body mutant huntingtin lowering preserves proteins and lipids important for synapse function and white matter maintenance in the LacQ140 mouse model
Abstract Lowering mutant huntingtin (mHTT) transcription is a promising approach to treat Huntington's disease (HD). Using a mHtt-inducible mouse model we analyzed mHtt lowering initiated at different ages and sustained for different time-periods. mHTT protein in cytoplasmic and synaptic compartments of the caudate putamen, which is most affected in HD, was reduced 38-52%. Little or no lowering of mHTT occurred in nuclear and perinuclear regions where aggregates formed at 12 months of age.
Huntingtin associates with the actin cytoskeleton and α-actinin isoforms to influence stimulus dependent morphology changes
Loading metrics Open Access Peer-reviewed Research Article Adelaide Tousley, Maria Iuliano, Elizabeth Weisman, Ellen Sapp, Heather Richardson, Petr Vodicka, Jonathan Alexander, Neil Aronin, Marian DiFiglia, Kimberly B. Kegel-Gleason Adelaide Tousley, Maria Iuliano, Elizabeth Weisman, Ellen Sapp, Heather Richardson, Petr Vodicka, Jonathan Alexander, Neil Aronin, Marian DiFiglia, Kimberly B.
The COOH-terminal domain of huntingtin interacts with RhoGEF kalirin and modulates cell survival
In previous studies, we showed that optineurin and Htt are associated with inactive Rab11 and others demonstrated that optineurin, named as FIP-2, interacts with Htt12,13. We used association with inactive Rab11 to search for other potential Htt interacting proteins. By mass spectrometry, we identified RhoGEF kalirin from proteins precipitated by inactive GST-Rab11 (data not shown).
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