| Literature DB >> 26019327 |
Maria Praggastis1, Brett Tortelli1, Jessie Zhang1, Hideji Fujiwara1, Rohini Sidhu1, Anita Chacko1, Zhouji Chen1, Chan Chung2, Andrew P Lieberman2, Jakub Sikora3, Cristin Davidson3, Steven U Walkley3, Nina H Pipalia4, Frederick R Maxfield4, Jean E Schaffer1, Daniel S Ory5.
Abstract
Niemann-Pick Type C1 (NPC1) disease is a rare neurovisceral, cholesterol-sphingolipid lysosomal storage disorder characterized by ataxia, motor impairment, progressive intellectual decline, and dementia. The most prevalent mutation, NPC1(I1061T), encodes a misfolded protein with a reduced half-life caused by ER-associated degradation. Therapies directed at stabilization of the mutant NPC1 protein reduce cholesterol storage in fibroblasts but have not been tested in vivo because of lack of a suitable animal model. Whereas the prominent features of human NPC1 disease are replicated in the null Npc1(-/-) mouse, this model is not amenable to examining proteostatic therapies. The objective of the present study was to develop an NPC1 I1061T knock-in mouse in which to test proteostatic therapies. Compared with the Npc1(-/-) mouse, this Npc1(tm(I1061T)Dso) model displays a less severe, delayed form of NPC1 disease with respect to weight loss, decreased motor coordination, Purkinje cell death, lipid storage, and premature death. The murine NPC1(I1061T) protein has a reduced half-life in vivo, consistent with protein misfolding and rapid ER-associated degradation, and can be stabilized by histone deacetylase inhibition. This novel mouse model faithfully recapitulates human NPC1 disease and provides a powerful tool for preclinical evaluation of therapies targeting NPC1 protein variants with compromised stability.Entities:
Keywords: NPC1; Niemann-Pick C; cholesterol; lysosomal storage; neurodegeneration; protein misfolding
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Year: 2015 PMID: 26019327 PMCID: PMC4444535 DOI: 10.1523/JNEUROSCI.4173-14.2015
Source DB: PubMed Journal: J Neurosci ISSN: 0270-6474 Impact factor: 6.167