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PMID: 16311254 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy.

Human molecular genetics ·Vol. 15 ·No. 1 ·2006-01-01 ·Pages 23-31

Davies JE, Sarkar S, Rubinsztein DC

Abstract

Oculopharyngeal muscular dystrophy (OPMD) is an autosomal dominant disease that presents in the fifth or sixth decade with dysphagia, ptosis and proximal limb weakness. OPMD is caused by the abnormal expansion of a polyalanine tract within the coding region of polyA binding protein nuclear 1 (PABPN1). The resultant mutant PABPN1 forms aggregates within the nuclei of skeletal muscle fibres. We have previously described a transgenic mouse model of OPMD that recapitulates the human disease and develops progressive muscle weakness accompanied by the formation of aggregates in skeletal muscle nuclei. The chemical chaperone trehalose has been used effectively to alleviate symptoms in a mouse model of Huntington's disease and is thought to elicit its effect by binding and stabilizing partially folded polyglutamine proteins and inhibiting the formation of aggregates. Here, we show that trehalose reduces aggregate formation and toxicity of mutant PABPN1 in cell models. Furthermore, oral administration of trehalose attenuated muscle weakness, reduced aggregate formation and decreased the number of TUNEL-labelled nuclei in skeletal muscle in an OPMD transgenic mouse model. Thus, anti-aggregation therapy may prove effective in the treatment of human OPMD.

MeSH Terms
Analysis of Variance Animals Blotting, Western COS Cells Chlorocebus aethiops In Situ Nick-End Labeling Inclusion Bodies/drug effects Mice Mice, Transgenic Muscle Contraction/physiology Muscle, Skeletal/pathology Muscular Dystrophy, Oculopharyngeal/drug therapy,genetics,pathology Mutation/genetics Poly(A)-Binding Protein II/genetics,metabolism Trehalose/pharmacology,therapeutic use
Chemicals
Poly(A)-Binding Protein II Trehalose
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Davies Janet E
Department of Medical Genetics, Cambridge Institute for Medical Research, Wellcome/MRC Building, Cambridge, UK.
Sarkar Sovan
Rubinsztein David C
Article Info
Journal
Human molecular genetics
Abbr.
Hum Mol Genet
ISSN
0964-6906
Published
2006-01-01
Epub
2005-00-25
Pages
23-31
Language
English
Region
England
NLM ID
9208958
Subset
IM
Grants
Wellcome Trust · United Kingdom
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