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PMID: 17913701 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A block of autophagy in lysosomal storage disorders.

Human molecular genetics ·Vol. 17 ·No. 1 ·2008-01-01 ·Pages 119-29

Settembre C, Fraldi A, Jahreiss L, Spampanato C, Venturi C, Medina D, de Pablo R, Tacchetti C, Rubinsztein DC, Ballabio A

Abstract

Most lysosomal storage disorders (LSDs) are caused by deficiencies of lysosomal hydrolases. While LSDs were among the first inherited diseases for which the underlying biochemical defects were identified, the mechanisms from enzyme deficiency to cell death are poorly understood. Here we show that lysosomal storage impairs autophagic delivery of bulk cytosolic contents to lysosomes. By studying the mouse models of two LSDs associated with severe neurodegeneration, multiple sulfatase deficiency (MSD) and mucopolysaccharidosis type IIIA (MPSIIIA), we observed an accumulation of autophagosomes resulting from defective autophagosome-lysosome fusion. An impairment of the autophagic pathway was demonstrated by the inefficient degradation of exogenous aggregate-prone proteins (i.e. expanded huntingtin and mutated alpha-synuclein) in cells from LSD mice. This impairment resulted in massive accumulation of polyubiquitinated proteins and of dysfunctional mitochondria which are the putative mediators of cell death. These data identify LSDs as 'autophagy disorders' and suggest the presence of common mechanisms in the pathogenesis of these and other neurodegenerative diseases.

MeSH Terms
Animals Autophagy/genetics,physiology Base Sequence Cells, Cultured DNA Primers/genetics Humans Lysosomal Storage Diseases/genetics,pathology,physiopathology Lysosomal Storage Diseases, Nervous System/genetics,pathology,physiopathology Lysosomes/pathology Membrane Fusion Mice Microtubule-Associated Proteins/genetics,metabolism Mitochondria/pathology Mucopolysaccharidosis III/genetics,pathology,physiopathology Multiple Sulfatase Deficiency Disease/genetics,pathology,physiopathology Nerve Degeneration/genetics,pathology,physiopathology Phagosomes/pathology Transfection Ubiquitination
Chemicals
DNA Primers MAP1LC3A protein, human Microtubule-Associated Proteins
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Settembre Carmine
Telethon Institute of Genetics and Medicine (TIGEM), Naples, Italy.
Fraldi Alessandro
Jahreiss Luca
Spampanato Carmine
Venturi Consuelo
Medina Diego
de Pablo Raquel
Tacchetti Carlo
Rubinsztein David C
Ballabio Andrea
Article Info
Journal
Human molecular genetics
Abbr.
Hum Mol Genet
ISSN
0964-6906
Published
2008-01-01
Epub
2007-00-03
Pages
119-29
Language
English
Region
England
NLM ID
9208958
Subset
IM
Grants
Wellcome Trust · 064354 · United Kingdom
Medical Research Council · G0600194 · United Kingdom
Medical Research Council · G0600194(77639) · United Kingdom
Telethon · GTF03001 · Italy
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