Linked Life Data

18000397

Source:http://linkedlifedata.com/resource/pubmed/id/18000397

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-12-6
pubmed:abstractText
The cellular turnover of proteins and organelles requires cooperation between the autophagic and the lysosomal degradation pathways. A crucial step in this process is the fusion of the autophagosome with the lysosome. In our study we demonstrate that in Lysosomal Storage Disorders (LSDs) accumulation of undegraded substrates in lysosomes, due to deficiency of specific lysosomal enzymes, impairs the fusion between autophagosomes and lysosomes. This, in turn, leads to a progressive accumulation of poly-ubiquitinated protein aggregates and of dysfunctional mitochondria. These findings suggest that neurodegeneration in LSDs may share some mechanisms with late-onset neurodegenerative disorders in which the accumulation of protein aggregates is a prominent feature.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1554-8635
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-4
pubmed:dateRevised
2011-6-30
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Lysosomal storage diseases as disorders of autophagy.
pubmed:affiliation
Telethon Institute of Genetics and Medicine (TIGEM), Naples, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't