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A single pathway targets several health challenges of the elderly.

Abstract
New avenues to modulate the autophagy-lysosomal route of protein clearance have the potential to help treat several disease states to which the elderly are particularly vulnerable. Two recent papers identified distinct ways to tap into the lysosomal degradation pathway of autophagy to reduce age-related protein accumulation events. Shoji-Kawata et al. (Nature 2013;494:201-206) describe a new autophagy-inducing peptide, Tat-Beclin 1, that enhances the clearance of polyglutamine aggregates related to Huntington's disease and, interestingly, suppresses viral and bacterial infections. Savolainen et al. (Neurobiol Dis 2014;68:1-15) describe a prolyl oligopeptidase inhibitor that reduces α-synuclein species related to Parkinson's disease and other α-synucleinopathies, and this inhibitor caused a concomitant increase in autophagic activation markers. Previous studies have also linked the autophagy-lysosomal pathway to the protective clearing of the Aβ peptides of Alzheimer's disease and tau species of tauopathies. Enhancing autophagy-lysosomal efficiency may provide a therapeutic avenue for diverse types of proteinopathies, including the most common neurodegenerative disorders of the elderly.
AuthorsBen A Bahr
JournalRejuvenation research (Rejuvenation Res) Vol. 17 Issue 4 Pg. 382-4 (Aug 2014) ISSN: 1557-8577 [Electronic] United States
PMID24953230 (Publication Type: Journal Article, Comment)
Chemical References
  • Apoptosis Regulatory Proteins
  • Membrane Proteins
  • Peptide Fragments
  • Serine Proteinase Inhibitors
  • alpha-Synuclein
  • Proline
  • Serine Endopeptidases
Topics
  • Animals
  • Apoptosis Regulatory Proteins (chemistry, therapeutic use)
  • Autophagy (drug effects)
  • Brain Diseases (genetics)
  • Humans
  • Membrane Proteins (chemistry, therapeutic use)
  • Peptide Fragments (chemistry, pharmacology)
  • Proline (analogs & derivatives)
  • Serine Endopeptidases (metabolism)
  • Serine Proteinase Inhibitors (therapeutic use)
  • alpha-Synuclein (metabolism)

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