Chaperone-mediated autophagy in aging and neurodegeneration: Lessons from α-synuclein

Urmi Bandhyopadhyay, Ana Maria Cuervo

Research output: Contribution to journalArticle

78 Citations (Scopus)

Abstract

Different conditions, ranging from genetic mutation to post-translational modification, result in the intracellular presence of misfolded or conformationally altered proteins. These abnormal proteins tend to organize in toxic oligomeric structures often resulting in cellular death. Alterations in the function of the surveillance systems that normally repair or remove abnormal proteins are the basis of many neurodegenerative disorders. In this review, we focus on such protein conformational disorders and on the role that altered function of intracellular proteolytic systems, in particular autophagy, plays in the evolution of these diseases. Using Parkinson disease as a main example, we recapitulate the different stages of this protein conformational disorder at the cellular level and relate them with changes in the different types of autophagy. Finally, we also comment on the effect that aggravating conditions, such as oxidative stress and aging, have on the functioning of the autophagic system and its ability to cope with altered proteins.

Original languageEnglish (US)
Pages (from-to)120-128
Number of pages9
JournalExperimental Gerontology
Volume42
Issue number1-2
DOIs
StatePublished - Jan 2007

Fingerprint

Synucleins
Autophagy
Aging of materials
Proteins
Oxidative stress
Poisons
Post Translational Protein Processing
Neurodegenerative Diseases
Parkinson Disease
Oxidative Stress
Repair
Mutation

Keywords

  • Chaperones
  • Lysosomes
  • Parkinson disease
  • Proteases
  • Protein conformational disorders

ASJC Scopus subject areas

  • Aging
  • Medicine(all)

Cite this

Chaperone-mediated autophagy in aging and neurodegeneration : Lessons from α-synuclein. / Bandhyopadhyay, Urmi; Cuervo, Ana Maria.

In: Experimental Gerontology, Vol. 42, No. 1-2, 01.2007, p. 120-128.

Research output: Contribution to journalArticle

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