Journal
EXPERIMENTAL GERONTOLOGY
Volume 42, Issue 1-2, Pages 120-128Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.exger.2006.05.019
Keywords
protein conformational disorders; chaperones; lysosomes; proteases; Parkinson disease
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Funding
- NIA NIH HHS [AG021904, AG19834] Funding Source: Medline
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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 confortnational 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. (c) 2006 Elsevier Inc. All rights reserved.
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