Document Detail


Aging and regulated protein degradation: who has the UPPer hand?
MedLine Citation:
PMID:  17681036     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In all cells, protein degradation is a constant, ongoing process that is critical for cell survival and repair. The ubiquitin/proteasome pathway (UPP) is the major proteolytic pathway that degrades intracellular proteins in a regulated manner. It plays critical roles in many cellular processes and diseases. Disruption of the UPP is particularly relevant to pathophysiological conditions that provoke the accumulation of aberrant proteins, such as in aging as well as in a variety of neurodegenerative disorders including Alzheimer's and Parkinson's diseases. For unknown reasons, most of these neurodegenerative disorders that include familial and sporadic cases exhibit a late onset. It is possible that these neurodegenerative conditions exhibit a late onset because proteasome activity decreases with aging. Aging-dependent impairment in proteolysis mediated by the proteasome may have profound ramifications for cell viability. It can lead to the accumulation of modified, potentially toxic proteins in cells and can cause cell injury or premature cell death by apoptosis or necrosis. While it is accepted that aging affects UPP function, the question is why does aging cause a decline in regulated protein degradation by the UPP? Herein, we review some of the properties of the UPP and mechanisms mediating its age-dependent impairment. We also discuss the relevance of these findings leading to a model that proposes that UPP dysfunction may be one of the milestones of aging.
Authors:
Vita A Vernace; Thomas Schmidt-Glenewinkel; Maria E Figueiredo-Pereira
Related Documents :
7202266 - Ultrastructure of the human intervertebral disc. i. changes in notochordal cells with age.
2457616 - T cell-mediated recognition of foreign antigen and the ia molecule observed by stopped-...
20628356 - Telomere capping in non-dividing yeast cells requires yku and rap1.
12032846 - Human telomerase accelerates growth of lens epithelial cells through regulation of the ...
1646686 - Human chorionic gonadotropin and related glycoprotein hormones in lung cancer cell lines.
6734746 - Proteolytic processing of micronuclear h3 and histone phosphorylation during conjugatio...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review     Date:  2007-08-06
Journal Detail:
Title:  Aging cell     Volume:  6     ISSN:  1474-9718     ISO Abbreviation:  Aging Cell     Publication Date:  2007 Oct 
Date Detail:
Created Date:  2007-09-18     Completed Date:  2007-12-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101130839     Medline TA:  Aging Cell     Country:  England    
Other Details:
Languages:  eng     Pagination:  599-606     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, Hunter College of the City University of New York, New York, NY 10021, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Aging / metabolism*
Animals
Humans
Proteasome Endopeptidase Complex / metabolism*
Proteins / metabolism*
Ubiquitin / metabolism*
Grant Support
ID/Acronym/Agency:
GM60654/GM/NIGMS NIH HHS; NS41073/NS/NINDS NIH HHS; RR03037/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Proteins; 0/Ubiquitin; EC 3.4.25.1/Proteasome Endopeptidase Complex

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Computer-assisted dosage calculation for strabismus therapy in myopic patients.
Next Document:  Loss of pregnancy-associated plasma protein A extends lifespan in mice.