Universität zu Köln

Saez, Isabel and Vilchez, David ORCID: 0000-0002-0801-0743 (2014). The Mechanistic Links Between Proteasome Activity, Aging and Agerelated Diseases. Curr. Genomics, 15 (1). S. 38 - 52. SHARJAH: BENTHAM SCIENCE PUBL LTD. ISSN 1875-5488

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Abstract

Damaged and misfolded proteins accumulate during the aging process, impairing cell function and tissue homeostasis. These perturbations to protein homeostasis (proteostasis) are hallmarks of age- related neurodegenerative disorders such as Alzheimer's, Parkinson's or Huntington's disease. Damaged proteins are degraded by cellular clearance mechanisms such as the proteasome, a key component of the proteostasis network. Proteasome activity declines during aging, and proteasomal dysfunction is associated with late- onset disorders. Modulation of proteasome activity extends lifespan and protects organisms from symptoms associated with proteostasis disorders. Here we review the links between proteasome activity, aging and neurodegeneration. Additionally, strategies to modulate proteasome activity and delay the onset of diseases associated to proteasomal dysfunction are discussed herein.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Saez, Isabel UNSPECIFIED UNSPECIFIED UNSPECIFIED Vilchez, David UNSPECIFIED orcid.org/0000-0002-0801-0743 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-447513
DOI:	10.2174/138920291501140306113344
Journal or Publication Title:	Curr. Genomics
Volume:	15
Number:	1
Page Range:	S. 38 - 52
Date:	2014
Publisher:	BENTHAM SCIENCE PUBL LTD
Place of Publication:	SHARJAH
ISSN:	1875-5488
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language LIFE-SPAN EXTENSION; MULTICATALYTIC PROTEINASE COMPLEX; BETA-AMYLOID PEPTIDE; RESTRICTION-INDUCED LONGEVITY; MOLECULAR-WEIGHT PROTEASES; NATIONAL-CANCER-INSTITUTE; NRF2 TRANSCRIPTION FACTOR; EMBRYONIC STEM-CELLS; AGE-RELATED DECLINE; OXIDATIVE-STRESS Multiple languages Biochemistry & Molecular Biology; Genetics & Heredity Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/44751