Universität zu Köln

Vilchez, David ORCID: 0000-0002-0801-0743, Simic, Milos S. and Dillin, Andrew (2014). Proteostasis and aging of stem cells. Trends Cell Biol., 24 (3). S. 161 - 171. LONDON: ELSEVIER SCIENCE LONDON. ISSN 0962-8924

Full text not available from this repository.

Abstract

The accumulation of misfolded or damaged proteins is an important determinant of the aging process. Mechanisms that promote the homeostasis of the proteome, or proteostasis, can slow aging and decrease the incidence of age-related diseases. Adult stem cell function declines during the aging process of an organism. This demise of somatic stem cell function could contribute to tissue degeneration and organismal aging. Accumulation of damaged proteins in embryonic stem cells (ESCs) may also have an impact on the aging process, because the passage of these proteins to progenitor cells during asymmetric division could compromise development and aging. Therefore, proteostasis maintenance in stem cells might have an important role in organismal aging. In this review, we discuss exciting new insights into stem cell aging and proteostasis and the questions raised by these findings.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Vilchez, David UNSPECIFIED orcid.org/0000-0002-0801-0743 UNSPECIFIED Simic, Milos S. UNSPECIFIED UNSPECIFIED UNSPECIFIED Dillin, Andrew UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-445586
DOI:	10.1016/j.tcb.2013.09.002
Journal or Publication Title:	Trends Cell Biol.
Volume:	24
Number:	3
Page Range:	S. 161 - 171
Date:	2014
Publisher:	ELSEVIER SCIENCE LONDON
Place of Publication:	LONDON
ISSN:	0962-8924
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language UNFOLDED PROTEIN RESPONSE; UBIQUITIN-PROTEASOME SYSTEM; OXIDATIVE STRESS; HEAT-SHOCK; PROTEOTOXIC STRESS; DAMAGED PROTEINS; REGULATING AUTOPHAGY; TRANSCRIPTION FACTOR; PROTEOMIC ANALYSIS; GENE-EXPRESSION Multiple languages Cell Biology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/44558