Chaperoning stem cells: a role for heat shock proteins in the modulation of stem cell self-renewal and differentiation?

Full text for this resource is not available from the Research Repository.

Prinsloo, Earl, Setati, Mokgadi M, Longshaw, Victoria M and Blatch, Gregory ORCID: 0000-0003-0778-8577 (2009) Chaperoning stem cells: a role for heat shock proteins in the modulation of stem cell self-renewal and differentiation? BioEssays, 31 (4). pp. 370-377. ISSN 0265-9247 (print) 1521-1878 (online)

Abstract

Self-renewal and differentiation of stem cells are tightly regulated processes subject to intrinsic and extrinsic signals. Molecular chaperones and co-chaperones, especially heat shock proteins (Hsp), are ubiquitous molecules involved in the modulation of protein conformational and complexation states. The function of Hsp, which are typically associated with stress response and tolerance, is well characterized in differentiated cells, while their role in stem cells remains unclear. It appears that embryonic stem cells exhibit increased stress tolerance and concomitant high levels of chaperone expression. This review critically evaluates stem cell research from a molecular chaperone perspective. Furthermore, we propose a model of chaperone-modulated self-renewal in mouse embryonic stem cells.

Dimensions Badge

Altmetric Badge

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8139
DOI 10.1002/bies.200800158
Official URL http://onlinelibrary.wiley.com/doi/10.1002/bies.20...
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 1004 Medical Biotechnology
Historical > FOR Classification > 1101 Medical Biochemistry and Metabolomics
Keywords ResPubID22193, heat shock proteins, human, molecular chaperones, mouse, stem cells
Citations in Scopus 61 - View on Scopus
Download/View statistics View download statistics for this item

Search Google Scholar

Repository staff login