Chaperoning stem cells: a role for heat shock proteins in the modulation of stem cell self-renewal and differentiation?
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.
Prinsloo
Earl
E
Biomedical Biotechnology Research Unit, Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahamstown, South Africa.
Setati
Mokgadi M
MM
Longshaw
Victoria M
VM
Blatch
Gregory L
GL
D000818:Animals; D002454:Cell Differentiation / Q000235:genetics / Q000502:physiology; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D013234:Stem Cells / Q000166:cytology* / Q000378:metabolism*
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones