Abstract
Heat shock proteins (Hsps) are highly conserved proteins that are induced in response to various physiological and environmental stressors. HspB1 (Hsp27) is a prominent member of the small Hsps family and is strongly induced during the stress response. Notably, HspB1 has powerful neuroprotective effects, increasing the survival of cells subjected to cytotoxic stimuli. This is especially relevant to the study of the retina, where cells are subject to death due to retinal disease and injury. While HspB1 shows constitutive expression in some areas of the mammalian retina, of particular interest is the upregulation of the protein in response to ischemia and oxidative stress, traumatic nerve injury, and elevated intraocular pressure and glaucoma. Several mechanisms have been proposed to account for the cytoprotective actions of HspB1, including its role as a molecular chaperone, a stabilizer of the cytoskeleton, and a regulator of apoptosis. This review will focus on the role of HspB1 in the retina, emphasizing effects on retinal ganglion cells, by analyzing the expression, induction by stressors, and mechanisms of its neuroprotective function. Finally, the potential of HspB1 as a clinical therapeutic will be examined.
Original language | English |
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Pages (from-to) | 124-132 |
Number of pages | 9 |
Journal | Molecular Neurobiology |
Volume | 42 |
Issue number | 2 |
DOIs | |
Publication status | Published - Oct 2010 |
Bibliographical note
Funding Information:Acknowledgements Amanda O’Reilly held a Natural Sciences and Engineering Research Council Undergraduate Student Research Award. Dr. Currie’s research is funded by the Heart and Stroke Foundation of New Brunswick. Dr. Clarke’s research is funded by the Natural Sciences and Engineering Research Council and the Canadian Institutes of Health Research in partnership with Nova Scotia Health Research Foundation.
ASJC Scopus Subject Areas
- Neurology
- Cellular and Molecular Neuroscience