HspB1 (Hsp 27) expression and neuroprotection in the retina.
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.
Department of Anatomy & Neurobiology, Faculty of Medicine, Dalhousie University, Halifax, NS, B3H 1X5, Canada.
Amanda M
AM
O'Reilly
R William
RW
Currie
David B
DB
Clarke
D000818:Animals; D017209:Apoptosis; D019610:Cytoprotection; D055551:HSP27 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D010084:Oxidation-Reduction; D012160:Retina / Q000378:metabolism; D055351:Retinal Neurons / Q000166:cytology* / Q000378:metabolism
D055551:HSP27 Heat-Shock Proteins