ArticleCell stress & chaperones2016
Induction and phosphorylation of the small heat shock proteins HspB1/Hsp25 and HspB5/αB-crystallin in the rat retina upon optic nerve injury.
Article in Cell stress & chaperones, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- AAV2-Mediated Expression of HspB1 in RGCs Prevents Somal Damage and Axonal Transport Deficits in a Mouse Model of Ocular Hypertension.Translational vision science & technology · 2022Article
- The protective role of HSP27 in ocular diseases.Molecular biology reports · 2022Review
- Small Heat Shock Proteins in Retinal Diseases.Frontiers in molecular biosciences · 2022Review
- Heat Shock Protein 27 Injection Leads to Caspase Activation in the Visual Pathway and Retinal T-Cell Response.International journal of molecular sciences · 2021Article
- A specific phosphorylation regulates the protective role of αA-crystallin in diabetes.JCI insight · 2018Article
- The growing world of small heat shock proteins: from structure to functions.Cell stress & chaperones · 2017Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several eye diseases are associated with axonal injury in the optic nerve, which normally leads to degeneration of retinal ganglion cells (RGCs) and subsequently to loss of vision. There is experimental evidence that some members of the small heat shock protein family (HspBs) are upregulated upon optic nerve injury (ONI) in the retina and sufficient to promote RGC survival. These data raise the question as to whether other family members may play a similar role in this context. Here, we performed a comprehensive comparative study comprising all HspBs in an experimental model of ONI. We found that five HspBs were expressed in the adult rat retina at control conditions but only HspB1 and HspB5 were upregulated in response to ONI. Furthermore, HspB1 and HspB5 were constitutively phosphorylated in Müller cells at serine 15 and serine 59, respectively. In RGCs, phosphorylation was stimulated by ONI and occurred at serine 86 of HspB1 and at serine 19 and 45 of HspB5. These data suggest that of all small heat shock proteins, only HspB1 and HspB5 might be of protective value for RGCs after ONI and that this process might be regulated by phosphorylation at serine 86 of HspB1 and serine 19 and serine 45 of HspB5. The molecular targets of phosphoHspB1 and phosphoHspB5 remain to be identified.
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