Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target

Aparna Vidyasagar,Arjang Djamali,Nancy A Wilson

doi:10.1186/1755-1536-5-7

Aparna Vidyasagar, Arjang Djamali + Show 1 more

Open Access

https://doi.org/10.1186/1755-1536-5-7

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Abstract

Heat shock protein 27 (HSP27) is a multidimensional protein which acts as a protein chaperone and an antioxidant and plays a role in the inhibition of apoptosis and actin cytoskeletal remodeling. In each of these capacities, HSP27 has been implicated in different disease states playing both protective and counter-protective roles. The current review presents HSP27 in multiple disease contexts: renal injury and fibrosis, cancer, neuro-degenerative and cardiovascular disease, highlighting its role as a potential biomarker and therapeutic target.

Highlights

Heat shock protein 27 (HSP27) is a multidimensional protein which acts as a protein chaperone and an antioxidant and plays a role in the inhibition of apoptosis and actin cytoskeletal remodeling
HSP27 was initially characterized in response to heat shock [2] as a protein chaperone that facilitates the proper refolding of damaged proteins [3,4]
The present summary highlights some of the recent data examining HSP27 in its diagnostic and therapeutic capacities

Summary

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Association between high HSP27 expression and incomplete resection margins in rectal cancer. An earlier study found that Her overexpressing breast cancer tumors showed increased expression of phosphorylated HSP27, at serine 78 [44,48]. Neuro-degenerative disease and neuronal injury Neuro-degenerative diseases are characterized by the accumulation of mis-folded proteins In their 2010 study Abisambra et al [21] highlighted the potential therapeutic properties of HSP27 and the variability in function between in vitro and in vivo models, and the importance of dynamic cycling between phosphorylated and unphosphorylated forms. HSP27 overexpression has potential protective effects during cerebral ischemia and subsequent neuronal injury, implicating it as a potential therapeutic agent during stroke. In keeping with the anti-apoptotic functions of HSP27 during neuronal injury, these transgenic mice showed reduced apoptosis and caspase 3 induction. HSP27 overexpression protects against ischemic injury (presumably utilizing its antioxidant properties) and acts as a biomarker of disease

Conclusions

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Findings

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