Heat Shock Protein 27 (HSP27), also known as HSPB1, is a small chaperone protein that plays a crucial role in cellular stress responses. It is part of the small heat shock protein (sHsp) family, which includes other members like α-crystallin and Hsp20. HSP27 is involved in various cellular processes, including thermotolerance, inhibition of apoptosis, regulation of cell development, and differentiation .
HSP27 has a highly conserved α-crystallin domain near its C-terminus, which is essential for its chaperone activity. This domain consists of 80 to 100 amino acids that fold into β-sheets, forming stable dimers. The N-terminus contains a less conserved WD/EPF domain, followed by a short variable sequence. The C-terminal region is highly flexible and polar, contributing to the protein’s solubility and stability .
HSP27 forms large oligomers with an average mass of around 500 kDa in vitro. These oligomers consist of stable dimers formed by the α-crystallin domains of neighboring monomers. The N-terminus is essential for the development of these large oligomers .
HSP27 is overexpressed in various cellular stress states and is involved in regulating proteostasis by stabilizing protein conformation and promoting the refolding of misfolded proteins. It plays a significant role in protecting cells from multiple sources of stress injury, including oxidative stress, inflammatory responses, and apoptosis .
In addition to its intracellular functions, recent studies have shown that HSP27 can be found in the extracellular space, where it may signal via membrane receptors to alter gene transcription and cellular function .
HSP27 has been implicated in various disease states, including cardiovascular diseases, where it plays both protective and counter-protective roles. Targeting HSP27 is considered a promising strategy for the treatment of cardiovascular diseases due to its involvement in oxidative stress, inflammatory responses, and apoptosis .
Human recombinant HSP27 with a His tag is a form of the protein that has been genetically engineered to include a polyhistidine tag. This tag facilitates the purification of the protein using affinity chromatography techniques. The recombinant form retains the functional properties of the native protein and is used in various research applications to study its structure, function, and therapeutic potential.