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Membrane Heat Shock Protein 70 (mHsp70)
- Target
- mHsp70
- Molecular classification
- Heat Shock Protein, Molecular Chaperone
01
Overview
Membrane heat shock protein 70 (Hsp70) is a member of the HSP70 family of molecular chaperones that is translocated to the plasma membrane, particularly in cancer cells. It assists in folding newly synthesized proteins, refolding misfolded or aggregated proteins, and translocating proteins across membranes. Membrane-bound Hsp70 has been implicated in tumor growth, invasion, migration, resistance to therapy, and immune modulation. Its presence on the plasma membrane makes it an attractive target for anti-cancer therapies. On membranes—especially lysosomal/endosomal—Hsp70 inhibits lysosomal membrane permeabilization which promotes cell survival.
- Other names
- Plasma membrane Hsp70Extracellular Hsp70
02
Mechanism of action
Inhibition of membrane Hsp70 function to disrupt tumor cell survival; blockade of interaction with client proteins; induction of immune response.
03
Biological functions
Protein foldingProtein refoldingProtein transportCellular stress responseInhibition of lysosomal membrane permeabilizationProtein homeostasis
04
Disease associations
CancerNeurodegenerative disease (potential)Protein misfolding diseases
05
Safety considerations
Potential off-target effects on intracellular Hsp70Immune-related adverse events (for antibody-based therapies)
06
Biomarkers
Surface expression of Hsp70 in tumor cells
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