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Heat shock protein HSP70
- Molecular classification
- Heat Shock Protein Family, Molecular chaperone
01
Overview
HSP70 refers to a family of 70 kilodalton heat shock proteins that are ubiquitously expressed across species. These proteins are central components of the cellular network of molecular chaperones and folding catalysts, assisting in the proper folding, assembly, translocation, and degradation of other proteins within the cell. It protects cells from apoptosis following injury and helps maintain proteostasis during disease states such as cancer or neurodegeneration. Extracellular HSP70 may serve as both biomarker and therapeutic target due to its role in tumor progression/treatment resistance.
- Other names
- HSPA9/GRP75/MortalinHSPA5/GRP78/BiP
02
Mechanism of action
Co-chaperones target HSP70s to specific substrates. Nucleotide exchange factors determine how long HSP70 remains bound to its substrate. ATP-dependent chaperone activity.
03
Biological functions
Protein folding/refoldingProtein quality controlAnti-apoptotic effectsAssists folding/assembly of newly synthesized polypeptidesRefolds misfolded or aggregated proteinsFacilitates membrane translocation of organellar/secretory proteinsRegulates activity/stability/degradation of regulatory or damaged proteinsMaintains protein quality control
04
Disease associations
CancerNeurodegenerative disordersInfection susceptibility/responsesAllograft rejection
05
Safety considerations
Tumor cells often show high intracellular/extracellular levels, potentially complicating therapeutic strategies.
06
Biomarkers
Extracellular HSP70 (eHsp70)
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