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Target intelligence / Profile preview
Heat Shock Protein 70 (HSP70)
- Target
- HSP70
- Molecular classification
- Molecular chaperone
01
Overview
HSP70 is a highly conserved family of molecular chaperones found in all organisms from bacteria to humans. These proteins are central to cellular protein homeostasis, assisting in the folding of newly synthesized proteins, refolding misfolded or aggregated proteins, translocation across membranes, and regulating the degradation of unwanted proteins. HSP70 expression is upregulated in response to various forms of cellular stress such as heat shock, oxidative stress, and inflammation.
- Other names
- Hsp72HSPA1AHsc70HSPA8BiPGrp78HSPA5mtHsp70Grp75MortalinHSPA9
02
Mechanism of action
Pharmacological modulation strategies include small molecules that induce/inhibit expression or interfere with co-chaperone interactions—some acting indirectly through inhibition of related chaperones like Hsp90
03
Biological functions
Protein foldingProtein refoldingPrevention of protein aggregationDisaggregation of proteinsProtein complex assembly/disassemblyTranslocation across organelle membranesRegulation of protein degradationFolding nascent polypeptidesTargeting damaged or excess proteins for degradation
04
Disease associations
CancerNeurodegenerative diseaseIschemic injuryStrokeInfectionImmune disorders
05
Safety considerations
Dysregulation or malfunction implicated in various diseasesCytoprotective effects can be a double-edged sword in cancer
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