Heat shock 70 kDa protein 1A (HSPA1A)

Heat shock 70 kDa protein 1A (HSPA1A) is a major member of the Hsp70 family of molecular chaperones, essential for protein quality control in the cell. It stabilizes nascent and misfolded proteins, assists in their refolding, and directs irreparably damaged proteins toward degradation via the ubiquitin-proteasome pathway. Its expression is highly inducible by cellular stresses, such as heat shock and oxidative stress. HSPA1A also inhibits apoptosis by blocking caspase activation and cytochrome c release and is directly involved in DNA repair. Elevated HSPA1A is observed in various cancers, neurodegenerative, cardiovascular, and inflammatory diseases, where it may protect cells, promote survival, and contribute to disease pathogenesis. Due to these functions, HSPA1A is considered a promising, though challenging, drug target in oncology and other fields, but inhibition carries a risk of toxicity due to its central role in cellular proteostasis[1][2][5][7].

Other names

HSP70-1HSP72HSP70.1Heat shock protein family A (Hsp70) member 1AHeat shock 70 kDa protein 1DnaK-type molecular chaperone HSP70-1Epididymis secretory sperm binding proteinEpididymis secretory protein Li 103HSPA1

Inhibition of ATPase activity; Disruption of chaperone function/protein folding; Promotion of apoptosis by abrogating anti-apoptotic Hsp70 activity