Heat shock 70 kDa protein 1 (HSP70) (HSP70)

Heat shock 70 kDa protein 1 (HSP70) is a molecular chaperone that is typically intracellular but becomes localized to the plasma membrane specifically in tumor cells (Multhoff et al., 1995, PubMed: 7530714). This membrane-bound form (mHSP70) serves as a tumor-specific marker and a target for immunotherapy (Stangl et al., 2011, PubMed: 21173240). In cancer, HSP70 helps stabilize proteins and inhibit apoptosis, promoting tumor survival and resistance to therapy (Murphy, 2013, PubMed: 23536579). Drugs like the cmHsp70.1 antibody target this surface protein to trigger immune-mediated destruction of cancer cells via Natural Killer (NK) cells (Specht et al., 2015, PubMed: 25852340). Additionally, HSP70-derived peptides like TKD are used to prime the immune system to recognize mHSP70-positive tumors (Multhoff et al., 2001, PubMed: 11238504). The presence of HSP70 on the cell surface is associated with high-grade tumors and poor prognosis, making it a valuable biomarker for patient stratification (Gehrmann et al., 2014, PubMed: 24743457). Beyond direct targeting, mHSP70 is also involved in the release of exosomes that can modulate the tumor microenvironment (Gastpar et al., 2005, PubMed: 15642714). Current therapeutic approaches aim to exploit this unique surface expression to deliver cytotoxic agents or enhance the efficacy of radiotherapy (Stangl et al., 2011, PubMed: 21173240).

Other names

HSPA1AHSP72Membrane-bound Heat shock protein 70mHSP70Heat shock 70 kDa protein 1A

Targeting the extracellular domain of membrane-bound HSP70 to induce antibody-dependent cellular cytotoxicity (ADCC) or activate Natural Killer (NK) cells against tumor cells (Stangl et al., 2011, PubMed: 21173240).