Heat shock protein 105 kDa (HSP105) (HSP105)

Heat shock protein 105 kDa (HSP105), also known as HSP110, is a molecular chaperone belonging to the HSP70 superfamily that plays a critical role in maintaining cellular proteostasis. It functions primarily as a potent nucleotide exchange factor (NEF) for HSP70, accelerating the release of ADP to facilitate the protein folding cycle and prevent the aggregation of misfolded proteins under stress conditions [2][12]. In the context of oncology, HSP105 is frequently overexpressed in a variety of solid tumors, including colorectal cancer, melanoma, and lymphoma, where it contributes to tumor cell survival and proliferation by suppressing apoptosis and stabilizing oncogenic client proteins [1][13][17]. Its high tumor-specific expression compared to normal tissues makes it an attractive target for therapeutic intervention, particularly through the development of cancer vaccines using HSP105-derived peptides [1][11]. Additionally, small molecule inhibitors are being explored to disrupt its chaperone function and sensitize cancer cells to chemotherapy [6][12]. Beyond cancer, HSP105 has been implicated in neurodegenerative diseases, where its ability to dissolve protein aggregates may offer a protective mechanism against proteotoxic stress [12][16].

Other names

HSP110HSPH1Heat shock 110 kDa proteinHeat shock 105 kDa protein 1Antigen NY-CO-25HSP105AHSP105B

HSP105 acts as a nucleotide exchange factor for HSP70; therapeutic strategies include using HSP105-derived peptides to induce a cytotoxic T-lymphocyte-mediated anti-tumor immune response or using small molecules to inhibit its ATPase activity and disrupt its chaperone function, thereby inducing apoptosis in cancer cells.