Mitochondrial 70 kDa heat shock protein (Mortalin) (HSPA9)

Mortalin, also known as HSPA9 or GRP75, is a member of the heat shock protein 70 (Hsp70) family that primarily functions as a mitochondrial chaperone. In many types of cancer, including pancreatic ductal adenocarcinoma (PDAC), mortalin is overexpressed and translocated from the mitochondria to the cell surface, where it contributes to tumor cell survival, proliferation, and evasion of apoptosis. The P19 aptamer is a 2-fluoro-modified RNA ligand specifically developed to recognize and internalize into cancer cells by binding to cell-surface mortalin. This receptor-mediated internalization has been exploited for the targeted delivery of various therapeutic cargoes, such as chemotherapeutic drugs (gemcitabine, 5-fluorouracil) and small activating RNAs (saRNAs), directly into the cytoplasm of malignant cells. By leveraging the differential expression of mortalin on the surface of tumor versus normal cells, P19-based delivery systems aim to enhance therapeutic efficacy while minimizing systemic toxicity.

Other names

MortalinGRP75mHSP70HSPA9PBP74MOTMOT2CSAMitochondrial 70 kDa heat shock protein

Aptamer-mediated delivery of cytotoxic agents or small activating RNA to cancer cells overexpressing mortalin on the cell surface.