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Heat shock 70 kDa protein 1-like (HSPA1L) is a molecular chaperone in the Hsp70 family that assists in folding newly synthesized proteins, refolding misfolded ones, and preventing aggregation in the cytosol and organelles through ATP-dependent cycles. It plays key roles in protein quality control, stress response, and processes like signal transduction, apoptosis regulation, and antigen presentation to immune cells. Encoded by a gene in the MHC class III region on chromosome 6, it shares high homology with HSPA1A and HSPA1B but is constitutively expressed, notably in testis, and not heat-inducible. In disease, HSPA1L contributes to cancer progression by stabilizing oncofetal proteins, enhancing tumor malignancy and therapy resistance, and serves as a prognostic marker in cancers like hepatocellular, gastric, and breast. It also mitigates neurodegenerative diseases by aiding parkin translocation to damaged mitochondria and is linked to inflammatory bowel disease via mutations. Additionally, it influences aging, cell senescence, and graft-versus-host disease, with polymorphisms associated with pathology.
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