HSPA9 and neoplasm: GRP75, a stress-induced molecular chaperone, belongs to the HSP70 family.28 It is traditionally localized in the mitochondria as an N-terminal signal peptide and regulates protein quality control, including the folding, assembly, and export of misfolded proteins for degradation.28 The overexpression of GRP75 in tumour tissues is often positively correlated with malignant progression.29 Proteomic analysis revealed that GRP75 was strongly associated with thermogenic adipocytes in perivascular adipose tissue,30 indicating the crucial role of GRP75 in tumour-induced adipocyte browning.