HSPH1, also known as heat shock 105kDa/110kDa protein 1, is a member of the heat shock protein family. Heat shock proteins play crucial roles in maintaining protein homeostasis, assisting in protein folding, preventing protein aggregation, and participating in stress responses within cells. HSPH1 has been implicated in multiple cellular processes and signaling pathways relevant to health and disease [4,7].

In cancer research, HSPH1 has diverse roles. In gastric cancer, it was identified as a target of ATF2. HSPH1 can interact with SLC7A11, increasing its protein stability, and thereby inhibiting sorafenib-induced ferroptosis [1]. In advanced lung adenocarcinoma, the rs2280059 genetic variant of HSPH1 affects its expression, and silencing HSPH1 can increase the antineoplastic effects of gefitinib [2]. In prostate cancer, HSPH1 may promote the stress response of CD8 + T cells, potentially inhibiting cancer cell invasion [3]. In aggressive B-cell non-Hodgkin lymphoma, silencing HSPH1 downregulates Bcl-6 and c-Myc, hampering tumor growth [5].

In doxorubicin-induced chronic cardiotoxicity, Hsph1 was identified as a potential biomarker along with Vegfa, and their combined expression was positively correlated with dilated cardiomyopathy-induced heart failure [8]. In LPS-induced acute lung injury, the IL-1β/KLF2/HSPH1 pathway activation promotes STAT3 phosphorylation in alveolar macrophages, exacerbating pulmonary inflammation [6].

In summary, HSPH1 is a key protein involved in maintaining cellular protein homeostasis and is implicated in various disease conditions, especially cancer and certain heart and lung diseases. Research on HSPH1, including through gene-knockout or knockdown models in these disease contexts, has provided insights into its functions, highlighting its potential as a therapeutic target or biomarker.