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<p>Heat shock proteins (HSPs) are evolutionarily conserved molecular chaperones that maintain cellular proteostasis under physiological and stress conditions. HSPH1 (Heat Shock Protein Family H Member 1, also known as HSP105 or HSP110) belongs to the HSP110 family and functions as a nucleotide exchange factor for HSP70, enhancing its folding activity. Beyond its canonical role, HSPH1 is increasingly recognized for its involvement in tumor progression. It has been reported to regulate cell proliferation, invasion, metastasis, and resistance to therapy in several cancers, including breast, lung, and liver cancer. Pan-cancer transcriptomic analyses have identified HSPH1 as frequently overexpressed and correlated with poor prognosis. In hepatocellular carcinoma (HCC), while other HSPs such as HSP70 and HSP90 are well-studied, the biological role of HSPH1 remains unclear. In this study, we systematically analyzed HSPH1 expression in HCC using TCGA and GEO datasets, and validated its clinical relevance in patient samples. HSPH1 was significantly upregulated in HCC tissues and associated with advanced tumor stage and worse overall survival. Functional enrichment and immune infiltration analyses suggested that HSPH1 participates in oncogenic pathways (e.g., p53, cell cycle) and modulates the tumor immune microenvironment. Knockdown of HSPH1 in HCC cell lines inhibited proliferation and colony formation. Together, our findings highlight HSPH1 as a potential prognostic biomarker and therapeutic target in HCC.</p>

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Heat shock protein family H member 1 HSPH1 expression correlates with progression and prognosis of hepatocellular carcinoma

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年8月24日

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  • Tianyi Huang,
  • Shimeng Xu,
  • Ming Li,
  • Cuihua Lu,
  • Jiaying Zhang

摘要

Heat shock proteins (HSPs) are evolutionarily conserved molecular chaperones that maintain cellular proteostasis under physiological and stress conditions. HSPH1 (Heat Shock Protein Family H Member 1, also known as HSP105 or HSP110) belongs to the HSP110 family and functions as a nucleotide exchange factor for HSP70, enhancing its folding activity. Beyond its canonical role, HSPH1 is increasingly recognized for its involvement in tumor progression. It has been reported to regulate cell proliferation, invasion, metastasis, and resistance to therapy in several cancers, including breast, lung, and liver cancer. Pan-cancer transcriptomic analyses have identified HSPH1 as frequently overexpressed and correlated with poor prognosis. In hepatocellular carcinoma (HCC), while other HSPs such as HSP70 and HSP90 are well-studied, the biological role of HSPH1 remains unclear. In this study, we systematically analyzed HSPH1 expression in HCC using TCGA and GEO datasets, and validated its clinical relevance in patient samples. HSPH1 was significantly upregulated in HCC tissues and associated with advanced tumor stage and worse overall survival. Functional enrichment and immune infiltration analyses suggested that HSPH1 participates in oncogenic pathways (e.g., p53, cell cycle) and modulates the tumor immune microenvironment. Knockdown of HSPH1 in HCC cell lines inhibited proliferation and colony formation. Together, our findings highlight HSPH1 as a potential prognostic biomarker and therapeutic target in HCC.