Aug 8, 2020 · Results: In summary, plasma levels of HSP90 were shown to be higher in patients with gastric cancer (GC) or colorectal cancer (CRC) than in controls with benign gastrointestinal diseases. In both GC and CRC patients, HSP90 was significantly associated with live metastasis.

Jun 14, 2024 · Heat-shock protein 90 (Hsp90) plays a crucial role in tumorigenesis and tumor progression; however, its mechanism of action in gastric cancer (GC) remains unclear. Here, the role of Hsp90 in GC metabolism is the focus of this research.

Feb 10, 2025 · In summary, high HSP90 expression enhance the stem cell-like properties of GC cells, significantly reducing patient survival rates. We identified 937 differentially expressed proteins (DEP) that interact with HSP90 through mass spectrometry analysis of GC cell lines (HGC27 and AGS).

Our results showed that HSP90α overexpression might be associated with disease progression and poorer survival in patients with GC. Therefore, HSP90α could be used as possible biomarker for the prognosis of GC.

Heat-shock protein 90 (Hsp90) plays a crucial role in tumorigenesis and tumor progression; however, its mechanism of action in gastric cancer (GC) remains unclear. Here, the role of Hsp90 in GC metabolism is the focus of this research.

Several successful cases of HSP90 inhibitors capable of inhibiting GC inspired us to try ganetespib, a clinically promising and actively investigated second-generation HSP90 inhibitor in GC treatment.

Aug 3, 2023 · We present the 3.9 Å resolution cryo-EM structure of the human membrane receptor guanylyl cyclase GC-C in complex with Hsp90 and its co-chaperone Cdc37, providing insight into the mechanism of Cdc37 mediated binding of GC-C to the Hsp90 regulatory complex.

HSP90 proteins take part in essential cellular processes and regulatory pathways like apoptosis, cell cycle control, cell viability, protein folding and degradation, and signalling events. In addition, they induce the adaptive immunity by activation of antigen presenting cells and dendritic cells.

Our multi-omics and in vitro studies revealed that HSP90 regulates glycolysis and influences the stemness properties of gastric cancer cells. Mechanistically, HSP90 facilitates the assembly of a glycolytic multi-enzyme complex, termed the HGEO …

Jan 23, 2023 · We present the 3.9 Å resolution cryo-EM structure of the human membrane receptor guanylyl cyclase GC-C in complex with Hsp90 and its co-chaperone Cdc37, providing insight into the mechanism of Cdc37 mediated binding of GC-C to the Hsp90 regulatory complex.