Drug Discov Today
January 2025
The heat shock protein (HSP) 110 family has a key role as a unique class of molecular chaperones maintaining cellular proteostasis in eukaryotes. Abnormal activation of Hsp110 has been implicated in several diseases. Given its important role in pathogenesis, Hsp110 has become a novel drug target for disease diagnosis and targeted therapy.
View Article and Find Full Text PDFBreast cancer, a leading cause of cancer-related mortality in women, is characterized by its propensity for metastasis. Heat shock protein 110 (Hsp110), a molecular chaperone encoded by the HSPH1 gene, has been implicated in cancer progression, including breast cancer, where it is upregulated and associated with worse outcomes. However, the role of Hsp110 in breast cancer pathogenesis and its potential as a therapeutic target have not been thoroughly investigated.
View Article and Find Full Text PDFPulmonary arterial hypertension (PAH) is a progressive and fatal cardiovascular disorder that is characterized by pulmonary vascular remodeling. Our previous results demonstrated that heat shock protein (Hsp110) was significantly activated to induce vascular remodeling by enhancing the Hsp110-STAT3 interaction. The development of inhibitors that disrupt this association represents a novel strategy for the treatment of PAH.
View Article and Find Full Text PDFWe investigated the blood lipid regulation effects and mechanism of a functional Natto yogurt in a high-fat diet-induced hyperlipidemia mouse model. Natto yogurt was characteristically fermented by Bacillus natto and Lactobacillus plantarum with milk-soy dual protein as substrates. After 5 weeks of Natto yogurt consumption, the body weight, fat, and liver weight of mice were significantly improved, while serum levels of TG, TC, LDL, ALT, TBIL, and TBA were reduced.
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