ArticleJournal of neuro-oncology2025
Glioblastoma cell motility and invasion is regulated by membrane-associated heat shock protein Hsp70.
Article in Journal of neuro-oncology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- The Epichaperome Matrix Theory: A systems-level model of active molecular organization.Cell stress & chaperones · 2026Article
- DBSCAN applied to EHRs data from patients with glioblastoma clusters patients based on cytosolic Hsp70 protein, sex, and brain subventricular zone.BioData mining · 2026Article
- Radiomic analysis of the peritumoral zone identifies imaging signatures of glioma invasion associated with HSP70 expression.Frontiers in oncology · 2026Article
- Review
- Fluorescence molecular imaging of high-grade gliomas and brain metastases using the RAS70 peptide targeting plasma membrane-bound Hsp70 on tumor cells.Journal of neuro-oncology · 2025Article
- Review
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Authors and funding
14 authors.
Funding
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Abstract
purposeMembrane-associated heat shock protein 70 kDa (mHsp70) is specifically localized on the plasma membrane of various malignant tumor cells. In current study, we investigated the role of mHsp70 in motility of glioblastoma cells, which are known to be characterized by a high ability to migrate and invade surrounding brain tissue.
methodsThe presence of mHsp70 on the membrane of patient-derived glioblastoma cells was detected with confocal microscopy, flow cytometry, Western blot, and proteome analysis of lipid rafts. The motility and invasion characteristics were studied using automatic single-cell tracking and transwell analysis with Hsp70 inhibitors.
resultsmHsp70 is able to influence the migration and invasion of glioblastoma cells, and the degree of protein expression correlates with motility. The involvement of mHsp70 in the regulation of cell motility is likely to be mediated by interactions with proteins responsible for cytoskeletal remodeling and connection with the extracellular matrix. Moreover, the protein is localized in lipid rafts associating with other members of the HSPs families. The application of small molecule Hsp70 inhibitors PES and JG-98 successfully reduced the migratory and invasive potential, which allowed them to be used as an adjuvant agent in tumor therapy.
conclusionThis study expands our understanding of mHsp70 function in cancer cells and contributes to the development of novel approaches to the treatment of malignant tumors.
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