ArticleFrontiers in endocrinology2022
Heat Shock Proteins 70 Regulate Cell Motility and Invadopodia-Associated Proteins Expression in Oral Squamous Cell Carcinoma.
Article in Frontiers in endocrinology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 4 citations in OpenAlex.
- Review
- Glioblastoma cell motility and invasion is regulated by membrane-associated heat shock protein Hsp70.Journal of neuro-oncology · 2025Article
- Exploring UBASH3A: from immune regulation to autoimmune diseases.Journal of translational medicine · 2025Review
- HSP70 Family in Cancer: Signaling Mechanisms and Therapeutic Advances.Biomolecules · 2023Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Many studies have shown that diabetes is often closely related to oral squamous cell carcinoma (OSCC) occurrence and metastasis. Heat shock protein 70 (Hsp70) is a molecular chaperone related to diabetes complications. This study aims to investigate the role of Hsp70 in OSCC in expression of invadopodia-associated proteins. Methods: The expressions and correlation of HSP70, Hif1α, MMP2, MMP14, and cortactin were examined using bioinformatics analysis and verified by OSCC tissue microarrays. Assay Results: The expressions of invadopodia-associated proteins were enhanced in OSCC tissues compared with paracarcinoma tissues and partially correlated with HSP70. Inhibiting HSP70 significantly decreased the cell viability, proliferation, and migration of OSCC cells. Conclusions: HSP70 may be involved in invadopodia-associated proteins in OSCC cells, which provides a promising method for treatment of OSCC metastasis.
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