ArticleMolecular pharmaceutics2010
Silencing heat shock protein 27 decreases metastatic behavior of human head and neck squamous cell cancer cells in vitro.
Article in Molecular pharmaceutics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 43 citations in OpenAlex.
- Review
- The heat shock protein Hsp27 controls mitochondrial function by modulating ceramide generation.Cell reports · 2023Article
- Article
- Review
- Protein Profile of Human Saliva as a Predictive and Prognostic Tool for OSCC in Tamol Chewer's Population in Assam.Asian Pacific journal of cancer prevention : APJCP · 2021Article
- Small Heat Shock Proteins in Cancers: Functions and Therapeutic Potential for Cancer Therapy.International journal of molecular sciences · 2020Review
- [Biology behavior of head and neck squamous cell cancer cells changes after knocking down heat shock protein 27].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2020Article
- Article
- Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy.Cells · 2019Review
- FOXM1 is a novel predictor of recurrence in patients with oral squamous cell carcinoma associated with an increase in epithelial‑mesenchymal transition.Molecular medicine reports · 2019Article
- Heat shock protein 27 promotes cell cycle progression by down-regulating E2F transcription factor 4 and retinoblastoma family protein p130.The Journal of biological chemistry · 2018Article
- Differentially expressed proteins in positive versus negative HNSCC lymph nodes.BMC medical genomics · 2018Article
- New HSP27 inhibitors efficiently suppress drug resistance development in cancer cells.Oncotarget · 2016Article
- Four and a half LIM domains 2 contributes to the development of human tongue squamous cell carcinoma.Journal of molecular histology · 2016Article
- A Targetable Molecular Chaperone Hsp27 Confers Aggressiveness in Hepatocellular Carcinoma.Theranostics · 2016Article
- Targeting the testis-specific heat-shock protein 70-2 (HSP70-2) reduces cellular growth, migration, and invasion in renal cell carcinoma cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
- Selective regulation of p38β protein and signaling by integrin-linked kinase mediates bladder cancer cell migration.Oncogene · 2014Article
- Fucosylated TGF-β receptors transduces a signal for epithelial-mesenchymal transition in colorectal cancer cells.British journal of cancer · 2014Article
- Up-regulation of microRNA-145 associates with lymph node metastasis in colorectal cancer.PloS one · 2014Article
- Dihydroceramide desaturase knockdown impacts sphingolipids and apoptosis after photodamage in human head and neck squamous carcinoma cells.Anticancer research · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The small heat shock protein 27 (Hsp27) is a molecular chaperone that is involved in a variety of cellular functions in cancer cells. The purpose of this research is to study Hsp27 in vitro metastatic behaviors of head and neck squamous cell carcinoma cells (HNSCC). The expression of Hsp27 in primary and metastatic cell lines derived from the primary HNSCC and a synchronous lymph node metastasis in the same patient was determined using real-time PCR and Western blotting. Proliferation of the primary and metastatic HNSCC cell lines was evaluated using the MTS proliferation assay. Metastatic behavior was assessed using migration and invasion assays. SiRNA knockdown of Hsp27 was performed in the highly migratory metastatic HNSCC cell line. MTS assays showed that the primary (UM-SCC-22A) and metastatic (UM-SCC-22B) HNSCC have similar proliferation rates. However, UM-SCC-22B derived from the metastasis showed 2.3- to 3.6-fold higher migration ability and 2-fold higher invasion ability than UM-SCC-22A. Real-time PCR demonstrated that Hsp27 mRNA is 22.4-fold higher in metastatic UM-SCC-22B than primary UM-SCC-22A. Similarly, Western blotting showed that Hsp27 is rarely detectable in UM-SCC-22A whereas UM-SCC-22B expresses a 25-fold higher level of Hsp27 protein. SiRNA-mediated knockdown of Hsp27 in UM-SCC-22B reduced Hsp27 mRNA expression by nearly 6-fold and protein expression by 23-fold. Furthermore, siRNA knockdown of Hsp27 decreased metastatic behaviors of UM-SCC-22B by 3- to 4-fold in migration and 2-fold in cell invasion reducing cell invasion and migration to levels similar to the primary HNSCC UM-SCC-22A. These data indicate that Hsp27 may regulate metastatic potential of HNSCC cancer cells. Targeting Hsp27 may decrease metastasis in head and neck squamous cell cancer cells.
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