ArticleCancer biomarkers : section A of Disease markers2016
Functional state of the Hsp27 chaperone as a molecular marker of an unfavorable course of larynx cancer.
Article in Cancer biomarkers : section A of Disease markers, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Review
- Comment on: Low expression of HSP27 and HSP70 predicts poor prognosis in laryngeal squamous cell carcinoma.Journal of cancer research and clinical oncology · 2025Article
- Low expression of HSP27 and HSP70 predicts poor prognosis in laryngeal squamous cell carcinoma.Journal of cancer research and clinical oncology · 2025Article
- Laryngeal Cancer in the Modern Era: Evolving Trends in Diagnosis, Treatment, and Survival Outcomes.Journal of clinical medicine · 2025Review
- Review
- Review
- Small Heat Shock Proteins in Cancers: Functions and Therapeutic Potential for Cancer Therapy.International journal of molecular sciences · 2020Review
- Circadian locomotor output cycles kaput affects the proliferation and migration of breast cancer cells by regulating the expression of E-cadherin via IQ motif containing GTPase activating protein 1.Oncology letters · 2018Article
- Role of Krüppel-like factor 4 and heat shock protein 27 in cancer of the larynx.Molecular and clinical oncology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe small heat shock protein 27 kDA (Hsp27) acts as an ATP-independent chaperone in protein folding, but is also implicated in architecture of the cytoskeleton, cell migration, metabolism, cell survival, growth/differentiation, mRNA stabilization, and tumor progression.
objectiveTo study the intracellular localization of phosphorylated and non-phosphorylated forms of Hsp27 in squamous cell carcinoma of the larynx (SCCL) and to evaluate their relationship with regional lymphatic metastasis and overall five-year survival.
methodsTumor biopsies of larynx tissue were collected from 50 patients who were between the ages of 30 to 80 years and had a confirmed diagnosis of squamous cell carcinoma of the larynx. Immunohistochemistry was used to determine the intracellular localization of the phosphorylated and non-phosphorylated forms of Hsp27.
resultsThe study revealed that the Hsp27 chaperone was expressed in both the cytoplasm and the nucleus of tumor cells in SCCL. The biopsies of patients with lymph node metastases showed significantly higher expression of the phosphorylated and unphosphorylated forms of Hsp27 in the nucleus compared to those of patients without lymph node metastases. At the same time, the cytoplasmic expression of Hsp27 in these patients did not differ statistically. Analysis of the overall five-year survival rates showed that negative Hsp27 expression in the nucleus of tumor cells is associated with the survival rate of patients with SCCL.
conclusionThe nuclear expression of phosphorylated and unphosphorylated forms of Hsp27 is a molecular marker of unfavorable squamous cell carcinoma of the larynx associated with lymphogenous metastasis and decreased total five-year survival.
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