title: Functional state of the Hsp27 chaperone as a molecular marker of an unfavorable course of larynx cancer.
abstract: BACKGROUND
  The 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.
  
  
  OBJECTIVE
  To 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.
  
  
  METHODS
  Tumor 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.
  
  
  RESULTS
  The 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.
  
  
  CONCLUSIONS
  The 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.
authors.affiliation: Tomsk Cancer Research Institute, Tomsk, Russian Federation.|Laboratory for Translational Cellular and Molecular Biomedicine, Tomsk State University, Tomsk, Russian Federation.|Siberian State Medical University, Tomsk, Russian Federation.
authors.forename: Evgeniya V
authors.initials: EV
authors.lastname: Kaigorodova
authors.affiliation: Tomsk Cancer Research Institute, Tomsk, Russian Federation.|Laboratory for Translational Cellular and Molecular Biomedicine, Tomsk State University, Tomsk, Russian Federation.|Siberian State Medical University, Tomsk, Russian Federation.
authors.forename: Marina V
authors.initials: MV
authors.lastname: Zavyalova
authors.affiliation: Tomsk Cancer Research Institute, Tomsk, Russian Federation.
authors.forename: Vyacheslav A
authors.initials: VA
authors.lastname: Bychkov
authors.affiliation: Tomsk Cancer Research Institute, Tomsk, Russian Federation.|Siberian State Medical University, Tomsk, Russian Federation.
authors.forename: Vladimir M
authors.initials: VM
authors.lastname: Perelmuter
authors.affiliation: Tomsk Cancer Research Institute, Tomsk, Russian Federation.|Siberian State Medical University, Tomsk, Russian Federation.
authors.forename: Evgenii L
authors.initials: EL
authors.lastname: Choynzonov
mesh_terms: D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D014408:Biomarkers, Tumor; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D005260:Female; D055551:HSP27 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D053208:Kaplan-Meier Estimate; D007822:Laryngeal Neoplasms / Q000378:metabolism* / Q000401:mortality / Q000473:pathology / Q000628:therapy; D008207:Lymphatic Metastasis; D008297:Male; D008875:Middle Aged; D011379:Prognosis; D021381:Protein Transport; D047368:Tumor Burden
chemical_list: D014408:Biomarkers, Tumor; D055551:HSP27 Heat-Shock Proteins
keywords: Larynx cancer; heat shock protein 27; immunohistochemistry; phospho S78-Hsp27; prognostic markers