Functional state of the Hsp27 chaperone as a molecular marker of an unfavorable course of larynx cancer.

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.