Stress proteins HSP27 and HSP70i predict survival in non-small cell lung carcinoma

Anticancer Res. 2008 Jan-Feb;28(1B):501-6.

Abstract

Background: The expression pattern of stress (heat shock) proteins (HSPs) in cancer cells is frequently different from that observed in normal cells; most often some stress-inducible HSPs are constitutively and highly expressed. The objective of this study was to determine the prognostic significance of stress proteins HSP70i and HSP27 in non-small cell lung carcinoma (NSCLC).

Materials and methods: An immunohistochemical procedure that enables unambiguous detection of HSP70i protein was used.

Results: Strong HSP70i staining showed a survival advantage, although multivariate analysis did not confirm this result. There was an evident correlation between HSP27 overexpression and survival of patients and the results were confirmed by multivariate analysis: 70% of patients with HSP27-negative tumors died within one year after the surgery.

Conclusion: Our data suggest that HSP27 and HSP70i positivity may represent a favorable prognostic factor in NSCLC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carcinoma, Non-Small-Cell Lung / metabolism*
  • Carcinoma, Non-Small-Cell Lung / pathology
  • Female
  • HSP27 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins / biosynthesis*
  • Heat-Shock Proteins / biosynthesis*
  • Humans
  • Immunohistochemistry
  • Lung Neoplasms / metabolism*
  • Lung Neoplasms / pathology
  • Male
  • Molecular Chaperones
  • Neoplasm Proteins / biosynthesis*
  • Neoplasm Staging
  • Prognosis

Substances

  • HSP27 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • HSPB1 protein, human
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Neoplasm Proteins