Enolase-alpha is frequently down-regulated in non-small cell lung cancer and predicts aggressive biological behavior

Clin Cancer Res. 2003 Sep 1;9(10 Pt 1):3641-4.

Abstract

Purpose: Enolase-alpha is a cytoplasmic glycolytic enzyme important in the formation of phosphoenolpyruvate. Enolase-alpha and c-myc binding protein (MBP-1) originate from a single gene through alternative use of translational starting sites. Both enolase-alpha and MBP-1 can bind to the P2 element in the c-myc promoter and compete with TATA-box binding protein (TBP) to suppress transcription of c-myc.

Experimental design: To determine a potential role of enolase-alpha in vivo, we analyzed enolase-alpha expression in non-small cell lung cancer (NSCLC) tissues from 46 patients by Western blotting and immunohistochemical analysis.

Results: Twelve (26%) of the 46 tumors showed a significantly reduced enolase-alpha expression. Although no statistically significant association was observed between the down-regulation of enolase-alpha and pathological stage, tumor histology, or differentiation, the patients whose tumors showed reduced enolase-alpha expression had a significantly poorer overall survival compared with those without down-regulation of this molecule (P = 0.0398).

Conclusions: Our results indicate down-regulation of enolase-alpha is common in NSCLC and may play an important role in lung tumorigenesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aged
  • Biomarkers, Tumor
  • Blotting, Western
  • Carcinoma, Non-Small-Cell Lung / enzymology*
  • Carcinoma, Non-Small-Cell Lung / mortality
  • DNA-Binding Proteins / biosynthesis*
  • Down-Regulation*
  • Female
  • Humans
  • Immunohistochemistry
  • Lung Neoplasms / enzymology*
  • Lung Neoplasms / metabolism
  • Lung Neoplasms / mortality
  • Male
  • Middle Aged
  • Phosphopyruvate Hydratase / biosynthesis*
  • Prognosis
  • Time Factors
  • Tumor Suppressor Proteins / biosynthesis*

Substances

  • Biomarkers, Tumor
  • DNA-Binding Proteins
  • Tumor Suppressor Proteins
  • ENO1 protein, human
  • Phosphopyruvate Hydratase