Over-expression of GAPDH in human colorectal carcinoma as a preferred target of 3-bromopyruvate propyl ester

J Bioenerg Biomembr. 2012 Feb;44(1):117-25. doi: 10.1007/s10863-012-9420-9. Epub 2012 Feb 18.

Abstract

It has long been observed that many cancer cells exhibit increased aerobic glycolysis and rely more on this pathway to generate ATP and metabolic intermediates for cell proliferation. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in glycolysis and has been known as a housekeeping molecule. In the present study, we found that GAPDH expression was significantly up-regulated in human colorectal carcinoma tissues compared to the adjacent normal tissues, and also increased in colon cancer cell lines compared to the non-tumor colon mucosa cells in culture. The expression of GAPDH was further elevated in the liver metastatic tissues compared to the original colon cancer tissue of the same patients, suggesting that high expression of GAPDH might play an important role in colon cancer development and metastasis. Importantly, we found that 3-bromopyruvate propyl ester (3-BrOP) preferentially inhibited GAPDH and exhibited potent activity in inducing colon cancer cell death by causing severe depletion of ATP. 3-BrOP at low concentrations (1-10 μM) inhibited GAPDH and a much higher concentration (300 μM) was required to inhibit hexokinase-2. The cytotoxic effect of 3-BrOP was associated with its inhibition of GAPDH, and colon cancer cells with loss of p53 were more sensitive to this compound. Our study suggests that GAPDH may be a potential target for colon cancer therapy.

Publication types

  • Comparative Study

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Apoptosis / drug effects
  • Blotting, Western
  • Cell Proliferation
  • Colorectal Neoplasms / metabolism*
  • Flow Cytometry
  • Gene Expression Regulation, Enzymologic / physiology*
  • Gene Expression Regulation, Neoplastic / physiology*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / antagonists & inhibitors
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism*
  • Hexokinase / antagonists & inhibitors
  • Humans
  • Immunohistochemistry
  • Liver Neoplasms / metabolism*
  • Liver Neoplasms / secondary
  • Pyruvates / pharmacology*

Substances

  • Pyruvates
  • bromopyruvate
  • Adenosine Triphosphate
  • Glyceraldehyde-3-Phosphate Dehydrogenases
  • Hexokinase