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Updated: Jul 18, 2025

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Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational

Sergio Enríquez-Flores1, Ignacio De la Mora-De la Mora1, Itzhel García-Torres1

  • 1Laboratorio de Biomoléculas y Salud Infantil, Instituto Nacional de Pediatría, Secretaría de Salud, Mexico City 04530, Mexico.

Molecules (Basel, Switzerland)
|August 26, 2023
PubMed

Insights

Triosephosphate isomerase, altered by post-translational modifications, shows promise as a novel cancer treatment target. Targeting this glycolytic enzyme exploits cancer cell differences for potential therapeutic strategies.

Area of Science:

  • Biochemistry
  • Oncology
  • Molecular Biology

Background:

  • Cancer is a global health challenge with increasing incidence and mortality, particularly in developing nations.
  • Current cancer treatments like chemotherapy and immunotherapy have limitations and severe side effects.
  • Cancer cells exhibit elevated glycolytic activity, distinguishing them from normal cells.

Purpose of the Study:

  • To explore the potential of triosephosphate isomerase (TPI) as a therapeutic target in cancer treatment.
  • To investigate the role of post-translational modifications in TPI's function within cancer cells.

Main Methods:

  • Analysis of glycolytic pathway enzymes in cancer cells.
  • Examination of post-translational modifications in human triosephosphate isomerase.
  • Comparative study of TPI in cancer versus normal cells.

Main Results:

  • Increased glycolytic activity is a hallmark of cancer cells.
  • Triosephosphate isomerase is crucial for ATP production via glycolysis.
  • Post-translational modifications can alter triosephosphate isomerase structure and function.

Conclusions:

  • Triosephosphate isomerase, particularly when modified post-translationally, represents a promising target for cancer therapy.
  • Exploiting differences in glycolytic enzymes between cancer and normal cells offers a potential therapeutic window.
Keywords:
S-nitrosylationdeamidationglycolysisphosphorylationpost-translational modification

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