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

Molecules. 2023 Aug 21;28(16):6163. doi: 10.3390/molecules28166163.

Abstract

Cancer involves a series of diseases where cellular growth is not controlled. Cancer is a leading cause of death worldwide, and the burden of cancer incidence and mortality is rapidly growing, mainly in developing countries. Many drugs are currently used, from chemotherapeutic agents to immunotherapy, among others, along with organ transplantation. Treatments can cause severe side effects, including remission and progression of the disease with serious consequences. Increased glycolytic activity is characteristic of cancer cells. Triosephosphate isomerase is essential for net ATP production in the glycolytic pathway. Notably, some post-translational events have been described that occur in human triosephosphate isomerase in which functional and structural alterations are provoked. This is considered a window of opportunity, given the differences that may exist between cancer cells and their counterpart in normal cells concerning the glycolytic enzymes. Here, we provide elements that bring out the potential of triosephosphate isomerase, under post-translational modifications, to be considered an efficacious target for treating cancer.

Keywords: S-nitrosylation; deamidation; glycolysis; phosphorylation; post-translational modification.

Publication types

  • Review

MeSH terms

  • Cell Cycle
  • Cell Proliferation
  • Humans
  • Neoplasms* / drug therapy
  • Protein Processing, Post-Translational
  • Triose-Phosphate Isomerase* / genetics

Substances

  • Triose-Phosphate Isomerase