Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2020 May 2;12(5):416.
doi: 10.3390/pharmaceutics12050416.

Glyceraldehyde-3-phosphate Dehydrogenase is a Multifaceted Therapeutic Target

Vladimir F Lazarev  1 , Irina V Guzhova  1 , Boris A Margulis  1
Affiliations
Review

Glyceraldehyde-3-phosphate Dehydrogenase is a Multifaceted Therapeutic Target

Vladimir F Lazarev et al. Pharmaceutics. .

Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme whose role in cell metabolism and homeostasis is well defined, while its function in pathologic processes needs further elucidation. Depending on the cell context, GAPDH may bind a number of physiologically important proteins, control their function and correspondingly affect the cell's fate. These interprotein interactions and post-translational modifications of GAPDH mediate its cytotoxic or cytoprotective functions in the manner of a Janus-like molecule. In this review, we discuss the functional features of the enzyme in cellular physiology and its possible involvement in human pathologies. In the last part of the article, we describe drugs that can be employed to modulate this enzyme's function in some pathologic states.

Keywords: GAPDH; cancer; diabetics; drugs; neurodegenerative diseases; treatment.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Mitsuzawa H., Kimura M., Kanda E., Ishihama A. Glyceraldehyde-3-phosphate dehydrogenase and actin associate with RNA polymerase II and interact with its Rpb7 subunit. FEBS Lett. 2005;579:48–52. doi: 10.1016/j.febslet.2004.11.045. - DOI - PubMed
    1. Seidler N.W. GAPDH: Biological Properties and Diversity (Advances in Experimental Medicine and Biology) Springer; Berlin, Germany: 2013.
    1. Lazarev V.F., Mikhaylova E.R., Dutysheva E.A., Suezov R.V., Guzhova I.V., Margulis B.A. A hydrocortisone derivative binds to GAPDH and reduces the toxicity of extracellular polyglutamine-containing aggregates. Biochem. Biophys. Res. Commun. 2017;487:723–727. doi: 10.1016/j.bbrc.2017.04.125. - DOI - PubMed
    1. Nakajima H., Amano W., Kubo T., Fukuhara A., Ihara H., Azuma Y.-T., Tajima H., Inui T., Sawa A., Takeuchi T. Glyceraldehyde-3-phosphate Dehydrogenase Aggregate Formation Participates in Oxidative Stress-induced Cell Death. J. Biol. Chem. 2009;284:34331–34341. doi: 10.1074/jbc.M109.027698. - DOI - PMC - PubMed
    1. Semenyuk P., Barinova K., Muronetz V. Glycation of α-synuclein amplifies the binding with glyceraldehyde-3-phosphate dehydrogenase. Int. J. Biol. Macromol. 2019;127:278–285. doi: 10.1016/j.ijbiomac.2019.01.064. - DOI - PubMed