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Related Experiment Videos

[Glutathione S-transferases (GSTs)]

M Sugimoto1

  • 1Second Department of Internal Medicine, Toho University School of Medicine.

Nihon Rinsho. Japanese Journal of Clinical Medicine
|May 1, 1995
PubMed
Summary
This summary is machine-generated.

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Glutathione S-transferases (GSTs) are detoxifying enzymes that neutralize harmful compounds. This review details a new nomenclature for human GST isoenzymes and their varied roles in different tissues and disease.

Area of Science:

  • Biochemistry
  • Enzymology
  • Toxicology

Context:

  • Glutathione S-transferases (GSTs) are crucial detoxifying enzymes.
  • They conjugate glutathione with electrophilic compounds, including carcinogens.
  • GSTs also bind various nonsubstrate ligands.

Purpose:

  • To introduce a new nomenclature for human GST isoenzymes.
  • To review recent investigations into GST enzyme functions.
  • To discuss the implications of different GST isoenzymes.

Summary:

  • Mammalian GSTs are classified into alpha, mu, and pi classes based on subunit composition.
  • GST-alpha is abundant in the liver.
  • GST-mu is found in the liver and lymphocytes, with variable prevalence in humans.

Related Experiment Videos

  • GST-pi is widely distributed in organs like the lung, kidney, GI tract, erythrocytes, and cancer cells.

    • Impact:

    • Understanding GST isoenzyme distribution and function is vital for toxicology and disease research.
    • The new nomenclature facilitates clearer communication and research on human GSTs.
    • Investigating GSTs offers insights into carcinogen metabolism and disease progression.