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<p>Glutathionylation is an important Phase II biotransformation pathway that utilizes glutathione transferases (GSTs) to conjugate glutathione with reactive electrophiles represented by a great diversity in chemical structures. After further processing, the resulting metabolite is highly polar and rapidly eliminated. This pathway thus represents an important route of xenobiotic detoxification. Cats and dogs possess a combined repertoire of at least 27 cytosolic glutathione transferases belonging to the GST-A, -M, -P, -T, -Z and -O classes, with the greatest genetic diversity observed for the GSTA, GSTM, GSTP, and GSTT classes. GST transcript and protein expression have been demonstrated for most tissues in dogs, but less so in cats. In contrast to humans, these two species have fewer actively expressing GSTM genes, but a larger number of active GSTT genes. Dogs and cats also express distinct GSTP1-like and GSTT1-like enzymes. These differences in GST type and multiplicity, as well as residue changes that impact the secondary and tertiary structure of the cat and dog GST proteins, affect substrate selectivity and catalytic efficiency. Further research is required, especially in cats, to understand how species differences in glutathionylation modulate the risk of toxicity following exposure to certain drugs and environmental contaminants.</p><p></p>

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Glutathione transferases in cats and dogs: diversity, structure, and function

  • 期刊论文

  • 发表日期：

    2025年10月16日

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  • James C. Sacco

摘要

Glutathionylation is an important Phase II biotransformation pathway that utilizes glutathione transferases (GSTs) to conjugate glutathione with reactive electrophiles represented by a great diversity in chemical structures. After further processing, the resulting metabolite is highly polar and rapidly eliminated. This pathway thus represents an important route of xenobiotic detoxification. Cats and dogs possess a combined repertoire of at least 27 cytosolic glutathione transferases belonging to the GST-A, -M, -P, -T, -Z and -O classes, with the greatest genetic diversity observed for the GSTA, GSTM, GSTP, and GSTT classes. GST transcript and protein expression have been demonstrated for most tissues in dogs, but less so in cats. In contrast to humans, these two species have fewer actively expressing GSTM genes, but a larger number of active GSTT genes. Dogs and cats also express distinct GSTP1-like and GSTT1-like enzymes. These differences in GST type and multiplicity, as well as residue changes that impact the secondary and tertiary structure of the cat and dog GST proteins, affect substrate selectivity and catalytic efficiency. Further research is required, especially in cats, to understand how species differences in glutathionylation modulate the risk of toxicity following exposure to certain drugs and environmental contaminants.