GSTA1 Mouse

Glutathione S-Transferase Alpha 1 (GSTA1) is a member of the glutathione S-transferase (GST) family, a group of enzymes involved in the detoxification of endogenous and exogenous compounds. These enzymes catalyze the conjugation of the tripeptide glutathione to a variety of electrophilic substrates, facilitating their excretion from the body. GSTA1 is particularly significant due to its role in protecting cells from oxidative stress and its involvement in various metabolic pathways.

GSTA1 belongs to the alpha class of GSTs, which are predominantly expressed in the liver and kidney. The enzyme is composed of two subunits, each containing a glutathione-binding site and a substrate-binding site. The active site of GSTA1 facilitates the nucleophilic attack of the sulfur atom of glutathione on electrophilic groups of substrates, forming glutathione conjugates .

The primary function of GSTA1 is to detoxify harmful compounds, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. This detoxification process is crucial for maintaining cellular homeostasis and protecting cells from damage. Additionally, GSTA1 exhibits glutathione peroxidase activity, which helps in reducing lipid hydroperoxides and protecting cells from oxidative damage .

The GSTA1 gene is located on chromosome 6 in humans and chromosome 9 in mice. It is part of a cluster of similar genes and pseudogenes. The gene is highly polymorphic, with variations that can influence an individual’s ability to metabolize different drugs and susceptibility to toxins .

In mice, recombinant GSTA1 is often used in research to study the enzyme’s function and its role in various physiological and pathological processes. The recombinant form is produced by cloning the GSTA1 gene into an expression vector, which is then introduced into a host organism, such as bacteria or yeast, to produce the enzyme in large quantities .

GSTA1 plays a critical role in protecting cells from reactive oxygen species (ROS) and the products of peroxidation. By conjugating glutathione to electrophilic compounds, GSTA1 helps in the detoxification and excretion of these harmful substances. This action is particularly important in the liver, where the enzyme is abundantly expressed and involved in metabolizing bilirubin and certain anti-cancer drugs .

In addition to its detoxification role, GSTA1 is involved in hormone biosynthesis. It catalyzes the isomerization of D5-androstene-3,17-dione into D4-androstene-3,17-dione, which is a key step in the biosynthesis of steroid hormones .

Alterations in GSTA1 expression and activity have been associated with various diseases and conditions. For example, increased levels of GSTA1 have been observed in response to oxidative stress and inflammation. Polymorphisms in the GSTA1 gene can affect an individual’s response to drugs and susceptibility to diseases such as cancer .

Recombinant GSTA1 is also used as a biomarker for cellular damage. Increases in serum and urinary GSTA1 levels have been linked to hepatocyte and renal proximal tubular necrosis, respectively. This makes GSTA1 a valuable tool for monitoring tissue injury and evaluating the efficacy of therapeutic interventions .