GSTM3
GSTM3 (glutathione S-transferase mu 3, also known as GST5 or GSTM3TV2) is a cytoplasmic mu-class glutathione S-transferase. It conjugates reduced glutathione to hydrophobic electrophiles, a reaction central to the detoxification of both endogenous compounds and xenobiotics. Browse Assay Genie's current range of GSTM3 research reagents below, or read on for the biology behind the target.
GSTM3 catalyses the conjugation of reduced glutathione to a wide range of exogenous and endogenous hydrophobic electrophiles. The mu class of enzymes to which it belongs acts in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. UniProt also notes that GSTM3 may govern the uptake and detoxification of endogenous compounds and xenobiotics at the testis and brain blood barriers.
The GSTM3 gene encodes a member of the GST superfamily, mu family, and is classed by HGNC within the soluble glutathione S-transferases. Mammalian cytosolic glutathione S-transferases fall into eight classes: alpha, kappa, mu, omega, pi, sigma, theta and zeta. These cytosolic forms are encoded by a supergene family distinct from the one encoding the membrane-bound forms. The GSTM3 protein is found in the cytoplasm. In mouse and rat, the orthologous genes are Gstm5 and Gstm7 respectively.
The mu-class genes are organised in a cluster on chromosome 1p13.3 and are known to be highly polymorphic. Such variation can change an individual's susceptibility to carcinogens and toxins, and can affect the toxicity and efficacy of certain drugs. Mutations in this class mu gene have been linked with a slight increase in a number of cancers, likely through exposure to environmental toxins. Alternative splicing produces multiple transcript variants. Earlier names for the gene include glutathione S-transferase M3 (brain), reflecting its original description.
GSTM3 conjugates glutathione to electrophilic carcinogens, drugs and environmental toxins, making it a useful subject for studies of cellular detoxification.
Mu-class enzymes act on products of oxidative stress, so GSTM3 is relevant to research into how cells handle reactive electrophilic by-products.
GSTM3 may govern uptake and detoxification of endogenous compounds and xenobiotics at the testis and brain blood barriers.
Polymorphism in the mu-class gene cluster alters susceptibility to carcinogens and drug toxicity or efficacy, and GSTM3 mutations are linked with a slight rise in some cancers.
GSTM3 catalyses the conjugation of reduced glutathione to many hydrophobic electrophiles, both endogenous and exogenous. This supports detoxification of carcinogens, drugs, environmental toxins and oxidative stress products. It may also govern uptake and detoxification of compounds at the testis and brain blood barriers.
The HGNC name is glutathione S-transferase mu 3, and the aliases are GST5 and GSTM3TV2. Earlier names were glutathione S-transferase M3 (brain) and glutathione S-transferase mu 3 (brain). The gene undergoes alternative splicing, which gives multiple transcript variants.
The mu-class gene cluster is highly polymorphic, and variation can alter susceptibility to carcinogens and toxins. Mutations in GSTM3 have been linked with a slight increase in a number of cancers. Mouse and rat orthologues are Gstm5 and Gstm7; check the datasheet of any product for its validated reactivity.
Other mu-class glutathione S-transferases from the same gene cluster, with related detoxification enzymes.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P21266; product specifications from Assay Genie datasheets.