Glutathione S-transferase Mu 2, also known as GST class-mu 2, GSTM2-2 and GSTM2, is a cytoplasm protein which belongs to the GST superfamily and Mu family. GSTM2 / GST4 contains one ,GST C-terminal domain and one ,GST N-terminal domain. The glutathione S-transferases (GSTs) are a multigene family of enzymes largely involved in the detoxification of chemicals. Eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. ,Butyrate, an important luminal component produced from fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2. Butyrate may act chemoprotectively by increasing detoxification capabilities in the colon mucosa.
Glutathione S-Transferases (GSTs) are members of the phase II detoxification enzyme family that conjugate glutathione to various electrophilic compounds, including metabolites generated by oxidative processes in the body, environmental toxins or carcinogens, and anti-cancer drugs. GSTP1 is a cytosolic protein that belongs to pi class of the GST superfamily. It is crystallized as a homodimer, but also exists in solution as an equilibrium mixture of monomer and dimer, depending on the protein concentration. Four genetic variants of GSTP1 with different enzymatic activities have been identified, which indicates the particular allelic form expressed in tissues could contribute to variation in catalytic efficiency and biological functions. Genetic polymorphisms and expression patterns of GSTP1 have been associated with a variety of effects on human cancer, anti-cancer drug resistance, and asthma. In addition to its role as a drug-metabolizing enzyme, GSTP1 has ligand binding properties and regulates kinase signaling pathways through protein-protein interactions.
HepaCAM2 belongs to the immunoglobulin family. HepaCAM2, together with HEPACAM1, are cell adhesion molecules. HEPACAM1 modulates cell adhesion and migration. It also inhibits cancer cell growth. HepaCAM2 contains 2 Ig-like C2-type (immunoglobulin-like) domains. The immunoglobulin domain is a type of protein domain that consists of a 2-layer sandwich of between 7 and 9 antiparallel β-strands arranged in two β-sheets with a Greek key topology. Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions.
Epidermal growth factor receptor 2 (HER2), also known as ErbB2, NEU, and CD340, is a type I membrane glycoprotein, and belongs to the epidermal growth factor (EGF) receptor family. HER2 protein cannot bind growth factors due to the lacking of ligand binding domain of its own and autoinhibited constitutively. However, HER2 forms a heterodimer with other ligand-bound EGF receptor family members, therefore stabilizes ligand binding and enhances kinase-mediated activation of downstream molecules. HER2 plays a key role in development, cell proliferation and differentiation. HER2 gene has been reported to associate with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate, ovarian, lung cancers and so on.
ERBB2 belongs to the protein kinase superfamily, Tyr protein kinase family and EGF receptor subfamily. It contains a protein kinase domain. ERBB2 is widely expressed in epithelial cells, and amplification and/or overexpression of ErbB2 has been reported associated with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate and ovarian cancers. Rat ERBB2 is an essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. ErbB2 mediates signalling pathways which involve mitogen-activated protein kinase and phosphatidylinositol-3 kinase, this receptor plays a key role in development, cell proliferation and differentiation.
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