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Lipid peroxidation and cell cycle signaling: 4-hydroxynonenal, a key molecule in stress mediated signaling.
- Yusong Yang, Rajendra K. Sharma, Abha Sharma, S. Awasthi, Y. Awasthi
- Biology, ChemistryActa biochimica Polonica
Evidence demonstrating the modulation of UV, oxidative stress, and chemical stress mediated apoptosis by blocking lipid peroxidation by the alpha-class glutathione S-transferases (GSTs) is presented is presented which suggest an important role of these enzymes in protection against oxidative stress and a role of lipidperoxidation products in stress mediated signaling.
Human glutathione S-transferases.
Activity of four allelic forms of glutathione S-transferase hGSTP1-1 for diol epoxides of polycyclic aromatic hydrocarbons.
It is proposed that amino acid 113 functions as part of a clamp that lines the mouth of the water channel leading to the active sites of the hGSTP1-1 dimer and controls the access to substrates, and the hydrophobicity and the size of residue 113 are important in co-determining the substrate specificity of the isoenzymes.
Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties.
Data indicate that the residue in position 104 helps to define the geometry of the hydrophobic substrate-binding site, and may also influence activity by interacting with residues directly involved in substrate binding.
Physiological role of mGSTA4-4, a glutathione S-transferase metabolizing 4-hydroxynonenal: generation and analysis of mGsta4 null mouse.
Purification and properties of human erythrocyte glutathione peroxidase.
Regulation of 4-hydroxynonenal-mediated signaling by glutathione S-transferases.
Mechanisms of anticarcinogenic properties of curcumin: the effect of curcumin on glutathione linked detoxification enzymes in rat liver.
Differential catalytic efficiency of allelic variants of human glutathione S-transferase Pi in catalyzing the glutathione conjugation of thiotepa.
- S. Srivastava, S. Singhal, X. Hu, Y. Awasthi, P. Zimniak, S. Singh
- Biology, ChemistryArchives of biochemistry and biophysics
- 1 June 1999
It is reported that the allelic variants of human Pi class GST (hGSTP1-1), which differ in their primary structures at amino acids in positions 104 and/or 113, exhibit significant differences in their activity in the GSH conjugation of alkylating anticancer drug thiotepa.