Artículos de revistas
High-affinity binding of fatty acyl-CoAs and peroxisome proliferator-CoA esters to glutathione S-transferases. Effect on enzymatic activity
Fecha
1999Registro en:
European Journal of Biochemistry, Volumen 266, Issue 1, 2018, Pages 143-150
00142956
10.1046/j.1432-1327.1999.00838.x
Autor
Silva, Cecilia
Loyola, Gloria
Valenzuela, Rodrigo
Garcia-Huidobro, Tea
Monasterio, Octavio
Bronfman, Miguel
Institución
Resumen
Acyl-CoAs are present at high concentrations within the cell, yet are strongly buffered lay specific binding proteins in order to maintain a low intracellular unbound acyl-CoA concentration, compatible with their metabolic role, their importance in cell signaling, and as protection from their detergent properties. This intracellular regulation may be disrupted by nonmetabolizables acyl-CoA esters of xenobiotics, such as peroxisome proliferators, which are formed at relatively high concentration within the liver cell. The low molecular mass acyl-CoA binding protein (ACBP) and fatty acyl-CoA binding protein (FABP) have been proposed as the buffering system for fatty acyl-CoAs. Whether these proteins also bind xenobiotic-CoA is not known. Here we have identified new liver cytosolic fatty acyl-CoA and xenobiotic-CoA binding sites as glutathione S-transferase (GST), using fluorescent polarization and a acyl-etheno-CoA derivative of the peroxisome proliferator nafenopin as ligand. Rat liver