[Glutathione S-transferase P1-1 in normal and cancerous lung tissue: properties, function, and possible mechanisms for regulating activity].
Different forms of one of the enzymes catalyzing the xenobiotic metabolism, glutathione S-transferase P1-1 (GST P1-1), purified from normal and tumoral lung tissues, are described. Statistically significant (p < 0.05) increasing of enzyme activity in tumour, as compared with normal tissue, is shown. Molecular weights and isoelectric points of the enzyme two forms were characterized. Statistically significant increasing in the concentration of fatty acids with C = 18 bound to GST P1-1 in tumour tissues, was demonstrated. The possibility of regulation of GST P1-1 activity, as well as the level of its phosphorylation on serine and threonine, under the influence of the epidermal growth factor, is shown.
Bulavin
D V
DV
Karpishchenko
A I
AI
Gubanov
A I
AI
Reshetov
A V
AV
D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D008168:Lung / Q000201:enzymology*; D008175:Lung Neoplasms / Q000378:metabolism*
D005982:Glutathione Transferase