VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Amino acid specificity of the phosphoprotein kinase activity of various fractions of non-histone chromatin proteins from the kidney, hepatoma and liver of rats after a single dose of diethylnitrosamine

   
Kushner V.P.
PubMed Id: 3420805
Year: 1988  Volume: 34  Issue: 3  Pages: 25-27
Amino acid specificity of phosphorylation of some nuclear non-histone proteins was studied in the fractions, eluted by 0.4-0.5 M NaCl from phosphocellulose columns, using the reaction of 33P transfer, catalized by native phosphoprotein kinase, from gamma-33P-ATP into the proteins. A number of amino acid residues, capable to reaction, were phosphorylated in the 0.4-0.5 M NaCl fraction of non-histone proteins from kidney of intact rats, from cells of hepatoma 27 and from liver cells after a single intraperitoneal administration of diethylnitrosamine. At the same time, methionine residue was markedly phosphorylated in the fraction of 0.4-0.5 M NaCl of intact rat kidney, whereas this effect was not found in the preparations of hepatoma 27 and in cells of "carcinogenous" liver tissue. As distinct from kidney non-histone proteins, proteins from the 0.4-0.5 M NaCl fraction of the latter preparations tended to exhibit tyrosine phosphokinase activity. It is well known that many of oncoproteins exhibited mainly the tyrosine-specific phosphoprotein kinase activity. The data obtained suggest that "tyrosine" shift in the preparations of non-histone proteins from tumoral cells or from rat liver cells, altered under the effect of hepatocarcinogenesis, may be an indication of functional activity of oncogenes.
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Kushner, V. P. (1988). Amino acid specificity of the phosphoprotein kinase activity of various fractions of non-histone chromatin proteins from the kidney, hepatoma and liver of rats after a single dose of diethylnitrosamine. Voprosy Meditsinskoi Khimii, 34(3), 25-27.
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