Interaction of a synthetic peptide of the interferon alpha 2 C-terminal part with human blood leukocytes. II. Effect on protein tyrosine phosphorylation.
Tyrosine phosphorylation in human blood lymphocytes was studied as a function of stimulation with concanavalin A (ConA) and treatment of the cells with interferon alpha 2 (IFN alpha 2) and/or an IFN-derived C-terminal synthetic peptide 2438 (amino acid residues 124-138). Both IFN alpha 2 and the peptide 2438 decreased the level of protein tyrosine phosphorylation in the ConA-stimulated cells. In unstimulated cells, IFN alpha 2 increased, and the peptide 2438 decreased the level of the tyrosine phosphorylation. A possible correlation of these effects with stimulation of cell proliferation is discussed.
Danilkovich
A V
AV
Moscow State University, Biological Faculty, USSR.
Kharitonenkov
A I
AI
Freze
K V
KV
Shevalier
A F
AF
Kolosova
O V
OV
Bulargina
T V
TV
Kirkin
A F
AF
Gusev
M V
MV
D015153:Blotting, Western; D002455:Cell Division; D002478:Cells, Cultured; D006801:Humans; D007370:Interferon Type I / Q000378:metabolism*; D007962:Leukocytes / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D011994:Recombinant Proteins; D014443:Tyrosine / Q000378:metabolism*
D007370:Interferon Type I; D010446:Peptide Fragments; D010455:Peptides; D011994:Recombinant Proteins; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases