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 pep...

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Bibliographic Details
Published in:FEBS letters 1992-01, Vol.296 (3), p.271-273
Main Authors: Danilkovich, A V, Kharitonenkov, A I, Freze, K V, Shevalier, A F, Kolosova, O V, Bulargina, T V, Kirkin, A F, Gusev, M V
Format: Article
Language:English
Subjects:
Blotting, Western
Cell Division
Cells, Cultured
Humans
Interferon Type I - metabolism
Leukocytes - metabolism
Peptide Fragments - metabolism
Peptides - metabolism
Phosphorylation
Protein-Tyrosine Kinases - metabolism
Recombinant Proteins
Tyrosine - metabolism
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Summary: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.
ISSN:0014-5793