Alterations in tyrosine protein kinase activities upon activation of human neutrophils

• Published in: Journal of leukocyte biology Vol. 49; no. 6; pp. 599 - 604
• Main Authors: Berkow, Roger L., Dodson, Robert W.
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Society for Leukocyte Biology 01.06.1991; Federation of American Societies for Experimental Biology
• Subjects: Autoradiography; Biological and medical sciences; Cell Separation; Cytosol - drug effects; Cytosol - enzymology; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Humans; Immunobiology; Myeloid cells: ontogeny, maturation, markers, receptors; N-Formylmethionine Leucyl-Phenylalanine - pharmacology; neutrophil activation; Neutrophils - drug effects; Neutrophils - enzymology; Neutrophils - physiology; Phosphorylation - drug effects; phosphotyrosine; Polynuclears; Protein-Tyrosine Kinases - metabolism; Protein-Tyrosine Kinases - physiology; stimulus response coupling; Tetradecanoylphorbol Acetate - pharmacology; Time Factors; Human; Phosphorylation; Enzymatic activity; Gel electrophoresis; Enzyme; Induction; Neutrophile; Granulocyte; Activation; Protein-tyrosine kinase
• ISSN: 0741-5400; 1938-3673
• DOI: 10.1002/jlb.49.6.599

Human neutrophils are phagocytic cells that can be activated by a variety of agonists to undergo a group of physiologic responses. This “stimulus‐response” coupling is thought to be dependent on the phosphorylation of specific proteins. We have previously shown that, in addition to the widely distributed serine and threonine protein kinases, neutrophils contain tryosine protein kinase activity in the cell cytosol and particulate fractions. When neutrophils are treated with a variety of agents, phosphorylation of both cytosolic and particulate proteins on tyrosine residues occurs. Increases in tyrosine phosphorylation may be a result of increases in the activity of tyrosine kinases or a decrease in the activity of phosphotyrosine phosphatases. In this study, we have used a novel nondenaturing polyacrylamide gel electrophoretic method to demonstrate that treatment of human neutrophils with the chemotactic peptide FMLP or the phorbol ester phorbol myristate acetate induces a time‐ and concentration‐dependent increase in the tyrosine protein kinase activity found in the cell cytosol and cell particulate fraction. The time course and concentration range over which these changes occur are similar to those seen for activation of the neutrophil oxidative burst and phosphorylation of proteins on tyrosine residues, suggesting that these events may be related.