Premium
Alterations in Tyrosine Protein Kinase Activities Upon Activation of Human Neutrophils
Author(s) -
Berkow Roger L.,
Dodson Robert W.
Publication year - 1991
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.49.6.599
Subject(s) - tyrosine phosphorylation , phosphorylation , protein tyrosine phosphatase , tyrosine , biology , biochemistry , cytosol , protein phosphorylation , protein kinase c , tyrosine kinase , serine , kinase , microbiology and biotechnology , protein kinase a , signal transduction , enzyme
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.