BIOMAT Database Logo BIOMAT Database Logo

p72syk tyrosine kinase is activated by oxidizing conditions that induce lymphocyte tyrosine phosphorylation and Ca2+ signals. 1993

G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121.

We have used H2O2 as a pharmacologic agent to examine the effects of oxidizing conditions on lymphocyte signal pathways. Treatment of Ramos cells with 5-10 mM H2O2 gave rapid and strong tyrosine phosphorylation of multiple cellular proteins and activation of p72syk to levels equal to or greater than that observed upon surface Ig cross-linking. Strong Ca2+ signals that could be blocked by the tyrosine kinase inhibitor herbimycin A were also observed under these conditions. However, there was no increase in activity for the Src family kinases p56lck, p59fyn, or p56/p53lyn. Our findings that the p72syk tyrosine kinase responds to H2O2 treatment of cells suggest that this kinase is likely to contribute to cellular tyrosine phosphorylation and calcium signaling induced by oxidizing conditions. Furthermore, H2O2 may be useful as a pharmacologic agent to distinguish the effects of p72syk-related kinases from those of Src family kinases.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008214 Lymphocytes White blood cells formed in the body's lymphoid tissue. The nucleus is round or ovoid with coarse, irregularly clumped chromatin while the cytoplasm is typically pale blue with azurophilic (if any) granules. Most lymphocytes can be classified as either T or B (with subpopulations of each), or NATURAL KILLER CELLS. Lymphoid Cells,Cell, Lymphoid,Cells, Lymphoid,Lymphocyte,Lymphoid Cell
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011233 Precipitin Tests Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate. Precipitin Test,Test, Precipitin,Tests, Precipitin
D011505 Protein-Tyrosine Kinases Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors. Tyrosine Protein Kinase,Tyrosine-Specific Protein Kinase,Protein-Tyrosine Kinase,Tyrosine Kinase,Tyrosine Protein Kinases,Tyrosine-Specific Protein Kinases,Tyrosylprotein Kinase,Kinase, Protein-Tyrosine,Kinase, Tyrosine,Kinase, Tyrosine Protein,Kinase, Tyrosine-Specific Protein,Kinase, Tyrosylprotein,Kinases, Protein-Tyrosine,Kinases, Tyrosine Protein,Kinases, Tyrosine-Specific Protein,Protein Kinase, Tyrosine-Specific,Protein Kinases, Tyrosine,Protein Kinases, Tyrosine-Specific,Protein Tyrosine Kinase,Protein Tyrosine Kinases,Tyrosine Specific Protein Kinase,Tyrosine Specific Protein Kinases
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D004792 Enzyme Precursors Physiologically inactive substances that can be converted to active enzymes. Enzyme Precursor,Proenzyme,Proenzymes,Zymogen,Zymogens,Precursor, Enzyme,Precursors, Enzyme
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Protein-tyrosine kinase p72syk is activated by thrombin and is negatively regulated through Ca2+ mobilization in platelets.
February 1993, The Journal of biological chemistry,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Protein-tyrosine kinase p72syk is activated by wheat germ agglutinin in platelets.
June 1992, Biochemical and biophysical research communications,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Protein-tyrosine kinase p72syk is activated by platelet activating factor in platelets.
December 1994, Thrombosis and haemostasis,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Protein-tyrosine kinase p72syk is activated by thromboxane A2 mimetic U44069 in platelets.
November 1993, Biochemical and biophysical research communications,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Xenopus MAP kinase activator is a serine/threonine/tyrosine kinase activated by threonine phosphorylation.
August 1992, The EMBO journal,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
The tyrosine phosphorylation of a p72syk-like protein in activated murine resident peritoneal macrophages.
January 1995, Cellular & molecular biology research,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Conformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides.
April 1996, Molecular and cellular biology,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Tyrosine phosphorylation and p72syk activation by an anti-glycoprotein Ib monoclonal antibody.
March 1997, Blood,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
B lymphocyte activation is accompanied by phosphorylation of a 72-kDa protein-tyrosine kinase.
August 1991, The Journal of biological chemistry,
G L Schieven, and J M Kirihara, and D L Burg, and R L Geahlen, and J A Ledbetter
Activation of protein tyrosine kinase p72syk by Fc epsilon RI aggregation in rat basophilic leukemia cells. p72syk is a minor component but the major protein tyrosine kinase of pp72.
June 1994, The Journal of biological chemistry,
Copied contents to your clipboard!