Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells. 1996

P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
National Institute for Medical Research, London, UK.

Activation of the high affinity IgE receptor (Fc epsilon RI) of mast cells, a member of the antigen receptor family, leads to the release of allergic mediators, a critical event in the onset of immediate hypersensitivity. Stimulation of Fc epsilon RI results in the rapid association and activation of the Syk tyrosine kinase. Using Syk-deficient mast cells we show that they fail to degranulate, synthesize leukotrienes and secrete cytokines when stimulated through Fc epsilon RI, conclusively demonstrating an essential role for Syk in Fc epsilon RI signalling. Furthermore, our data strongly supports a model of Fc epsilon RI engagement leading to the sequential activation of the tyrosine kinases Lyn and then Syk. A similar mechanism is likely to apply to signal transduction through all members of the antigen receptor family.

UI MeSH Term Description Entries
D008407 Mast Cells Granulated cells that are found in almost all tissues, most abundantly in the skin and the gastrointestinal tract. Like the BASOPHILS, mast cells contain large amounts of HISTAMINE and HEPARIN. Unlike basophils, mast cells normally remain in the tissues and do not circulate in the blood. Mast cells, derived from the bone marrow stem cells, are regulated by the STEM CELL FACTOR. Basophils, Tissue,Basophil, Tissue,Cell, Mast,Cells, Mast,Mast Cell,Tissue Basophil,Tissue Basophils
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
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
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D004792 Enzyme Precursors Physiologically inactive substances that can be converted to active enzymes. Enzyme Precursor,Proenzyme,Proenzymes,Zymogen,Zymogens,Precursor, Enzyme,Precursors, Enzyme
D000072377 Syk Kinase An SH2 domain-containing non-receptor tyrosine kinase that regulates signal transduction downstream of a variety of receptors including B-CELL ANTIGEN RECEPTORS. It functions in both INNATE IMMUNITY and ADAPTIVE IMMUNITY and also mediates signaling in CELL ADHESION; OSTEOGENESIS; PLATELET ACTIVATION; and vascular development. SYK Tyrosine Kinase,Spleen Tyrosine Kinase,Kinase, SYK Tyrosine,Kinase, Spleen Tyrosine,Kinase, Syk,Tyrosine Kinase, SYK,Tyrosine Kinase, Spleen
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001619 beta-N-Acetylhexosaminidases A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease. beta-N-Acetylhexosaminidase,N-Acetyl-beta-D-hexosaminidase,beta-Hexosaminidase,beta-N-Acetyl-D-hexosaminidase,beta-N-Acetyl-hexosaminidase,N Acetyl beta D hexosaminidase,beta Hexosaminidase,beta N Acetyl D hexosaminidase,beta N Acetyl hexosaminidase,beta N Acetylhexosaminidase,beta N Acetylhexosaminidases
D012701 Serotonin A biochemical messenger and regulator, synthesized from the essential amino acid L-TRYPTOPHAN. In humans it is found primarily in the central nervous system, gastrointestinal tract, and blood platelets. Serotonin mediates several important physiological functions including neurotransmission, gastrointestinal motility, hemostasis, and cardiovascular integrity. Multiple receptor families (RECEPTORS, SEROTONIN) explain the broad physiological actions and distribution of this biochemical mediator. 5-HT,5-Hydroxytryptamine,3-(2-Aminoethyl)-1H-indol-5-ol,Enteramine,Hippophaine,Hydroxytryptamine,5 Hydroxytryptamine
D015289 Leukotrienes A family of biologically active compounds derived from arachidonic acid by oxidative metabolism through the 5-lipoxygenase pathway. They participate in host defense reactions and pathophysiological conditions such as immediate hypersensitivity and inflammation. They have potent actions on many essential organs and systems, including the cardiovascular, pulmonary, and central nervous system as well as the gastrointestinal tract and the immune system. Leukotriene

Related Publications

P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
May 1991, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
June 1998, Journal of biochemistry,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
November 1999, Nature,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
July 1996, The Journal of experimental medicine,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
June 2000, International archives of allergy and immunology,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
February 2000, International immunology,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
January 2014, PloS one,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
January 1983, Contemporary topics in molecular immunology,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
November 2019, Toxicology and applied pharmacology,
P S Costello, and M Turner, and A E Walters, and C N Cunningham, and P H Bauer, and J Downward, and V L Tybulewicz
January 2001, Immunology letters,
Copied contents to your clipboard!