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RESEARCH PRODUCT
Feedback Regulation of Syk by Protein Kinase C in Human Platelets
Stephanie DorschelStepan GambaryanStepan GambaryanStephanie MakhoulUlrich WalterKerstin Jurksubject
0301 basic medicineIndolesPlatelet AggregationSyk030204 cardiovascular system & hematologyenvironment and public healthMaleimideslcsh:Chemistrychemistry.chemical_compound0302 clinical medicinePhosphorylationlcsh:QH301-705.5SpectroscopyFeedback PhysiologicalKinaseConvulxinhemic and immune systemsGeneral MedicineComputer Science ApplicationsCell biologyAdenosine DiphosphateplateletsPhosphorylationbiological phenomena cell phenomena and immunityBlood Plateletschemical and pharmacologic phenomenaViper Venomsspleen tyrosine kinase (Syk)CatalysisArticleInorganic Chemistryglycoprotein VIglycoprotein Ibα03 medical and health sciencesCrotalid VenomsHumansSyk KinaseCyclic adenosine monophosphateLectins C-TypePlatelet activationPhysical and Theoretical ChemistryMolecular BiologyProtein kinase CPhospholipase C gammaOrganic Chemistryenzymes and coenzymes (carbohydrates)030104 developmental biologyProtein kinase domainchemistrylcsh:Biology (General)lcsh:QD1-999Calciumcyclic adenosine monophosphate (cAMP)protein kinase Cdescription
The spleen tyrosine kinase (Syk) is essential for immunoreceptor tyrosine-based activation motif (ITAM)-dependent platelet activation, and it is stimulated by Src-family kinase (SFK)-/Syk-mediated phosphorylation of Y352 (interdomain-B) and Y525/526 (kinase domain). Additional sites for Syk phosphorylation and protein interactions are known but remain elusive. Since Syk S297 phosphorylation (interdomain-B) was detected in platelets, we hypothesized that this phosphorylation site regulates Syk activity via protein kinase C (PKC)-and cyclic adenosine monophosphate (cAMP)-dependent pathways. ADP, the GPVI-agonist convulxin, and the GPIb&alpha
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-12-01 | International Journal of Molecular Sciences |