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(Journal of Leukocyte Biology. 2001;69:831-840.)
© 2001 by Society for Leukocyte Biology

Protein kinase C {theta} is expressed in mast cells and is functionally involved in Fc{varepsilon} receptor I signaling

Yin Liu*, Caroline Graham*, Valentino Parravicini2, Martin J. Brown*, Juan Rivera2 and Stephen Shaw*

* Experimental Immunology Branch, National Cancer Institute, and
{dagger} Section on Chemical Immunology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland

Correspondence: Stephen Shaw. National Cancer Institute, 9000 Rockville Pike, Bldg. 10/4B36, Bethesda, MD 20892. E-mail: sshaw{at}nih.gov

We investigated possible expression and function in mast cells of protein kinase C (PKC) {theta}, a member of the PKC family with demonstrated function in a limited range of cell types. We found that PKC {theta} is expressed in bone marrow-derived mast cells and in the RBL-2H3 mast cell line. PKC {theta} underwent translocation to the membrane in response to Fc{varepsilon} receptor I (Fc{varepsilon}R I) activation. Receptor activation induced phosphorylation of PKC {theta}. The tyrosine phosphorylation of PKC {theta} is delayed relative to PKC {delta} and coincides temporally with PKC {theta} association with c-src family members Lyn and Src. Studies of RBL-2H3 cells transduced with PKC {theta} constructs indicated a role for PKC {theta} in receptor-induced activation of extracellular regulated kinases, interleukin-3 gene transcription, and degranulation in response to antigen stimulation. These studies extend the known functions of PKC{theta} to another important immune cell type and indicate the concurrent participation of multiple PKCs in the Fc{varepsilon}R I-mediated response of mast cells.

Key Words: mast cells • kinases • protein • signal transduction • Fc receptors




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