During the course of the above-mentioned study, they found interactions between Btk and protein kinase C (PKC)-b and terreic acid as a novel Btk inhibitor that blocked Btk-PKC-b interactions. Their study also showed that PKC-b and Akt are essential for degranulation and cytokine production via activation of several transcription factors. These studies established how cytokine production is regulated by FceRI-stimulated mast cells.
Selected References
Yao, L., Kawakami, Y., and Kawakami, T. The pleckstrin homology domain of Btk tyrosine kinase interacts with protein kinase C. Proc. Natl. Acad. Sci. USA 91:9175-9179, 1994
Kitaura, J., Asai, K., Maeda-Yamamoto, M., Kawakami, Y., Kikkawa, U., and Kawakami, T. Akt-dependent cytokine production in mast cells. J. Exp. Med. 192:729-739, 2000.
Kawakami, Y., Kitaura, J., Hartman, S. E., Lowell, C. A., Siraganian, R. P., and Kawakami, T.
Regulation of protein kinase CbI by two protein-tyrosine kinases, Btk and Syk. Proc. Natl. Acad. Sci. USA. 97:7423-7428, 2000.
Kawakami, Y., Kitaura, J., Yao, L., McHenry, R. W., Kawakami, Y., Newton, A. C., Kang, S., Kato, R. M., Leitges, M., Rawlings, D. J., and Kawakami, T. A Ras activation pathway dependent on Syk phosphorylation of protein kinase C. Proc. Natl. Acad. Sci. USA. 100:9470-9475, 2003.