CD40 Ligation Results in Protein Kinase C-Independent Activation of ERK and JNK in Resting Murine Splenic B Cells

Yi Yang Li, Mekhine Baccam, Steven B. Waters, Jeffrey E. Pessin, Gail A. Bishop, Gary A. Koretzky

Research output: Contribution to journalArticle

86 Scopus citations

Abstract

CD40 is a 45- to 50-kDa transmembrane glycoprotein that plays an important role in B cell proliferation, survival, memory, and Ig isotype switching. How CD40 engagement couples to these distal events in B cell activation remains poorly understood. In this study, we have examined signal transduction events mediated by CD40 cross-linking in resting murine splenic B cells. In comparison to signaling via the B cell Ag receptor (BCR), CD40 cross-linking was less effective at activating protein tyrosine kinases. Interestingly, however, CD40 engagement resulted in the phosphorylation of both extracellular signal-regulated protein kinase (ERK) and the Ras guanine nucleotide exchange factor, Son of sevenless. In addition, both ERK and c-Jun NH2-terminal kinase activities were increased after both CD40 and BCR ligation. Overnight treatment of cells with phorbol ester as well as pharmacologic inhibitors of protein kinase C abrogated these signaling events after BCR treatment; however, no effect was seen on CD40-mediated activation of ERK or c-Jun NH2-terminal kinase, suggesting that the BCR and CD40 differentially utilize protein kinase C to couple with these signaling pathways.

Original languageEnglish (US)
Pages (from-to)1440-1447
Number of pages8
JournalJournal of Immunology
Volume157
Issue number4
StatePublished - Aug 15 1996
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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    Li, Y. Y., Baccam, M., Waters, S. B., Pessin, J. E., Bishop, G. A., & Koretzky, G. A. (1996). CD40 Ligation Results in Protein Kinase C-Independent Activation of ERK and JNK in Resting Murine Splenic B Cells. Journal of Immunology, 157(4), 1440-1447.