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

doi:10.4049/jimmunol.157.4.1440

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CD40 ligation results in protein kinase C-independent activation of ERK and JNK in resting murine splenic B cells

Journal article

Peer reviewed

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 and Gary A Koretzky

The Journal of immunology (1950), Vol.157(4), pp.1440-1447

08/15/1996

DOI: 10.4049/jimmunol.157.4.1440

PMID: 8759724

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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.

Protein Processing, Post-Translational - drug effects

Protein Kinase C - metabolism

JNK Mitogen-Activated Protein Kinases

Female

Mice, Inbred DBA

Receptors, Antigen, B-Cell - physiology

Membrane Proteins - metabolism

Phosphorylation - drug effects

Antibodies, Monoclonal - immunology

Protein-Serine-Threonine Kinases - metabolism

CD40 Antigens - physiology

B-Lymphocytes - enzymology

Son of Sevenless Proteins

Specific Pathogen-Free Organisms

Antibodies, Monoclonal - pharmacology

Mice, Inbred C57BL

B-Lymphocytes - physiology

Protein Kinase C - antagonists & inhibitors

Spleen - cytology

Enzyme Activation - drug effects

Nerve Tissue Proteins - metabolism

B-Lymphocytes - drug effects

Animals

Signal Transduction - drug effects

Lymphocyte Activation - drug effects

Mice

Mice, Inbred BALB C

CD40 Antigens - immunology

Calcium-Calmodulin-Dependent Protein Kinases - metabolism

MAP Kinase Kinase Kinase 1

Mitogen-Activated Protein Kinases - metabolism

Details

Title: Subtitle: CD40 ligation results in protein kinase C-independent activation of ERK and JNK in resting murine splenic B cells
Creators: Yi-Yang Li - Department of Internal Medicine, College of Medicine, University of Iowa, Iowa City 52242, USA
Mekhine Baccam
Steven B Waters
Jeffrey E Pessin
Gail A Bishop
Gary A Koretzky
Resource Type: Journal article
Publication Details: The Journal of immunology (1950), Vol.157(4), pp.1440-1447
Publisher: United States
DOI: 10.4049/jimmunol.157.4.1440
PMID: 8759724
ISSN: 0022-1767
eISSN: 1550-6606
Grant note: GM53256 / NIGMS NIH HHS CA56050 / NCI NIH HHS DK33823 / NIDDK NIH HHS
Language: English
Date published: 08/15/1996
Academic Unit: Microbiology and Immunology; President
Record Identifier: 9984002392102771

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