Evidence map›Paper›PMID 25543269›Full record

ArticleCellular and molecular life sciences : CMLS2015

Syk is indispensable for CpG-induced activation and differentiation of human B cells.

Mariann Kremlitzka, Bernadett Mácsik-Valent, Anna Erdei

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

  1. B cells in cancer: functions, mechanisms and therapeutic advances.Signal transduction and targeted therapy · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Mariann KremlitzkaMTA-ELTE Immunology Research Group, Budapest, Hungary.
Bernadett Mácsik-Valent
Anna Erdei

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

B cells are efficiently activated by CpG oligodeoxynucleotides (ODNs) to produce pro-inflammatory cytokines and antibody (Ab). Here, we describe a so far unidentified, spleen tyrosine kinase (Syk)-dependent pathway, which is indispensable for CpG-induced human B cell activation. We show that triggering of B cells by CpG results in Syk and src kinase phosphorylation, proliferation, as well as cytokine and Ab production independent of the BCR. Notably, all these functions are abrogated when Syk is inhibited. We demonstrate that CpG-induced Syk activation originates from the cell surface in a TLR9-dependent manner. While inhibition of Syk does not influence the uptake of CpG ODNs, activation of the kinase is a prerequisite for the delivery of CpG into TLR9-containing endolysosomes and for the CpG-induced up-regulation of TLR9 expression. Our results reveal an alternative, Syk-dependent pathway of CpG-induced B cell stimulation, which is initiated at the plasma membrane and seems to be an upstream requirement for endosomal TLR9-driven B cell proliferation and differentiation.

Indexed as

B-LymphocytesCell DifferentiationCell ProliferationCpG IslandsHumansIntracellular Signaling Peptides and ProteinsLymphocyte ActivationMitogen-Activated Protein KinasesMyeloid Differentiation Factor 88NF-kappa BOligodeoxyribonucleotidesPhosphorylationProtein BindingProtein-Tyrosine KinasesRNA InterferenceRNA, Small InterferingIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein KinasesMYD88 protein, humanMyeloid Differentiation Factor 88NF-kappa BOligodeoxyribonucleotidesProtein-Tyrosine KinasesRNA, Small Interferingsrc-Family KinasesSyk KinaseSYK protein, humanTLR9 protein, humanToll-Like Receptor 9

Identifiers

PMID25543269
PMCPMC11113211

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.