Role of initial protein phosphorylation events and localized release-activated calcium influx in B cell antigen receptor signaling.

Abstract:

:An increase in intracellular calcium concentration is one of the major initial steps in B cell activation following antigen receptor (BCR) ligation. We show herein that in C57BL/6 murine B lymphocytes and in model cell lines, BCR-mediated calcium ion (Ca(2+)) influx occurs via highly selective Ca(2+) release-activated channels, and stromal interaction molecule 1 (STIM1) plays an important role in this pathway. We also demonstrate the temporal relation between Ca(2+)-dependent signaling events and formation of the immune synapse. Our data indicate that cytoplasmic Ca(2+) levels in areas adjacent to the immune synapse differ from those in the rest of the cytoplasm. Finally, a comparison of phosphorylation patterns of BCR-triggered signaling proteins in the presence or absence of Ca(2+) revealed the unanticipated finding that initial BCR-triggered, Ca(2+)-dependent tyrosine phosphorylation events involve predominantly Ca(2+) released from intracellular stores and that influx-derived Ca(2+) is not essential. This suggests a different role for this phase of Ca(2+) influx.

journal_name

J Leukoc Biol

authors

Lyubchenko T,Nielsen JP,Miller SM,Liubchenko GA,Holers VM

doi

10.1189/jlb.0308193

subject

Has Abstract

pub_date

2009-02-01 00:00:00

pages

298-309

issue

2

eissn

0741-5400

issn

1938-3673

pii

jlb.0308193

journal_volume

85

pub_type

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