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J. Biol. Chem., Vol. 277, Issue 50, 49047-49054, December 13, 2002
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From the Department of Microbiology and Immunology, Stritch School
of Medicine, Loyola University Chicago, Maywood, Illinois 60153
The unfolded protein
response pathway (UPR) is believed to detect and compensate
for excessive protein accumulation in the endoplasmic reticulum (ER).
The UPR can be induced by pharmacological agents that perturb ER
functions, but may also occur during cellular developmental processes
such as the transition of B-lymphocytes into antibody-secreting plasma
cells. Here we show that major UPR components are activated in B cells
stimulated to secrete antibody. Increased expression of UPR targets
including the ER chaperones BiP and GRP94 and the transcription factor
XBP-1 initiates early in the differentiation program prior to
up-regulated synthesis of Ig chains. Furthermore, these same kinetics
are observed during differentiation for cleavage of the ER-localized
ATF6
Activation of an Unfolded Protein Response during Differentiation
of Antibody-secreting B Cells*
protein and splicing of XBP-1 mRNA to generate
p50ATF6 and p54XBP-1, the two known UPR transcriptional activators.
All of these UPR events reach maximal levels once Ig synthesis and
secretion are markedly induced. Interestingly, these events are not
accompanied by expression of CHOP, a transcription factor induced by ER
stress agents commonly used to investigate the UPR. These results
suggest that a physiological UPR elicited during differentiation of
B-lymphocytes into high-rate secretory cells may be distinct from the
UPR defined by agents that disrupt protein maturation in the
ER.
*
This work was supported by National Institutes of Health
Grant GM61970 (to J. W. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 708-216-5816;
Fax: 708-216-9574; E-mail: jbrewer@lumc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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