H. Ogata et al., REGULATION OF INTERLEUKIN-13 RECEPTOR CONSTITUENTS ON MATURE HUMAN B-LYMPHOCYTES, The Journal of biological chemistry, 273(16), 1998, pp. 9864-9871
Human B cells stimulated through both their immunoglobulin and CD40 re
ceptors up-regulate 745 +/- 51 interleukin (IL)-13 ligand binding site
s with an affinity of 0.91 +/- 0.08 nar within 24 h. IL-13 binds prima
rily to the IL-13R alpha 1 with subsequent sequestration of the IL-4R
alpha into the complex. IL-13R alpha 1 may also be found in those rece
ptors capable of binding IL-4. gamma chain (gamma(c)) participates in
receptors capable of binding IL-4 but is not found in association with
bound IL-13, Dimeric receptors composed of the IL-4R alpha complexed
with either the IL-13R alpha 1 or gamma(c) occur simultaneously within
defined B cell populations. mRNAs for all receptor constituents are i
ncreased subsequent to immunoglobulin stimulation alone, while maximal
expression of IL-13R alpha 1 is more dependent upon co-stimulation of
immunoglobulin and CD40 receptors, mRNA levels for IL-13R alpha 1 var
y over a wider range subsequent to surface stimulation than other rece
ptor components. Although gamma(c) is not bound to IL-13 in B cells un
der the conditions evaluated, it may influence IL-13 binding by compet
ing with IL-13R alpha 1 for association/sequestration with the IL-4R a
lpha chain, IL-13R alpha 2 does not participate in the IL-13 receptor
that is up-regulated upon activation of quiescent tonsillar B lymphocy
tes, although mRNA for the protein may be found in the centroblastic f
raction of tonsillar cells.