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J. Biol. Chem., Vol. 277, Issue 32, 29283-29293, August 9, 2002
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From the A novel member of the
EGF-TM7 family, mEMR4, was identified and characterized. The
full-length mouse EMR4 cDNA encodes a predicted 689-amino acid
protein containing two epidermal growth factor (EGF)-like modules, a
mucin-like spacer domain, and a seven-transmembrane domain with a
cytoplasmic tail. Genetic mapping established that mEMR4 is localized in the distal region of mouse
chromosome 17 in close proximity to another EGF-TM7 gene,
F4/80 (Emr1). Similar to
F4/80, mEMR4 is predominantly
expressed on resident macrophages. However, a much lower expression
level was also detected in thioglycollate-elicited peritoneal
neutrophils and bone marrow-derived dendritic cells. The expression of
mEMR4 is up-regulated following macrophage activation in
Biogel and thioglycollate-elicited peritoneal macrophages. Similarly,
mEMR4 is over-expressed in TNF- The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY032690.
EMR4, a Novel Epidermal Growth Factor (EGF)-TM7
Molecule Up-regulated in Activated Mouse Macrophages, Binds to a
Putative Cellular Ligand on B Lymphoma Cell Line A20*
§¶,
,**,§§,§§,**, and§¶¶
Sir William Dunn School of
Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE,
United Kingdom and Biology and
Biotechnology Research Program, Lawrence Livermore National Laboratory,
Livermore, California 94550
-treated resident peritoneal macrophages, whereas interleukin-4 and -10 dramatically reduce the expression. mEMR4 was found to undergo proteolytic processing within the extracellular stalk region resulting in two protein subunits
associated noncovalently as a heterodimer. The proteolytic cleavage
site was identified by N-terminal amino acid sequencing and located at
the conserved GPCR (G
protein-coupled receptor) proteolytic site in the extracellular region. Using multivalent biotinylated mEMR4-mFc fusion proteins as a probe, a putative cell
surface ligand was identified on a B lymphoma cell line, A20, in a
cell-binding assay. The mEMR4-ligand interaction is Ca2+-independent and is mediated predominantly by the
second EGF-like module. mEMR4 is the first EGF-TM7 receptor known to
mediate the cellular interaction between myeloid cells and B cells.
*
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.
Supported by a University Challenge Seed Fund award
from the University of Oxford.
**
Supported by grants from the Medical Research Council, UK.
§§
The work of these authors was performed under the auspices of the
United States Department of Energy, Office of Biological and
Environmental Research, at the University of California,
Lawrence Livermore National Laboratory, under Contract No.
W-7405-Eng-48.
¶¶
Supported by a research grant from Celltech
R&D. To whom correspondence should be addressed: Sir William Dunn
School of Pathology, University of Oxford, South Parks Road, Oxford,
OX1 3RE, UK. Tel.: 44-1865-275532; Fax: 44-1865-275515; E-mail:
hlin@molbiol.ox.ac.uk.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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