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(Received for publication, January 31, 1997, and in revised form, March 24, 1997)
From the Liver and
activation-regulated chemokine
(LARC) is a recently identified CC chemokine that is expressed mainly
in the liver. LARC functions as a selective chemoattractant for
lymphocytes that express a class of receptors specifically binding to
LARC with high affinity. To identifiy the receptor for LARC, we
examined LARC-induced calcium mobilization in cells stably expressing
five CC chemokine receptors (CCR1-CCR5) and five orphan
seven-transmembrane receptors. LARC specifically induced calcium flux
in K562 cells as well as 293/EBNA-1 cells stably expressing an orphan
receptor GPR-CY4. LARC induced migration in 293/EBNA-1 cells stably
expressing GPR-CY4 with a bi-modal dose-response curve. LARC fused with
secreted alkaline phosphatase (LARC-SEAP) bound specifically to Raji
cells stably expressing GPR-CY4 with a Kd of 0.9 nM. Only LARC but not five other CC chemokines (MCP-1,
RANTES, MIP-1
Volume 272, Number 23,
Issue of June 6, 1997
pp. 14893-14898
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
,
Shionogi Institute for Medical Science,
2-5-1 Mishima, Settsu-shi, Osaka 566, Japan and the Departments of
§ Biochemistry and ¶ Internal Medicine, Kumamoto
University Medical School, Honjo, Kumamoto 860, Japan
, MIP-1
, and TARC) competed with LARC-SEAP for
binding to GPR-CY4. By Northern blot analysis, GPR-CY4 mRNA was
expressed mainly in speen, lymph nodes, Appendix, and fetal liver among
various human tissues. Among various leukocyte subsets, GPR-CY4
mRNA was detected in lymphocytes (CD4+ and
CD8+ T cells and B cells) but not in natural killer cells,
monocytes, or granulocytes. Expression of GPR-CY4 mRNA in
CD4+ and CD8+ T cells was strongly up-regulated
by IL-2. Taken together, GPR-CY4 is the specific receptor for LARC
expressed selectively on lymphocytes, and LARC is a unique functional
ligand for GPR-CY4. We propose GPR-CY4 to be designated as CCR6.
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