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*
Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892; and
Laboratory of Retrovirus Research, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892
We isolated cDNAs for a chemokine receptor-related protein having
the database designation GPR-9-6. Two classes of cDNAs were identified
from mRNAs that arose by alternative splicing and that encode receptors
that we refer to as CCR9A and CCR9B. CCR9A is predicted to contain 12
additional amino acids at its N terminus as compared with CCR9B. Cells
transfected with cDNAs for CCR9A and CCR9B responded to the chemokine
CC chemokine ligand 25 (CCL25)/thymus-expressed chemokine
(TECK)/chemokine ß-15 (CKß-15) in assays for both calcium flux and
chemotaxis. No other chemokines tested produced responses specific for
the cDNA-transfected cells. mRNA for CCR9A/B is expressed predominantly
in the thymus, coincident with the expression of CCL25, and highest
expression for CCR9A/B among thymocyte subsets was found in
CD4+CD8+ cells. mRNAs encoding the A and B
forms of the receptor were expressed at a ratio of 
10:1 in
immortalized T cell lines, in PBMC, and in diverse populations of
thymocytes. The EC50 of CCL25 for CCR9A was lower than that
for CCR9B, and CCR9A was desensitized by doses of CCL25 that failed to
silence CCR9B. CCR9 is the first example of a chemokine receptor in
which alternative mRNA splicing leads to proteins of differing
activities, providing a mechanism for extending the range of
concentrations over which a cell can respond to increments in the
concentration of ligand. The study of CCR9A and CCR9B should enhance
our understanding of the role of the chemokine system in T cell
biology, particularly during the stages of thymocyte
development.
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