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The assignment of chemokine‐chemokine receptor pairs: TARC and MIP‐1β are not ligands for human CC‐chemokine receptor 8
Author(s) -
Garlisi Charles G.,
Xiao Hong,
Tian Fang,
Hedrick Joseph A.,
Billah M. Motasim,
Egan Robert W.,
Umland Shelby P.
Publication year - 1999
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/(sici)1521-4141(199910)29:10<3210::aid-immu3210>3.0.co;2-w
Subject(s) - ccl21 , chemokine receptor , xcl2 , c c chemokine receptor type 6 , ccl17 , ccr1 , chemokine , cc chemokine receptors , ccl13 , microbiology and biotechnology , chemokine receptor ccr5 , biology , chemotaxis , cxcl16 , ccl5 , ccl7 , immunology , receptor , t cell , biochemistry , immune system , il 2 receptor
Abstract Identification of chemokine receptors and their associated ligands is crucial to the understanding of most immune reactions. Three human chemokines [I‐309, thymus and activation‐regulated chemokine (TARC) and macrophage inflammatory protein‐1β (MIP‐1β)] have been reported to be ligands for CC‐chemokine receptor 8 (CCR8). In this report, we present evidence that TARC and MIP‐1β did not bind to or induce chemotaxis through CCR8 on a stable transfected cell line (1D‐21) and did not bind to CCR8 on in vitro differentiated human CD4 + Th 2 cell cultures. Also, I‐309‐dependent calcium mobilization in 1D‐21 cells and in Th 2 cells was desensitized by I‐309 but not by MIP‐1β or TARC. These results provide strong evidence that, at physiologically relevant concentrations, I‐309 is the only known human ligand for CCR8. These data also provide a framework for suggesting minimum requirements for the assignment of chemokine receptor‐ligand pairs.