CDB15:0000258 CCL5 — CCR4
Experimentally validated in Human, Mixed species; Orthology-inferred in Human, Mouse, Rat, Frog, Chicken, Macaque, Pig, Dog, Cow, Chimp, Horse, Marmoset
Title
Journal:; Year Published:
Abstract
Selective CCL5/RANTES-induced mast cell migration through interactions with chemokine receptors CCR1 and CCR4.
Biochemical and biophysical research communications, 2002; PubMed, Homo sapiens CCL5 — Homo sapiens CCR4
ABSTRACT: Mast cells (MCs) accumulate at sites of allergic mucosal inflammation where they act as central effector and regulatory cells. Because chemokines are of vital importance in directing inflammatory leukocytes to the sites of inflammations, we have investigated the expression and function of CC-chemokine receptor (CCR) on human MCs. Two previously unrecognized MC-chemokine receptors, CCR1 and CCR4, could be identified on cord blood-derived MCs (CBMCs). CCR1 and CCR4 expressed on CBMCs exhibited a unique response profile. Of seven CCR1 and CCR4 agonists tested, only CCL5/RANTES act as an agonist inducing chemotaxis. The migration could be partially blocked by specific antibodies against CCR1 or CCR4, while a complete inhibition was achieved when both CCR1 and CCR4 were blocked. These results demonstrate that both CCR1 and CCR4 are functional receptors on human mast cells with capacity to mediate migration towards CCL5.
Molecular cloning of murine CC CKR-4 and high affinity binding of chemokines to murine and human CC CKR-4.
Biochemical and biophysical research communications, 1996; PubMed, Homo sapiens CCL5 — Homo sapiens CCR4
ABSTRACT: We have cloned the murine homologue of human CC Chemokine Receptor-4 (CC CKR-4). In equilibrium competition binding assays performed in undifferentiated HL-60 cells transfected with human and murine CC CKR-4 cDNA, the IC50 values for the binding of [125I]macrophage inflammatory protein-1 alpha to human and murine CC CKR-4 were 14.5 +/- 9.0 nM and 10.1 +/- 3.0 nM, respectively, and the IC50 values for the binding of [125I]RANTES to human and murine CC CKR-4 were 9.3 +/- 3.0 nM and 5.7 +/- 2.6 nM, respectively. The cDNA clone for murine CC CKR-4 is 1531 bp, and the largest open reading frame encodes a protein of 360 amino acids that is 85% identical to human CC CKR-4. Murine CC CKR-4 was detected in the thymus and T-cell lines by Northern blot analysis. This first report of direct binding of chemokines to CC CKR-4 demonstrates that the highly homologous human and murine receptors have similar binding characteristics and tissue distribution.