CCL19 is a specific ligand of the constitutively recycling atypical human chemokine receptor CRAM-B (original) (raw)

Leick, M., Catusse, J., Follo, M., Nibbs, R.J. ORCID: https://orcid.org/0000-0002-8150-0044, Hartmann, T.N., Veelken, H. and Burger, M.(2010) CCL19 is a specific ligand of the constitutively recycling atypical human chemokine receptor CRAM-B.Immunology, 129(4), pp. 536-546. (doi: 10.1111/j.1365-2567.2009.03209.x)

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Publisher's URL: http://dx.doi.org/10.1111/j.1365-2567.2009.03209.x

Abstract

The human chemokine receptor CRAM (chemokine receptor on activated macrophages), encoded by the gene CCRL2, is a new candidate for the atypical chemokine receptor family that includes the receptors DARC, D6 and chemocentryx chemokine receptor (CCX-CKR). CRAM is maturation-stage-dependently expressed on human B lymphocytes and its surface expression is up-regulated upon short-term CCL5 exposure. Here, we demonstrate that the homeostatic chemokine CCL19 is a specific ligand for CRAM. In radioactive labelling studies CCL19 bound to CRAM-expressing cells with an affinity similar to the described binding of its other receptor CCR7. In contrast to the known CCL19/CCR7 ligand/receptor pair, CRAM stimulation by CCL19 did not result in typical chemokine-receptor-dependent cellular activation like calcium mobilization or migration. Instead, we demonstrate that CRAM is constitutively recycling via clathrin-coated pits and able to internalize CCL19 as well as anti-CRAM antibodies. As this absence of classical chemokine receptor responses and the recycling and internalization features are characteristic for non-classical chemokine receptors, we suggest that CRAM is the newest member of this group. As CCL19 is known to be critically involved in lymphocyte and dendritic cell trafficking, CCL19-binding competition by CRAM might be involved in modulating these processes.

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