Selective binding of the truncated form of the chemokine CKbeta8 (25-99) to CC chemokine receptor 1(CCR1)

Biochem Pharmacol. 2000 Mar 1;59(5):591-6. doi: 10.1016/s0006-2952(99)00354-8.


Human CC chemokine receptor 1 (CCR1) has been proposed as a receptor for CKbeta8. To obtain conclusive evidence, binding-displacement studies of 125I-CKbeta8 (25-99) were performed on membranes of Chinese hamster ovary cells expressing human CCR1. The Ic50 for displacement of 125I-CKbeta8 (25-99) with CKbeta8 (25-99) was 0.22 nM. The longer forms of CKbeta8 (24-99 and 1-99) also displaced 125I-CKbeta8, with Ic50 values of 6.5 and 16 nM, respectively. Displacement profiles of 125I-CKbeta8 (25-99) on freshly prepared human monocytes indicated that CCR1 was the major receptor for CKbeta8. We conclude that CCR1 is a receptor for different-length CKbeta8 and that CKbeta8 (25-99) has a similar affinity for CCR1 as macrophage inflammatory protein-1alpha (MIP-1alpha). The longer variants of CKbeta8 are significantly less potent than CKbeta8 (25-99) and MIP-1a on CCR1 and monocytes (P < 0.05).

MeSH terms

  • Animals
  • Binding, Competitive
  • CHO Cells
  • Chemokines, CC / metabolism*
  • Cricetinae
  • Humans
  • Iodine Radioisotopes
  • Monocytes / metabolism
  • Peptides / metabolism
  • Receptors, CCR1
  • Receptors, Chemokine / metabolism*
  • Transfection


  • CCL23 protein, human
  • CCR1 protein, human
  • Chemokines, CC
  • Iodine Radioisotopes
  • Peptides
  • Receptors, CCR1
  • Receptors, Chemokine