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The Journal of Immunology, 1999, 162: 4938-4942.
Copyright © 1999 by The American Association of Immunologists

Differential Effects of Leukotactin-1 and Macrophage Inflammatory Protein-1{alpha} on Neutrophils Mediated by CCR11

Shangming Zhang2,*, Byung-S. Youn2,*, Ji-Liang Gao{dagger}, Philip M. Murphy{dagger} and Byoung S. Kwon3,*,{ddagger}

* Department of Microbiology and Immunology and Walther Oncology Center, Indiana University School of Medicine, and the Walther Cancer Institute, Indianapolis, IN 46202, {dagger} Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892; and {ddagger} Department of Biological Sciences and the Immunomodulation Research Center, University of Ulsan, Ulsan, Korea

The human CC chemokine leukotactin-1 (Lkn-1) is both a strong chemoattractant for neutrophils, monocytes, and lymphocytes and a potent agonist for CCR1 and CCR3. However, human neutrophils do not migrate when the cells are stimulated with other human CC chemokines, such as human macrophage inflammatory protein-1{alpha} (hMIP-1{alpha}) and eotaxin, which also use the CCR1 and CCR3 as their receptors. In this report, we demonstrate that while hMIP-1{alpha} induced a negligible level of calcium flux and chemotaxis, Lkn-1 produced a high level of calcium flux and chemotaxis in human neutrophils. Lkn-1 cross-desensitized hMIP-1{alpha}-induced calcium flux, but hMIP-1{alpha} had little effect on the Lkn-1-induced response in human neutrophils. The same pattern was observed in peritoneal neutrophils from wild-type mice, whereas neutrophils from CCR1-/- mice failed to respond to either MIP-1{alpha} or Lkn-1. Scatchard analysis revealed a single class of receptor for both hMIP-1{alpha} and Lkn-1 on human neutrophils with dissociation constants (Kd) of 3.2 nM and 1.1 nM, respectively. We conclude that CCR1 is a receptor mediating responses to both MIP-1{alpha} and Lkn-1 on neutrophils and produces different biological responses depending on the ligand bound.




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