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The Journal of Immunology, 1999, 162: 3765-3769.
Copyright © 1999 by The American Association of Immunologists


CUTTING EDGE

Cutting Edge: Species Specificity of the CC Chemokine 6Ckine Signaling Through the CXC Chemokine Receptor CXCR3: Human 6Ckine Is Not A Ligand for the Human or Mouse CXCR3 Receptors

Chung-Her Jenh1, Mary Ann Cox, Heather Kaminski, Meng Zhang, Heather Byrnes, Jay Fine, Daniel Lundell, Chuan-Chu Chou, Satwant K. Narula and Paul J. Zavodny

Department of Immunology, Schering-Plough Research Institute, Kenilworth, NJ 07033

The CC chemokine known as 6Ckine (SLC, Exodus-2, or TCA4) has been identified as a ligand for CCR7. Mouse 6Ckine has also been shown to signal through mouse CXCR3 and share some of the activities of IFN-{gamma} inducible protein 10 and monokine induced by IFN-{gamma}. Nonetheless, human 6Ckine has not been shown to bind CXCR3 receptor or have angiostatic activity. In this study, we report that human 6Ckine does not induce a calcium flux in either human CXCR3 or mouse CXCR3 transfected cells, although it is an equally potent agonist as mouse 6Ckine and human macrophage inflammatory protein-3ß in human CCR7 transfected cells. Mouse 6Ckine (but not human 6Ckine) is capable of competing with radiolabeled IFN-{gamma} inducible protein 10 for human CXCR3. In addition, radiolabeled human 6Ckine does not bind to either human CXCR3 or mouse CXCR3. Together these data suggest that human CC chemokine 6Ckine is not a ligand for the human or mouse CXC chemokine receptor CXCR3.




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