Journal of Leukocyte Biology
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A more recent version of this article appeared on March 1, 2005

Published online before print December 2, 2004
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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.0704398

Received for publication July 14, 2004.
Revised October 5, 2004.
Accepted for publication October 25, 2004.

Article

cCXCR1 is a receptor for cIL8 (9E3/cCAF) and its N- and C-terminal peptides and is also activated by hIL8 (CXCL8)

Qi-Jing Li , Min Yao , Melissa Dueck , Vladimir Parpura , and Manuela Martins-Green @

Department of Cell Biology and Neuroscience, University of California, Riverside

@ To whom correspondence should be addressed. E-mail: mmgreen{at}ucrac1.ucr.edu.


  Abstract

Chemokines are chemotactic cytokines that play important roles in immune responses and wound healing, as well as in pathological conditions such as chronic inflammation and tumorigenesis. The chemokines and their receptors are highly conserved and maintain similar functions in different species. One noteworthy exception is the chemokine interleukin (IL)8/CXC ligand 8 and its specific receptor CXCR1, which are found in humans but are not found in the traditional model organisms, mice and rats. As a consequence, we are using model organisms other than mice to study the functions of IL-8 and CXCR1, as well as the mechanisms involved in receptor activation by IL8. Toward this goal, we have isolated and characterized a new receptor that is highly homologous to human (h)CXCR1, which we named chicken (c)CXCR1. To determine whether this receptor is activated by cIL-8 and its N- and C-terminal peptides and whether it responds to hIL-8, we expressed cCXCR1 in NIH3T3 cells, which naturally lack this receptor, and used single-cell Ca2+ imaging to detect increases in intracellular Ca2+ and immunoblot analysis to detect extracellular signal-regulated kinase 1/2 phosphorylation. We show that cIL-8, its N and C peptides, and hIL-8 activate cCXCR1. We further show that cIL-8 and hIL-8 stimulate chemotaxis of chicken embryonic fibroblasts, cells that express cCXCR1, and that this effect is specific for each chemokine and this receptor. These results strongly suggest that cCXCR1 is the ortholog for hCXCR1 and that chickens can be used as an effective model system to study the functions of IL-8, its terminal peptides, and its specific receptor CXCR1.

Key Words: chemokine signaling • signal transduction • Ca2+ release • MAPK • stress response




This article has been cited by other articles:


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T. Y. Poh, J. Pease, J. R. Young, N. Bumstead, and P. Kaiser
Re-evaluation of Chicken CXCR1 Determines the True Gene Structure: CXCLi1 (K60) AND CXCLi2 (CAF/INTERLEUKIN-8) ARE LIGANDS FOR THIS RECEPTOR
J. Biol. Chem., June 13, 2008; 283(24): 16408 - 16415.
[Abstract] [Full Text] [PDF]


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