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Science 13 September 1991:
Vol. 253. no. 5025, pp. 1278 - 1280
DOI: 10.1126/science.1840701
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Articles

Science, Vol 253, Issue 5025, 1278-1280
Copyright © 1991 by American Association for the Advancement of Science

articles

Structure and functional expression of a human interleukin-8 receptor

WE Holmes, J Lee, WJ Kuang, GC Rice, and WI Wood

Department of Molecular Biology, Genentech, Inc., South San Francisco, CA 94080.

Interleukin-8 (IL-8) is a member of a family of pro-inflammatory cytokines. Although the best characterized activities of IL-8 include the chemoattraction and activation of neutrophils, other members of this family have a wide range of specific actions including the chemotaxis and activation of monocytes, the selective chemotaxis of memory T cells, the inhibition of hematopoietic stem cell proliferation, and the induction of neutrophil infiltration in vivo. A complementary DNA encoding the IL-8 receptor from human neutrophils has now been isolated. The amino acid sequence shows that the receptor is a member of the superfamily of receptors that couple to guanine nucleotide binding proteins (G proteins). The sequence is 29% identical to that of receptors for the other neutrophil chemoattractants, fMet-Leu-Phe and C5a. Mammalian cells transfected with the IL-8 receptor cDNA clone bind IL-8 with high affinity and respond specifically to IL-8 by transiently mobilizing calcium. The IL-8 receptor may be part of a subfamily of related G protein-coupled receptors that transduce signals for the IL-8 family of pro-inflammatory cytokines.


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   Abstract »    Full Text »    PDF »
CXCR1 and CXCR2 Are Rapidly Down-Modulated by Bacterial Endotoxin Through a Unique Agonist-Independent, Tyrosine Kinase-Dependent Mechanism.
M. H. Khandaker, L. Xu, R. Rahimpour, G. Mitchell, M. E. DeVries, J. G. Pickering, S. K. Singhal, R. D. Feldman, and D. J. Kelvin (1998)
J. Immunol. 161, 1930-1938
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Binding and Functional Properties of Recombinant and Endogenous CXCR3 Chemokine Receptors.
Y. Weng, S. J. Siciliano, K. E. Waldburger, A. Sirotina-Meisher, M. J. Staruch, B. L. Daugherty, S. L. Gould, M. S. Springer, and J. A. DeMartino (1998)
J. Biol. Chem. 273, 18288-18291
   Abstract »    Full Text »    PDF »
The CC chemokine 6Ckine binds the CXC chemokine receptor CXCR3.
H. Soto, W. Wang, R. M. Strieter, N. G. Copeland, D. J. Gilbert, N. A. Jenkins, J. Hedrick, and A. Zlotnik (1998)
PNAS 95, 8205-8210
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Quantitative comparison of C-X-C chemokines produced by endotoxin-stimulated human alveolar macrophages.
R. B. Goodman, R. M. Strieter, C. W. Frevert, C. J. Cummings, P. Tekamp-Olson, S. L. Kunkel, A. Walz, and T. R. Martin (1998)
Am J Physiol Lung Cell Mol Physiol 275, L87-L95
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Differential Regulation of Chemoattractant-Stimulated {beta}2, {beta}3, and {beta}7 Integrin Activity.
C. Sadhu, B. Masinovsky, and D. E. Staunton (1998)
J. Immunol. 160, 5622-5628
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Down-Regulation of CXCR2 Expression on Human Polymorphonuclear Leukocytes by TNF-{alpha}.
K. Asagoe, K. Yamamoto, A. Takahashi, K. Suzuki, A. Maeda, M. Nohgawa, N. Harakawa, K. Takano, N. Mukaida, K. Matsushima, et al. (1998)
J. Immunol. 160, 4518-4525
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Identification of a Potent, Selective Non-peptide CXCR2 Antagonist That Inhibits Interleukin-8-induced Neutrophil Migration.
J. R. White, J. M. Lee, P. R. Young, R. P. Hertzberg, A. J. Jurewicz, M. A. Chaikin, K. Widdowson, J. J. Foley, L. D. Martin, D. E. Griswold, et al. (1998)
J. Biol. Chem. 273, 10095-10098
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Multiple Signaling Pathways of Human Interleukin-8 Receptor A. INDEPENDENT REGULATION BY PHOSPHORYLATION.
R. M. Richardson, H. Ali, B. C. Pridgen, B. Haribabu, and R. Snyderman (1998)
J. Biol. Chem. 273, 10690-10695
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Secondary Lymphoid-tissue Chemokine Is a Functional Ligand for the CC Chemokine Receptor CCR7.
R. Yoshida, M. Nagira, M. Kitaura, N. Imagawa, T. Imai, an