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Cited by 1,090

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Structure and Functional Expression of a Human Interleukin-8 Receptor

Holmes, William E., Lee, James, Kuang, Wun-Jing, Rice, Glenn C., Wood, William I.·1991·Science

Abstract

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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Metadata

Authors
Holmes, W. E., Lee, J., Kuang, W.-J., Rice, G. C., & Wood, W. I.
Venue
Science
Published
1991-09-13
Volume
253
Issue
5025
Pages
1278-1280
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2039137468
Cited by
1,090
References
1
FWCI
25.48
Type
journal article
Language
en
Open access
closed

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