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Cited by 871

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Cloning of Complementary DNA Encoding a Functional Human Interleukin-8 Receptor

Open access
Murphy, Philip M., Tiffany, H. Lee·1991·Science

Abstract

Interleukin-8 (IL-8) is an inflammatory cytokine that activates neutrophil chemotaxis, degranulation, and the respiratory burst. Neutrophils express receptors for IL-8 that are coupled to guanine nucleotide-binding proteins (G proteins); binding of IL-8 to its receptor induces the mobilization of intracellular calcium stores. A cDNA clone from HL-60 neutrophils, designated p2, has now been isolated that encodes a human IL-8 receptor. When p2 is expressed in oocytes from Xenopus laevis , the oocytes bind 125 I-labeled IL-8 specifically and respond to IL-8 by mobilizing calcium stores with an EC 50 of 20 nM. This IL-8 receptor has 77% amino acid identity with a second human neutrophil receptor isotype that binds IL-8 with higher affinity. It also exhibits 69% amino acid identity with a protein reported to be an N-formyl peptide receptor from rabbit neutrophils, but less than 30% identity with all other known G protein-coupled receptors, including the human N-formyl peptide receptor.

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Crossref · 10.1126/science.1891716

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Metadata

Authors
Murphy, P. M., & Tiffany, H. L.
Venue
Science
Published
1991-09-13
Volume
253
Issue
5025
Pages
1280-1283
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2058902088
Cited by
871
References
0
FWCI
22.90
Type
journal article
Language
en
Open access
green

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