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PMID: 8140420 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Neutrophil activation by monomeric interleukin-8.

Science (New York, N.Y.) ·Vol. 264 ·No. 5155 ·1994-04-01 ·Pages 90-2

Rajarathnam K, Sykes BD, Kay CM, Dewald B, Geiser T, Baggiolini M, Clark-Lewis I

Abstract

Interleukin-8 (IL-8), a pro-inflammatory protein, has been shown by nuclear magnetic resonance (NMR) and x-ray techniques to exist as a homodimer. An IL-8 analog was chemically synthesized, with the amide nitrogen of leucine-25 methylated to selectivity block formation of hydrogen bonds between monomers and thereby prevent dimerization. This analog was shown to be a monomer, as assessed by analytical ultracentrifugation and NMR. Nevertheless, it was equivalent to IL-8 in assays of neutrophil activation, which indicates that the monomer is a functional form of IL-8.

MeSH Terms
Calcium/metabolism Chemotaxis, Leukocyte Humans Hydrogen Bonding Interleukin-8/analogs & derivatives,chemistry,metabolism,pharmacology Leukocyte Elastase Models, Chemical Neutrophils/drug effects,physiology Pancreatic Elastase/metabolism Protein Conformation Protein Structure, Secondary Receptors, Interleukin/chemistry,metabolism Receptors, Interleukin-8A
Chemicals
Interleukin-8 Receptors, Interleukin Receptors, Interleukin-8A Pancreatic Elastase Leukocyte Elastase Calcium
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Rajarathnam K
Protein Engineering Network of Centres of Excellence (PENCE), University of Alberta, Edmonton, Canada.
Sykes B D
Kay C M
Dewald B
Geiser T
Baggiolini M
Clark-Lewis I
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1994-04-01
Pages
90-2
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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