Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1993-9-14
pubmed:abstractText
In order to establish the pathophysiological roles of IL-8, rabbit IL-8 was expressed in Escherichia coli and purified to homogeneity by sequential chromatography on heparin agarose, CM-HPLC, and RP-HPLC. The purified recombinant rabbit IL-8 was homogeneous on SDS-PAGE and the ED50 of neutrophil chemotactic activity for rabbit peritoneal neutrophils was 2 ng/ml. The binding of 125I-labeled rabbit IL-8 to rabbit neutrophils was inhibited by unlabeled human IL-8 as well as rabbit IL-8 but not by another leucocyte chemotactic cytokine (chemokine), monocyte chemotactic and activating factor. Scatchard plot analysis of the binding of 125I-labeled rabbit IL-8 to rabbit peritoneal neutrophils revealed that the rabbit neutrophils have two affinity classes of receptors for IL-8 (Kd = 2.3 nM, 4.1 x 10(4) sites/cell; Kd = 18.0 nM, 11.4 x 10(4) sites/cell). It was found that a previously generated mouse anti-human IL-8 mAb, WS-4, inhibited the binding of 125I-labeled rabbit IL-8 to rabbit neutrophils, and blocked neutrophil chemotaxis in vitro in a specific and dose-dependent manner. An ELISA system for rabbit IL-8 was established using this mAb and guinea pig polyclonal antibodies to recombinant rabbit IL-8 to measure the levels of IL-8 in rabbit plasma. Intravenous administration of lipopolysaccharide (LPS) (100 micrograms) in rabbits caused the highest level of IL-8 in blood at around 2 h. Intravenous administration of WS-4 (10 mg) inhibited neutrophil infiltration at the site of LPS injection into the rabbit skin, suggesting that IL-8 is essential in the recruitment of neutrophils at sites of acute inflammation in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0953-8178
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:geneSymbol
IL-8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
681-90
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed-meshheading:8347559-Amino Acid Sequence, pubmed-meshheading:8347559-Animals, pubmed-meshheading:8347559-Antibodies, Monoclonal, pubmed-meshheading:8347559-Base Sequence, pubmed-meshheading:8347559-Chemotaxis, Leukocyte, pubmed-meshheading:8347559-Cloning, Molecular, pubmed-meshheading:8347559-Cross Reactions, pubmed-meshheading:8347559-DNA, pubmed-meshheading:8347559-Dermatitis, pubmed-meshheading:8347559-Escherichia coli, pubmed-meshheading:8347559-Female, pubmed-meshheading:8347559-Gene Expression, pubmed-meshheading:8347559-Humans, pubmed-meshheading:8347559-Interleukin-8, pubmed-meshheading:8347559-Lipopolysaccharides, pubmed-meshheading:8347559-Molecular Sequence Data, pubmed-meshheading:8347559-Neutrophils, pubmed-meshheading:8347559-Rabbits, pubmed-meshheading:8347559-Recombinant Proteins
pubmed:year
1993
pubmed:articleTitle
Expression of recombinant rabbit IL-8 in Escherichia coli and establishment of the essential involvement of IL-8 in recruiting neutrophils into lipopolysaccharide-induced inflammatory site of rabbit skin.
pubmed:affiliation
Department of Hygiene, Kanazawa University, Japan.
pubmed:publicationType
Journal Article