Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1992-11-13
pubmed:abstractText
IL-8 and its structural analogs derived from blood platelets have been proposed as stimuli of IgE-independent basophil activation. In order to clarify the mechanism of action of these peptides, we examined the effects of pure IL-8, connective tissue-activating peptide III (CTAP-III), neutrophil-activating peptide 2 (NAP-2), and platelet factor 4 (PF-4) on blood basophils with and without pretreatment by IL-3, which modulates mediator release. After pretreatment with IL-3, significant histamine release was observed with 10(-8) M and 10(-7) M IL-8 and 10(-7) M NAP-2, but not with the other peptides. At higher concentrations (10(-6) M), however, all IL-8 analogs, as well as the unrelated cationic peptides poly-D-lysine, histone VS, and lysozyme, induced histamine release to variable degrees. Binding and competition studies with [125I]IL-8 revealed specific IL-8R on basophils from a patient with chronic myelogenous leukemia and normal individuals. From 3500 to 9600 receptors with a mean Kd value of 0.15 nM were found on average per chronic myelogenous leukemia and normal basophil, respectively. NAP-2 weakly competed for IL-8 binding. IL-8 and, to a lesser extent, NAP-2 led to a transient rise of cytosolic free calcium concentration ([Ca2+]i), which was independent of a preexposure to IL-3. IL-8 prevented the [Ca2+]i rise induced by NAP-2, but did not influence [Ca2+]i responses to other agonists, e.g. C5a, C3a, or platelet-activating factor. IL-8 induced [Ca2+]i changes and histamine release in IL-3-primed basophils were pertussis toxin sensitive. CTAP-III or PF-4 did not compete for IL-8 binding, did not induce [Ca2+]i changes, and did not influence the [Ca2+]i response to IL-8 and NAP-2. This study shows that IL-8 and NAP-2 activate human basophils by a receptor-mediated mechanism similar to that operating in neutrophils. At high concentrations histamine release can also be induced by cationic peptides by a mechanism that does not involve the IL-8R, and probably depends on cationic interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Blood Coagulation Factors, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-3, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-8, http://linkedlifedata.com/resource/pubmed/chemical/PPBP protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Platelet Factor 4, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-8A, http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella, http://linkedlifedata.com/resource/pubmed/chemical/beta-Thromboglobulin, http://linkedlifedata.com/resource/pubmed/chemical/connective tissue-activating peptide, http://linkedlifedata.com/resource/pubmed/chemical/low affinity platelet factor 4
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
149
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2662-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1383321-Amino Acid Sequence, pubmed-meshheading:1383321-Basophils, pubmed-meshheading:1383321-Binding, Competitive, pubmed-meshheading:1383321-Blood Coagulation Factors, pubmed-meshheading:1383321-Calcium, pubmed-meshheading:1383321-Cells, Cultured, pubmed-meshheading:1383321-Histamine Release, pubmed-meshheading:1383321-Humans, pubmed-meshheading:1383321-Interleukin-3, pubmed-meshheading:1383321-Interleukin-8, pubmed-meshheading:1383321-Molecular Sequence Data, pubmed-meshheading:1383321-Peptides, pubmed-meshheading:1383321-Pertussis Toxin, pubmed-meshheading:1383321-Platelet Factor 4, pubmed-meshheading:1383321-Receptors, Immunologic, pubmed-meshheading:1383321-Receptors, Interleukin-8A, pubmed-meshheading:1383321-Virulence Factors, Bordetella, pubmed-meshheading:1383321-beta-Thromboglobulin
pubmed:year
1992
pubmed:articleTitle
Activation of human basophils through the IL-8 receptor.
pubmed:affiliation
Institute of Clinical Immunology, University of Bern, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't