Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1984-11-21
pubmed:abstractText
Binding of the fluoresceinated chemoattractant N-formylmethionylleucylphenylalanyllysine to neutrophils was measured simultaneously with cell membrane potential by flow cytometry to determine how chemoattractant was bound by different populations of responding neutrophils. Cells exhibiting an apparent depolarization of membrane potential bound more chemoattractant than cells which did not respond or which exhibited a small hyperpolarization. Approximately 45% of the peptide bound to depolarized cells was displaced by unlabeled peptide, whereas only 3% was displaced from the nonresponding cells. By utilizing the well-known observation that extracellular fluorescein fluorescence is quenched by acid pH, it was determined that approximately one-half of the nondisplaceable peptide of both cell types was internalized, but a significant amount remained tightly bound to the extracellular membrane surface and accessible to lowering of the extracellular pH to 5.5. Treatment of cells with cytochalasin B to convert nonresponding cells to depolarizing cells also resulted in expression of displaceable binding by these cells, suggesting a close correlation between displaceable peptide binding and depolarization. Differential binding of chemoattractant among neutrophils and its modulation may account for observations of functional heterogeneity of neutrophils.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:volume
133
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2641-6
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Differential binding of chemoattractant peptide to subpopulations of human neutrophils.
pubmed:publicationType
Journal Article