Premium
Expression of α 4 ‐integrins on human neutrophils
Author(s) -
Kirveskari Juha,
Bono Petri,
Granfors Kaisa,
LeirisaloRepo Marjatta,
Jalkanen Sirpa,
Salmi Marko
Publication year - 2000
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.68.2.243
Subject(s) - integrin , biology , in vitro , subclass , microbiology and biotechnology , in vivo , neutrophil extracellular traps , messenger rna , extracellular , cell adhesion molecule , immunology , antibody , receptor , biochemistry , gene , inflammation
α 4 Integrins are important adhesion molecules mediating binding of lymphocytes, monocytes, and eosinophils to multiple cellular and extracellular ligands. Mature neutrophils have been recently suggested to express α 4 ‐integrins as well. We studied whether human neutrophils can synthesize α 4 ‐integrins upon activation in vitro or in vivo . Two anti‐α 4 mAbs, but not multiple subclass‐matched non‐binding controls, reacted with granulocytes in an inducer and time‐dependent manner. Nevertheless, staining with Ig subclass‐specific second‐stage reagents surprisingly revealed that commercial anti‐α 4 mAbs contain two distinct Igs, the α 4 ‐specific IgG1 and an IgG2a of an unknown specificity. We showed that in vitro inductions used by us and others only induce the binding of nonspecific IgG2a from the commercial HP2/1 to activated neutrophils. By reverse‐transcriptase polymerase chain reaction, α 4 mRNA was not detectable in purified neutrophils. Our results show that α 4 integrin protein and mRNA are absent from normal and stimulated human neutrophils.