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(Journal of Leukocyte Biology. 2000;68:243-250.)
© 2000 by Society for Leukocyte Biology

Expression of ₄-integrins on human neutrophils

Juha Kirveskari^*, Petri Bono^*,, Kaisa Granfors^*, Marjatta Leirisalo-Repo, Sirpa Jalkanen^*, and Marko Salmi^*,

^* National Public Health Institute, Department in Turku;
MediCity Research Laboratory, University of Turku; and
Helsinki University Central Hospital, Department of Internal Medicine, Helsinki, Finland

Correspondence: Dr. Marko Salmi, MediCity Research Laboratory, University of Turku, Tykistökatu 6A, FIN-20520 Turku, Finland. E-mail: marko.salmi{at}utu.fi

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 ₄-integrins as well. We studied whether human neutrophils can synthesize ₄-integrins upon activation in vitro or in vivo. Two anti-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-₄ mAbs contain two distinct Igs, the 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, ₄ mRNA was not detectable in purified neutrophils. Our results show that ₄ integrin protein and mRNA are absent from normal and stimulated human neutrophils.

Key Words: adhesion molecules • cell trafficking • antibody • FACS

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