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Dimeric S100A8 in human neutrophils is diminished after phagocytosis
Author(s) -
Kumar Rakesh K.,
Yang Zheng,
Bilson Susan,
Thliveris Soula,
Cooke Bridget E.,
Geczy Carolyn L.
Publication year - 2001
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.70.1.59
Subject(s) - phagocytosis , s100a8 , zymosan , biology , s100a9 , in vitro , immunostaining , opsonin , in vivo , macrophage , phagocyte , antibody , microbiology and biotechnology , inflammation , immunology , biochemistry , immunohistochemistry
S100A8 is a major cytoplasmic protein of neutrophils andmonocytes/macrophages and has been associated with myeloid celldifferentiation and activation. Little is known about its functions ormechanisms of release from neutrophils. We have developed a monoclonalantibody to murine S100A8, which cross‐reacts with human S100A8. Thisantibody, which recognizes the homodimeric form of the protein, detectsits expression specifically in human neutrophils and is reactive informalin‐fixed, paraffin‐embedded tissues. Using this antibody as wellas a commercially available antibody to human S100A8, we show thatphagocytic activation of neutrophils, in vivo in acuteappendicitis and in vitro following phagocytosis ofopsonized zymosan, is characterized by loss of cytoplasmicimmunoreactivity for S100A8. In vitro , phagocytosis isassociated with rapid diminution of immunostaining without loss ofviability. Loss of immunoreactivity for S100A8 may serve as a marker oflocalized neutrophil activation in tissues.