Journal of Leukocyte Biology
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(Journal of Leukocyte Biology. 2001;70:59-64.)
© 2001 by Society for Leukocyte Biology

Dimeric S100A8 in human neutrophils is diminished after phagocytosis

Rakesh K. Kumar*, Zheng Yang*, Susan Bilson*, Soula Thliveris*, Bridget E. Cooke{dagger} and Carolyn L. Geczy*

* School of Pathology, University of New South Wales, Sydney, Australia; and
{dagger} Department of Anatomical Pathology, Prince of Wales Hospital, Randwick, Australia

Correspondence: R. K. Kumar, School of Pathology, University of New South Wales, Sydney, Australia 2052. E-mail: R.Kumar{at}unsw.edu.au

S100A8 is a major cytoplasmic protein of neutrophils and monocytes/macrophages and has been associated with myeloid cell differentiation and activation. Little is known about its functions or mechanisms of release from neutrophils. We have developed a monoclonal antibody to murine S100A8, which cross-reacts with human S100A8. This antibody, which recognizes the homodimeric form of the protein, detects its expression specifically in human neutrophils and is reactive in formalin-fixed, paraffin-embedded tissues. Using this antibody as well as a commercially available antibody to human S100A8, we show that phagocytic activation of neutrophils, in vivo in acute appendicitis and in vitro following phagocytosis of opsonized zymosan, is characterized by loss of cytoplasmic immunoreactivity for S100A8. In vitro, phagocytosis is associated with rapid diminution of immunostaining without loss of viability. Loss of immunoreactivity for S100A8 may serve as a marker of localized neutrophil activation in tissues.

Key Words: acute inflammation • neutrophil activation • immuno-histochemistry • S100 proteins




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