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Binding of fluorescein-labeled anaphylatoxin C5a to human peripheral blood,
spleen, and bone marrow leukocytes
T Werfel, M Oppermann, M Schulze, G Krieger, M Weber and O Gotze
Department of Immunology, University of Gottingen, Germany.
The expression of C5a receptors (C5aR) on human leukocytes was evaluated by
flow cytometry using fluorescein-labeled human C5a (C5a- F). Granulocytes
and CD14+ mononuclear cells (MNL) but not CD3+, CD20+, CD16+, CD56+, or
CD11b+ lymphocytes in peripheral blood and spleen bound C5a-F. C5a-F
binding was saturable and inhibitable by anti-C5a monoclonal antibody
(MoAb) C17/5 or unlabeled C5a. During hemodialysis, which led to the
generation of C5a, only granulocytes and monocytes increased their
expression of the adhesion molecule CD11b (CR3). In vitro, C5a induced an
increase of CR3 and p 150/95 (CD11c/CR4) only on myeloid cells. However,
treatment of leukocytes with phorbol 12- myristate 13 acetate increased CR3
and CR4 expression on both myeloid cells and a lymphocyte subpopulation.
Stimulation of MNL in mixed lymphocyte cultures or by treatment with
conditioned medium or with IFN- gamma did not induce binding sites for C5aR
on lymphocytes and reduced the binding of C5a-F to monocytes. The
expression of C5aR on low- density bone marrow cells was analyzed by
setting appropriate gates during flow cytometry. Cells that bound C5a-F
were found in all populations that contained granulocyte and monocyte
precursors, but not in lymphocyte precursor populations. All C5aR+ bone
marrow cells were CD34 and expressed high levels of CR3, which suggests a
late appearance of C5aR during myeloid cell maturation. Our results
indicate that C5aR is exclusively expressed on myeloid cells within the
hematopoetic cell population.
Volume 79,
Issue 1,
pp. 152-160,
01/01/1992
Copyright © 1992 by The American Society of Hematology
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