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Immunophenotyping and functional analysis of purified human uterine mast
cells
CB Guo, A Kagey-Sobotka, LM Lichtenstein and BS Bochner
Johns Hopkins Asthma and Allergy Center, Baltimore, MD 21224.
Human mast cells have been purified from uterine tissues, and their surface
marker profile and function have been evaluated as part of ongoing studies
of mast cell heterogeneity. Using a panel of antibodies, purified uterine
mast cells (UMC; 81% +/- 7% purity, n = 10) were analyzed by
immunofluorescence and flow cytometry for surface expression of various
antigens. Consistent with previous analyses of mast cells from other
tissues, UMC expressed HLA class I, IgE, c-kit receptor, CD9, CD33, CD43,
CD45, and CD54, while CD11a, CD11b, CD14, CD16, CD23, and CD64 were not
detected. Unlike other mast cells, UMC expressed CD11c/CD18 (p150,95) and
CD32 (Fc gamma RII). Additional antigens not previously studied on mast
cells included the selectin LECAM-1 (Leu-8) and several beta 1 and beta 3
integrins; expression of very late activation antigen-4 (VLA-4)
(CD49d/CD29), VLA-5 (CD49e/CD29), and the vitronectin receptor (CD51/CD61)
was seen. Functional studies showed that treatment of human umbilical vein
endothelial cells with interleukin-1 (5 ng/mL for 4 hours) resulted in a
twofold to threefold increase in adhesiveness for UMC. Purification
procedures did not alter histamine release responses to anti-IgE or the
calcium ionophore A23187, and treatment of UMC with an anti-CD32 monoclonal
antibody (IV.3) did not induce histamine release or alter anti-IgE-induced
release. These data suggest that UMC may possess unique phenotypic
characteristics, and support the concept of mast cell heterogeneity.
Volume 79,
Issue 3,
pp. 708-712,
02/01/1992
Copyright © 1992 by The American Society of Hematology
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