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Blood, 1 February 2002, Vol. 99, No. 3, pp. 966-972
IMMUNOBIOLOGY
Regulatory effects of stem cell factor and interleukin-4 on
adhesion of human mast cells to extracellular matrix proteins
Axel Lorentz,
Detlef Schuppan,
Andreas Gebert,
Michael P. Manns, and
Stephan C. Bischoff
From the Department of Internal
Medicine/Gastroenterology and the Department of Anatomy, Medical School
of Hannover, Germany; and the Department of Medicine II, University of
Erlangen, Germany.
Mast cells are inflammatory and immunoregulatory cells resident in
tissues. They develop from bone marrow-derived progenitor cells that
enter the tissue through the blood circulation. The specific
localization and migration of mast cells in tissues is dependent on
their interaction with extracellular matrix (ECM) proteins. Adhesion of
human mast cells isolated from intestinal mucosa and cultured in the
presence of stem cell factor (SCF) to ECM proteins is analyzed. It was
observed that SCF is a unique cytokine enhancing mast cell adhesion to
all tested ECM proteins (fibronectin, laminin, collagen I, III, IV, VI,
XIV) up to 5-fold, particularly to fibronectin (54% ± 12% of mast
cells) and to denatured collagens (40% ± 12% on cyanogen
bromide-cleaved peptides of collagen I). Most noteworthy, preculture of
mast cells with interleukin-4 (IL-4), in addition to SCF, reduced their
potency to adhere to ECM proteins to one third compared to mast cells
cultured with SCF alone. Mast cell adhesion was preferentially mediated
by  1 integrins, and most cells expressed the ECM-binding
integrins  21, 31, 41, 51, and V3.
SCF-induced mast cell adhesion was totally blocked by wortmannin and
apigenin, indicating an involvement of phosphatidylinositol 3-kinase
and mitogen-activated protein kinase, and it was related to an
up-regulation of the HUTS-21 1 epitope, which is associated with an
activated conformation of 1. In conclusion, these data indicate that
SCF induces the adhesion of cultured mast cells to ECM proteins,
whereas IL-4 may promote detachment from the ECM.
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