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Blood, Vol. 95 No. 3 (February 1), 2000:
pp. 973-978
Adenosine triphosphate-induced oxygen radical production and
CD11b up-regulation: Ca++ mobilization and actin
reorganization in human eosinophils
Stefan Dichmann,
Marco Idzko,
Ulrich Zimpfer,
Clemens Hofmann,
Davide Ferrari,
Werner Luttmann,
Christian Virchow Jr,
Francesco Di
Virgilio, and
Johannes Norgauer
From the Departments of Dermatology and Pneumology, University of
Freiburg, Germany, and the Institute of General Pathology, University
of Ferrara, Italy.
Eosinophils are major effector cells in cellular inflammatory
conditions such as parasitic infections, atopic diseases, bullous dermatoses, and vasculitis. Biological activities of adenosine triphosphate (ATP) were characterized in human eosinophils and compared
with those of other eosinophil activators such as complement fragment
product C5a, platelet-activating factor (PAF), and
eotaxin. ATP initiated production of reactive oxygen
metabolites, as demonstrated by lucigenin-dependent chemiluminescence.
Furthermore, ATP caused up-regulation of the integrin CD11b. In
addition, fluorescence microscope measurements labeled with
fura-2
(1-[2-(5-carboxy-oxazol-2-yl)-6-aminobenzofuran-5-oxy]-2-(2'-amino-5'-methyl-phenoxy)-ethane-N, N, N, N'-tetraacetic acid, pentaacetoxymethyl ester)
eosinophils in the presence or absence of ethyleneglycotetraacetic acid
(EGTA) indicated that there was Ca++ mobilization from
intracellular stores by ATP. Flow cytometric studies showed transient
actin polymerization upon stimulation with ATP and its stable analogues
adenosine 5'-0-(3-thiotriphosphate) and 2-methylthioadenosine
triphosphate tetrasodium (met-ATP). The reactions induced by ATP were
comparable to those obtained by C5a, PAF, and eotaxin. Production of
reactive oxygen metabolites and actin polymerization after stimulation
with ATP was inhibited by pertussis toxin, which indicated involvement
of receptor-coupled guanine nucleotide-binding proteins
(Gi proteins). In addition, experiments with oxidized ATP
also suggest involvement of P2X receptors in this activation process.
The results show that ATP is a strong activator of eosinophils and has
biological activity comparable to those of the eosinophil chemotaxins
C5a, PAF, and eotaxin. The findings strongly suggest a role of ATP in
the pathogenesis of eosinophilic inflammation as an activator of
proinflammatory effector functions.
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