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Blood, 15 May 2001, Vol. 97, No. 10, pp. 3303-3305
BRIEF REPORT
The basophil activation marker defined by antibody 97A6 is
identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3
Hans-Jörg Bühring,
Martina Seiffert,
Christina Giesert,
Anke Marxer,
Lothar Kanz,
Peter Valent, and
Kimihiko Sano
From the University of Tübingen, Department of
Internal Medicine II, Division of Hematology, Immunology, and
Oncology, Germany; University of Vienna, Department of Internal
Medicine I, Division of Hematology and Hemostaseology, Austria; and
Kobe University School of Medicine, Department of Pediatrics, Japan.
It has recently been shown that monoclonal antibody (MoAb) 97A6
detects a surface antigen expressed on basophils and their CD34+ precursor cells, as well as the basophil cell line
KU-812. In this report the partial amino acid sequence of affinity
chromatography- and sodium dodecyl sulfate-polyacrylamide gel
electrophoresis-separated 97A6 antigen(s) from KU-812 lysates was
determined. Sequence alignment of high-performance liquid
chromatography-selected tryptic peptides from the resulting 130- and
150-kd bands revealed a 100% identity with amino acids 393 to 405 of
ectonucleotide pyrophosphatase/phosphodiesterase-3 (E-NPP3; CD203c) but
not of the related ectoenzyme PC-1 (E-NPP1). Moreover, MoAb 97A6
selectively recognized 293 cells transfected with human E-NPP3, but did
not react with cells transfected with PC-1 or parental 293 cells. In
addition, E-NPP3 messenger RNA expression was detected in basophils but
not other peripheral blood cells. Finally, MoAb 97A6 immunoprecipitated
phosphodiesterase activity from KU-812 cells and peripheral blood
basophils, but not from other cell populations. These data demonstrate
that MoAb 97A6 recognizes the functionally active type II
transmembrane ectoenzyme E-NPP3.
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