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Blood, Vol. 93 No. 2 (January 15), 1999:
pp. 632-642
Detection of Normal and Chimeric Nucleophosmin in Human Cells
Jacqueline L. Cordell,
Karen A.F. Pulford,
Barbara Bigerna,
Giovanna Roncador,
Alison Banham,
Emanuela Colombo,
Pier-Giuseppe Pelicci,
David Y. Mason, and
Brunangelo Falini
From the Leukaemia Research Fund Immunodiagnostics Unit, Nuffield
Department of Clinical Biochemistry and Cellular Science, John
Radcliffe Hospital, Oxford, UK; and the Institute of Hematology,
Policlinico Monteluce, Perugia, Italy.
In anaplastic large-cell lymphoma (ALCL), the (2;5) chromosomal
translocation creates a fusion gene encoding the 80-kD NPM-ALK hybrid
protein. This report describes three new monoclonal antibodies, two of
which recognize, by Western blotting, the N-terminal portion of NPM
present in the NPM-ALK fusion protein and also in two other NPM fusion
proteins (NPM-RAR and NPM-MLF1). The third antibody recognizes the
C-terminal portion (deleted in NPM-ALK) and reacts only with wild-type
NPM. The three antibodies immunostain wild-type NPM (in
paraffin-embedded normal tissue samples) in cell nuclei and in the
cytoplasm of mitotic cells. Cerebral neurones, exceptionally, show
diffuse cytoplasmic labeling. In contrast to normal tissues, the two
antibodies against the N-terminal portion of NPM labeled the cytoplasm
of neoplastic cells, in four ALK-positive ALCL, reflecting their
reactivity with NPM-ALK fusion protein, whereas the antibody to the
C-terminal NPM epitope labeled only cell nuclei. Immunocytochemical
labeling with these antibodies can therefore confirm that an
ALK-positive lymphoma expresses NPM-ALK (rather than a variant
ALK-fusion protein) and may also provide evidence for chromosomal
anomalies involving the NPM gene other than the classical (2;5)
translocation.
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