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Blood, Vol. 95 No. 10 (May 15), 2000:
pp. 3204-3207
Further demonstration of the diversity of chromosomal changes
involving 2p23 in ALK-positive lymphoma: 2 cases expressing ALK
kinase fused to CLTCL (clathrin chain polypeptide-like)
Christian Touriol,
Catherine Greenland,
Laurence Lamant,
Karen Pulford,
Frédéric Bernard,
Thérèse Rousset,
David Y. Mason, and
Georges Delsol
UPCM-ERS 1590 CNRS, CHU Purpan, Toulouse, France; Department of
Pathology, CHU Purpan, Toulouse, France; LRF Immunodiagnostics Unit,
Department of Clinical Biochemistry and Cellular Science, John
Radcliffe Hospital, Oxford, UK; Hôpital Arnaud de Villeneuve, CHU
de Montpellier, France; Laboratoire d'Anatomie Pathologique-Gui de
Chauliac, Montpellier, France.
Anaplastic lymphoma kinase (ALK)-positive lymphomas are
characterized by expression of a hybrid protein, comprising the
cytoplasmic portion of the ALK tyrosine kinase fused to a partner
protein. This hybrid kinase is often encoded by the nucleophosmin (NPM) NPM-ALK fusion gene resulting from the (2;5)(p23;q35)
chromosomal translocation. However, the ALK gene at 2p23 may
also be involved in 2 variant translocations, namely t(1;2)(q25;p23)
and t(2;3)(p23;q21), which create the TPM3-ALK and
TFG-ALK fusion genes, respectively. We report here 2 lymphomas
with an unusual finely granular cytoplasmic ALK staining pattern,
clearly different from the pattern observed in ALK-positive lymphomas
carrying NPM-ALK or its variants. A cloned complementary DNA
sequence from 1 of these 2 lymphomas contained the ALK gene
fused to the second clathrin heavy chain gene (also referred to as
clathrin heavy polypeptide-like gene) (CLTCL). The distinctive
granular cytoplasmic staining pattern for ALK was likely to be due to
binding of the fusion protein to clathrin-coated vesicles. The
CLTCL gene is constitutively expressed in lymphoid cells and
therefore presumably contributes an active promoter for the
CLTCL-ALK gene. The fusion protein had a molecular weight (250 kd) that differs from all known ALK products, and it was
autophosphorylated in an in vitro kinase assay, confirming that it is
constitutively active and hence capable of contributing to malignant
transformation. These 2 cases, therefore, represent a hitherto
undescribed mechanism of ALK activation in lymphoma and further
illustrate the diversity of fusion partners for the ALK gene.
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