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Expression of isoforms of the human receptor tyrosine kinase c-kit in
leukemic cell lines and acute myeloid leukemia
PS Crosier, ST Ricciardi, LR Hall, MR Vitas, SC Clark and KE Crosier
Department of Molecular Medicine, School of Medicine, University of
Auckland, New Zealand.
Because mutations in receptor tyrosine kinases may contribute to cellular
transformation, studies were undertaken to examine c-kit in human leukemia.
Isoforms of c-kit have been characterized in the human megakaryoblastic
leukemia cell line M-07. Deletion of the four amino acids Gly-Asn-Asn-Lys
in the extracellular domain represents an alternatively spliced isoform
that has been shown by others, in mice, to be associated with constitutive
receptor autophosphorylation (Reith et al, EMBO J 10:2451, 1991).
Additional isoforms differ in the inclusion or exclusion of a serine
residue in the interkinase domain, a region that contains the binding site
for phosphatidylinositol 3- kinase. By RNase protection analysis, we have
shown coexpression of the Gly-Asn-Asn-Lys+ and Gly-Asn-Asn-Lys- isoforms,
with dominance of the Gly-Asn-Asn-Lys- transcript, in normal human bone
marrow, normal melanocytes, a range of tumor cell lines, and the blasts of
23 patients with acute myeloid leukemia. Analysis of transcripts for the
Ser+ and Ser- isoforms also showed coexpression in all normal and leukemic
cells examined. The ratios of isoform expression for both the
Gly-Asn-Asn-Lys and Ser variants were relatively constant, providing no
evidence in the tumors examined that upregulation of one isoform
contributes to the neoplastic process.
Volume 82,
Issue 4,
pp. 1151-1158,
08/15/1993
Copyright © 1993 by The American Society of Hematology
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