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Genomic structure, chromosomal localization, and conserved alternative
splice forms of thrombopoietin
AL Gurney, WJ Kuang, MH Xie, BE Malloy, DL Eaton and FJ de Sauvage
Department of Molecular Biology, Genentech, Inc, San Francisco, CA 94080.
Thrombopoietin (TPO), the ligand for c-mpl, is a novel cytokine comprising
an amino terminal domain with homology to erythropoietin and a glycosylated
carboxyl terminal domain that does not bear overall homology to other known
proteins. We report the cloning of cDNAs encoding the porcine and murine
TPO and the characterization of the human TPO gene. The cDNA for an
additional splice form (TPO-2) with a four-amino-acid deletion within the
erythropoietin-like domain has been isolated and is conserved between
humans, pigs, and mice. Species comparison of TPO shows that the amino
terminal erythropoietin-like domain is highly conserved, while the carboxyl
terminal domain is less conserved. Recombinant murine TPO and human TPO are
each able to activate both the murine and human c-mpl receptors, indicating
an absence of strict species specificity. Human TPO is encoded by a single
gene consisting of six exons and located on chromosome 3q27-28.
Volume 85,
Issue 4,
pp. 981-988,
02/15/1995
Copyright © 1995 by The American Society of Hematology
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