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A novel protein tyrosine phosphatase expressed in lin(lo)CD34(hi)Sca(hi)
hematopoietic progenitor cells
J Cheng, L Daimaru, C Fennie and LA Lasky
Department of Molecular Oncology, Genetech Inc, South San Francisco, CA
94080, USA.
Stem cells are capable of extensive self-renewal in the absence of
differentiation. The maintenance of this undifferentiated state occurs
despite the fact that this cell is exposed to a milieu that is rich in a
variety of growth and differentiation factors. A unifying feature of such
hematopoietic factors is that they mediate their effects through the
phosphorylation of tyrosine residues by various cellular kinases.
Therefore, one mechanism that might inhibit such differentiation signals in
the self-renewing stem cell is the dephosphorylation of tyrosine residues
by protein tyrosine phosphatases (PTPs). We have thus investigated the
types of tyrosine phosphatases expressed by murine embryonic
lin(lo)CD34hiSca(hi) hematopoietic progenitor cells by using a consensus
polymerase chain reaction (PCR) approach. Although many known tyrosine
phosphatases were detected using this method, a novel PTP related to the
previously described PTP PEST type enzymes, murine PTP PEP and murine/human
PTP PEST, was also observed. Cloning of the full-length cDNA encoding this
enzyme showed that it was indeed a novel new member of this family, with an
amino terminal tyrosine phosphatase domain followed by a region rich in
serine, threonine, and proline. The carboxy terminus of this novel PTP
contained a short sequence that was homologous to a region of the murine
PTP PEP that was involved with nuclear localization. Bacterial expression
of the phosphatase domain showed that this enzyme could efficiently
dephosphorylate tyrosines in vitro. Analysis of the expression of the novel
nuclear PTP by quantitative PCR showed that the transcript disappeared as
the lin(lo)CD34hiSca(hi) cells differentiated in the presence of
interleukin-1, interleukin-3, erythropoietin, and granulocyte- macrophage
colony-stimulating factor. In agreement with its potential role in the
hematopoietic progenitor cell, this novel PTP was expressed at a barely
detectable level in a very limited subset of adult tissues. However,
analysis of several murine hematopoietic progenitor cell lines, but not of
a differentiated T-cell line, showed a high level of expression of the
novel PTP. These data suggest that this novel phosphatase may play a
critical role in the maintenance of the undifferentiated state of the
hematopoietic stem cell.
Volume 88,
Issue 4,
pp. 1156-1167,
08/15/1996
Copyright © 1996 by The American Society of Hematology
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