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Neutrophils and monocytes express high levels of PU.1 (Spi-1) but not Spi-B
HM Chen, P Zhang, MT Voso, S Hohaus, DA Gonzalez, CK Glass, DE Zhang and DG Tenen
Department of Medicine, Beth Israel Hospital, Harvard Medical School,
Boston, MA 02215, USA.
PU.1 (the Spi-1 oncogene) and Spi-B are closely related members of the ets
transcription factor family, sharing similar DNA binding specificities
mediated by similar DNA binding domains. PU.1 and Spi-B have been
previously described as being predominantly expressed coordinately in
macrophages and B cells, but their expression in early hematopoietic stages
and during the course of myeloid differentiation to monocytes and
macrophages or to neutrophils has not been extensively investigated. Here,
we report that PU.1 mRNA is upregulated during myeloid differentiation of
human purified CD34+ cells and murine multipotential FDCP-mix A4 cells,
suggesting that PU.1 is upregulated as an early event during
differentiation of multipotential progenitor cells. PU.1 expression is
maintained at stable levels during differentiation of myeloid cell lines
U937 and HL-60 to monocytic and neutrophilic cells. PU.1 is expressed at
highest levels in mature human monocytes and human peripheral blood
neutrophils. In contrast to PU.1, significant levels of Spi-B mRNA and
protein are found only in some B- cell lines and spleen but are not found
in myeloid cell lines, neutrophils, or macrophages. In vitro translated
Spi-B protein can bind to PU.1 binding sites in myeloid promoters and
transactivate these promoters in nonmyeloid cells. Therefore, although PU.1
and Spi-B may bind to similar DNA control elements and have redundancy of
transactivation function in vitro, the lack of significant levels of Spi-B
in myeloid cells makes it unlikely that Spi-B plays a significant role in
myeloid lineage development and gene expression. In contrast, PU.1 is
expressed at high levels not only in monocytes and macrophages but also in
neutrophils, indicating that PU.1 can activate gene expression in both
major myeloid lineages.
Volume 85,
Issue 10,
pp. 2918-2928,
05/15/1995
Copyright © 1995 by The American Society of Hematology
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Human Proteinase-3 Expression Is Regulated by PU.1 in Conjunction with a Cytidine-rich Element
J. Biol. Chem.,
December 13, 1996;
271(50):
32392 - 32402.
[Abstract]
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T. Cheng, H. Shen, D. Giokas, J. Gere, D. G. Tenen, and D. T. Scadden
Temporal mapping of gene expression levels during the differentiation of individual primary hematopoietic cells
PNAS,
November 12, 1996;
93(23):
13158 - 13163.
[Abstract]
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H.-m. Chen, P. Zhang, H. S. Radomska, C. J. Hetherington, D.-E. Zhang, and D. G. Tenen
Octamer Binding Factors and Their Coactivator Can Activate the Murine PU.1 (spi-1) Promoter
J. Biol. Chem.,
June 28, 1996;
271(26):
15743 - 15752.
[Abstract]
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A. G. Rosmarin, D. G. Caprio, D. G. Kirsch, H. Handa, and C. P. Simkevich
GABP and PU.1 Compete for Binding, yet Cooperate to Increase CD18 (beta(2) Leukocyte Integrin) Transcription
J. Biol. Chem.,
October 6, 1995;
270(40):
23627 - 23633.
[Abstract]
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R. T. Lewis, A. Andreucci, and B. S. Nikolajczyk
PU.1-mediated Transcription Is Enhanced by HMG-I(Y)-dependent Structural Mechanisms
J. Biol. Chem.,
March 16, 2001;
276(12):
9550 - 9557.
[Abstract]
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K. L. Anderson, S. L. Nelson, H. B. Perkin, K. A. Smith, M. J. Klemsz, and B. E. Torbett
PU.1 Is a Lineage-specific Regulator of Tyrosine Phosphatase CD45
J. Biol. Chem.,
March 2, 2001;
276(10):
7637 - 7642.
[Abstract]
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