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GABP cooperates with c-Myb and C/EBP to activate the neutrophil elastase
promoter
I Nuchprayoon, CP Simkevich, M Luo, AD Friedman and AG Rosmarin
Division of Pediatric Oncology, The Johns Hopkins Oncology Center, Johns
Hopkins University, Baltimore, MD, USA.
Neutrophil elastase (NE) is a serine protease that is transcriptionally
regulated during early myeloid differentiation. The murine NE (mNE)
promoter contains functionally important c-Myb, C/EBP, and ets binding
sites. Deletion of the ets site reduced promoter activity by 90%. Although
the ets transcription factor, PU.1, bound to this ets site, it only
modestly activated the mNE promoter. Here, we show that a second
transcription factor from myeloid cells-GABP-binds to the mNE ets site but
strongly activates the mNE promoter. GABP is a heteromeric transcription
factor complex that consists of GABP alpha, an ets factor, and GABP beta, a
Notch-related protein. GABP alpha bound to the mNE ets site and, in turn,
recruited GABP beta to form a transcriptionally active complex. GABP alpha
and PU.1 competed with each other for binding to the mNE ets site. GABP
increased the activity of the mNE promoter sevenfold in U937 myeloid cells.
GABP cooperated with c-Myb and C/EBP alpha to activate the mNE promoter
more than 85- fold in otherwise nonpermissive, nonhematopoietic NIH 3T3
cells. Thus, GABP binds to the crucial mNE promoter ets site and powerfully
activates its expression alone and in cooperation with the transcription
factors c-Myb and C/EBP.
Volume 89,
Issue 12,
pp. 4546-4554,
06/15/1997
Copyright © 1997 by The American Society of Hematology
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