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Prepublished online as a Blood First Edition Paper on December 19, 2002; DOI 10.1182/blood-2002-04-1039.
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Blood, 15 April 2003, Vol. 101, No. 8, pp. 3265-3273
PHAGOCYTES
Regulation of neutrophil and eosinophil secondary granule gene
expression by transcription factors C/EBP and
PU.1
Adrian F. Gombart,
Scott H. Kwok,
Karen L. Anderson,
Yuji Yamaguchi,
Bruce E. Torbett, and
H. Phillip Koeffler
From the Division of Hematology/Oncology, Cedars-Sinai
Medical Center, Los Angeles, CA; the Burns and Allen Research
Institute, University of California at Los Angeles School of Medicine;
the Departments of Molecular and Experimental Medicine and Immunology,
The Scripps Research Institute, La Jolla, CA; and the Center for Sleep
Respiratory Disorders, Fukoka, Japan.
In the bone marrow of C/EBP  / mice, expression of
neutrophil secondary and tertiary granule mRNAs is absent for
lactoferrin (LF), neutrophil gelatinase (NG), murine cathelinlike
protein (MCLP), and the cathelin B9; it is severely reduced for
neutrophil collagenase (NC) and neutrophil gelatinase-associated
lipocalin (NGAL). In addition, the expression of eosinophil granule
genes, major basic protein (MBP), and eosinophil peroxidase (EPX) is absent. These mice express C/EBP , C/EBP , and C/EBP in the bone marrow at levels similar to those of their wild-type counterparts, suggesting a lack of functional redundancy among the family in vivo.
Stable inducible expression of C/EBP and C/EBP in the murine
fibroblast cell line NIH 3T3 activated expression of mRNAs for B9,
MCLP, NC, and NGAL but not for LF. In transient transfections of
C/EBP and C/EBP, B9 was strongly induced with weaker
induction of the other genes. C/EBP and C/EBP proteins weakly
induced B9 expression, but C/EBP induced NC expression more
efficiently than the other C/EBPs. The expression of MBP was
inefficiently induced by C/EBP alone and weakly induced with
C/EBP and GATA-1, but the addition of PU.1 resulted in a striking
cooperative induction of MBP in NIH 3T3 cells. Mutation of a predicted
PU.1 site in the human MBP promoter-luciferase reporter construct
abrogated the response to PU.1. Gel-shift analysis demonstrated binding of PU.1 to this site. MBP and EPX mRNAs were absent in a PU.1-null myeloid cell line established from the embryonic liver of
PU.1/ mice. Restitution of PU.1 protein expression
restored MBP and EPX protein expression. This study demonstrates that
C/EBP is essential and sufficient for the expression of a particular
subset of neutrophil secondary granule genes. Furthermore, it indicates the importance of PU.1 in the cooperative activation of eosinophil granule genes.
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