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Originally published In Press as doi:10.1074/jbc.M109793200 on November 16, 2001

J. Biol. Chem., Vol. 277, Issue 4, 2997-3005, January 25, 2002
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Role of CBP/p300 and SRC-1 in Transcriptional Regulation of the Pulmonary Surfactant Protein-A (SP-A) Gene by Thyroid Transcription Factor-1 (TTF-1)*

Ming YiDagger , Guo-Xia TongDagger **, Barbara MurryDagger , and Carole R. MendelsonDagger §

From the Departments of Dagger  Biochemistry and § Obstetrics & Gynecology, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9038

Surfactant protein-A (SP-A) gene expression is developmentally regulated in fetal lung type II cells and is enhanced by cAMP. cAMP stimulation of SP-A gene expression is mediated by protein kinase A (PKA) phosphorylation of thyroid transcription factor 1 (TTF-1), expressed selectively in developing lung epithelium. In this study, we analyzed roles of CREB-binding protein (CBP) and steroid receptor coactivator-1 (SRC-1) in TTF-1 regulation of SP-A expression. Upon differentiation of human fetal lung in culture, nuclear localization of CBP, SRC-1, and TTF-1 increased in ductular epithelium in association with type II cell differentiation and induction of SP-A expression. In transient transfections, CBP and SRC-1 acted synergistically with TTF-1 to increase SP-A promoter activity. Overexpression of PKA catalytic subunit enhanced hSP-A promoter activation by SRC-1 plus TTF-1. Adenoviral E1A overexpression reduced TTF-1 ± SRC-1 induction of SP-A promoter activity, suggesting a role of endogenous CBP/p300. TTF-1 interacted with SRC-1 and CBP in vitro. SRC-1 immunodepletion from type II cell nuclear extracts reduced binding to the TTF-1 binding element upstream of SP-A gene. In cultured type II cells, cAMP increased TTF-1 acetylation. This suggests that cAMP-mediated TTF-1 phosphorylation facilitates interaction with CBP and SRC-1, resulting in its hyperacetylation, further enhancing TTF-1 DNA-binding and transcriptional activity.

* This work was supported by National Institutes of Health Grant R37HL50022.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** Present address: Dept. of Pathology, New York University School of Medicine.

To whom correspondence should be addressed: Dept. of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Blvd., Dallas, TX 75390-9038. Tel.: 214-648-2944; Fax: 214-648-3214; E-mail: cmende@biochem.swmed.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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