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J Biol Chem, Vol. 275, Issue 11, 8176-8182, March 17, 2000

Inhibition of Laminin-5 Production in Breast Epithelial Cells by Overexpression of p300*

Kristi A. MillerDagger , Jean ChungDagger , David LoDagger , Jonathan C. R. Jones§, Bayar Thimmapaya, and Sigmund A. WeitzmanDagger ||

From the Departments of Dagger  Medicine, Division of Hematology/Oncology, § Cell and Molecular Biology, and  Microbiology and Immunology and the Lurie Cancer Center, Northwestern University Medical School, Chicago, Illinois 60611

The transcriptional coactivator p300 is essential for normal embryonic development and cellular differentiation. We have been studying the role of p300 in the transcription of a variety of genes, and we became interested in the role of this coactivator in the transcription of genes important in breast epithelial cell biology. From MCF-10A cells (spontaneously immortalized, nontransformed human breast epithelial cells), we developed cell lines that stably overexpress p300. These p300-overexpressing cells displayed reduced adhesion to culture dishes and were found to secrete an extracellular matrix deficient in laminin-5. Laminin-5 is the major extracellular matrix component produced by breast epithelium. Immunofluorescence studies, as well as experiments using normal matrix, confirmed that the decreased adhesion of p300-overexpressing cells is due to laminin-5-deficient extracellular matrix and not due to loss of laminin-5 receptors. Northern blots revealed markedly decreased levels of expression of two of the genes (designated LAMA3 and LAMC2) encoding the alpha 3 and gamma 2 chains of the laminin-5 heterotrimer in the cells that overexpress p300, whereas LAMB3 mRNA, encoding the third or beta 3 chain of laminin-5, was not markedly reduced. Transient transfection experiments with a vector containing a murine LAMA3 promoter demonstrate that overexpressing p300 down-regulates the LAMA3 promoter. In summary, overexpression of p300 leads to down-regulation of laminin-5 production in breast epithelial cells, resulting in decreased adhesion.

* This work was supported by United States Army Grants DAMD17-94-J-4466 (to K. A. M.) and DAMD17-94-J-4291(to J. C. R. J. and S. A. W.), National Institutes of Health Grants 5T32CA09560 (to K. A. M.), DE12328 (to J. C. R. J.), and CA74403 (to B.T.).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.

|| To whom correspondence should be addressed: Olson 8524, 303 E. Chicago Ave., Chicago, IL 60611. Tel.: 312-908-5284; Fax: 312-908-5717; E-mail: saweitz@casbah.acns.nwu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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