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Volume 271, Number 31, Issue of August 2, 1996 pp. 18981-18988
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Activation of a Nuclear DNA-binding Protein Recognized by a Transcriptional Element, bcn-1, from the Laminin B2 Chain Gene Promoter

(Received for publication, November 17, 1995, and in revised form, May 2, 1996)

From the Department of Medicine, University of Washington, Seattle, Washington 98195

Treatment of mesangial cells with either phorbol 12-myristate 13-acetate (PMA) or interleukin-1 induces an increase in laminin B2 chain mRNA levels. In other systems, activation of gene expression by these agents is transcriptionally mediated. To identify transcription factors that control expression of laminin B2 chain gene, we employed a strategy consisting of a computer-based analysis of murine and human gene promoter sequences and gel shift assays. Although overall the laminin B2 chain promoters from the two species have low sequence similarity, the mouse promoter contained sequences that were also contained in one motif, 5-CCCCGCCCACCTCGCGCGC-3, designated bcn-1, from the human promoter. Treatment of mesangial cells with either PMA or interleukin-1 induced a transient increase in nuclear DNA binding activity, designated BCN-1, recognized the bcn-1 motif in a gel shift assay. A single nucleotide replacement in the bcn-1 motif abolished DNA binding, indicating that bcn-1·BCN-1 complex formation is highly specific. In transient transfections, the ability of PMA to induce the laminin B2 chain promoter was abolished by mutating the bcn-1 motif. These results suggest that the bcn-1 element and its cognate inducible BCN-1 protein regulate laminin B2 chain gene transcription.

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