TY - JOUR
T1 - ETS sites in the promoters of the matrix metalloproteinases collagenase (MMP-1) stromelysin (MMP-3) are auxiliary elements that regulate basal and phorbol-induced transcription
AU - White, Lori Anne
AU - Maute, Christine
AU - Brinckerhoff, Constance E.
N1 - Funding Information:
Supported by grants from NIH, AR-26599 and The RGK Foundation (to CEB) and by a fellowship from the NH Chapter of the American Heart Association (to LAW).
PY - 1997
Y1 - 1997
N2 - The matrix metalloproteinases collagenase (MMP-1) and stromelysin (MMP-3) are often coordinately expressed, and their promoters contain similar regulatory elements, including an AP-1 site at about -70. There are, however, additional sequences including an adjacent ETS site at about -90 in both promoters, and a NIP (nuclear inhibitory protein) binding site in the stromelysin promoter. In this paper, we have investigated the role of these elements in transcriptional activation by phorbol myristate acetate (PMA). Using mobility shift assays, we demonstrate that in the collagenase promoter, PMA induction requires the binding of nuclear proteins to the ETS site as well as to the adjacent AP-1 element. In the stromelysin promoter, we used mutational analysis and DNA/protein interactions to illustrate a role for a single ETS site and for the NIP element in phorbol induction. These data suggest that ETS elements interact with other cis-acting sequences in these promoters to elicit transcriptional activation, and that the placement of the ETS sites in these promoters may influence transcriptional activity.
AB - The matrix metalloproteinases collagenase (MMP-1) and stromelysin (MMP-3) are often coordinately expressed, and their promoters contain similar regulatory elements, including an AP-1 site at about -70. There are, however, additional sequences including an adjacent ETS site at about -90 in both promoters, and a NIP (nuclear inhibitory protein) binding site in the stromelysin promoter. In this paper, we have investigated the role of these elements in transcriptional activation by phorbol myristate acetate (PMA). Using mobility shift assays, we demonstrate that in the collagenase promoter, PMA induction requires the binding of nuclear proteins to the ETS site as well as to the adjacent AP-1 element. In the stromelysin promoter, we used mutational analysis and DNA/protein interactions to illustrate a role for a single ETS site and for the NIP element in phorbol induction. These data suggest that ETS elements interact with other cis-acting sequences in these promoters to elicit transcriptional activation, and that the placement of the ETS sites in these promoters may influence transcriptional activity.
KW - AP-1
KW - Gel mobility shift analysis
KW - Transcription
KW - Transfection
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U2 - 10.3109/03008209709160231
DO - 10.3109/03008209709160231
M3 - Article
C2 - 9610890
AN - SCOPUS:0031412558
SN - 0300-8207
VL - 36
SP - 321
EP - 335
JO - Connective Tissue Research
JF - Connective Tissue Research
IS - 4
ER -