Abstract
Matrix metalloproteinases (MMPs) are a family of secreted or transmembrane proteins that have been implicated in multiple physiological and pathological processes related to extracellular matrix turnover. Recent evidence strongly suggests a role for collagenase-3 (MMP-13) in tumor metastasis and invasion. We report here that collagenase-3 is constitutively expressed in the breast cancer cell line MDA-MB231 (MDA) and outline the molecular mechanism regulating its expression. Functional analysis of the collagenase-3 promoter showed that both the activator protein-1 (AP-1) site and the runt domain (RD) binding site were required for maximal constitutive expression of collagenase-3 in MDA cells. Determination of factors binding to those sites by Northern analysis and transient transfections identified the requirement of Fra-1, c-Jun, and Cbfa1 for basal collagenase-3 promoter activity in MDA cells. (C) 2000 Academic Press.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 218-223 |
| Number of pages | 6 |
| Journal | Molecular Cell Biology Research Communications |
| Volume | 3 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 2000 |
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Keywords
- Activator protein-1
- Collagenase- 3
- Core binding factor
- Matrix metalloproteinase
- Tumor metastasis and invasion
ASJC Scopus subject areas
- Molecular Biology
Cite this
Constitutive expression and regulation of collagenase-3 in human breast cancer cells. / Selvamurugan, Nagarajan; Partridge, Nicola.
In: Molecular Cell Biology Research Communications, Vol. 3, No. 4, 04.2000, p. 218-223.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Constitutive expression and regulation of collagenase-3 in human breast cancer cells
AU - Selvamurugan, Nagarajan
AU - Partridge, Nicola
PY - 2000/4
Y1 - 2000/4
N2 - Matrix metalloproteinases (MMPs) are a family of secreted or transmembrane proteins that have been implicated in multiple physiological and pathological processes related to extracellular matrix turnover. Recent evidence strongly suggests a role for collagenase-3 (MMP-13) in tumor metastasis and invasion. We report here that collagenase-3 is constitutively expressed in the breast cancer cell line MDA-MB231 (MDA) and outline the molecular mechanism regulating its expression. Functional analysis of the collagenase-3 promoter showed that both the activator protein-1 (AP-1) site and the runt domain (RD) binding site were required for maximal constitutive expression of collagenase-3 in MDA cells. Determination of factors binding to those sites by Northern analysis and transient transfections identified the requirement of Fra-1, c-Jun, and Cbfa1 for basal collagenase-3 promoter activity in MDA cells. (C) 2000 Academic Press.
AB - Matrix metalloproteinases (MMPs) are a family of secreted or transmembrane proteins that have been implicated in multiple physiological and pathological processes related to extracellular matrix turnover. Recent evidence strongly suggests a role for collagenase-3 (MMP-13) in tumor metastasis and invasion. We report here that collagenase-3 is constitutively expressed in the breast cancer cell line MDA-MB231 (MDA) and outline the molecular mechanism regulating its expression. Functional analysis of the collagenase-3 promoter showed that both the activator protein-1 (AP-1) site and the runt domain (RD) binding site were required for maximal constitutive expression of collagenase-3 in MDA cells. Determination of factors binding to those sites by Northern analysis and transient transfections identified the requirement of Fra-1, c-Jun, and Cbfa1 for basal collagenase-3 promoter activity in MDA cells. (C) 2000 Academic Press.
KW - Activator protein-1
KW - Collagenase- 3
KW - Core binding factor
KW - Matrix metalloproteinase
KW - Tumor metastasis and invasion
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UR - http://www.scopus.com/inward/citedby.url?scp=0033862549&partnerID=8YFLogxK
U2 - 10.1006/mcbr.2000.0215
DO - 10.1006/mcbr.2000.0215
M3 - Article
VL - 3
SP - 218
EP - 223
JO - Molecular Cell Biology Research Communications
JF - Molecular Cell Biology Research Communications
SN - 1522-4724
IS - 4
ER -