Constitutive expression and regulation of collagenase-3 in human breast cancer cells

Nagarajan Selvamurugan, Nicola Partridge

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)218-223
Number of pages6
JournalMolecular Cell Biology Research Communications
Volume3
Issue number4
DOIs
StatePublished - Apr 2000

Fingerprint

Matrix Metalloproteinase 13
Breast Neoplasms
Physiological Phenomena
Transcription Factor AP-1
Pathologic Processes
Matrix Metalloproteinases
Extracellular Matrix
Transfection
Binding Sites
Neoplasm Metastasis
Cell Line
Neoplasms

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 journalArticle

@article{720ec8c3f3cc49d88df0a1581139b05c,
title = "Constitutive expression and regulation of collagenase-3 in human breast cancer cells",
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.",
keywords = "Activator protein-1, Collagenase- 3, Core binding factor, Matrix metalloproteinase, Tumor metastasis and invasion",
author = "Nagarajan Selvamurugan and Nicola Partridge",
year = "2000",
month = "4",
doi = "10.1006/mcbr.2000.0215",
language = "English (US)",
volume = "3",
pages = "218--223",
journal = "Molecular Cell Biology Research Communications",
issn = "1522-4724",
publisher = "Academic Press Inc.",
number = "4",

}

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

UR - http://www.scopus.com/inward/record.url?scp=0033862549&partnerID=8YFLogxK

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

C2 - 10891395

AN - SCOPUS:0033862549

VL - 3

SP - 218

EP - 223

JO - Molecular Cell Biology Research Communications

JF - Molecular Cell Biology Research Communications

SN - 1522-4724

IS - 4

ER -