Expression of collagenase‐related metalloproteinase genes in human lung or head and neck tumours

Muller, Danièle; Breathnach, Richard; Engelmann, A.; Millon, Régine; Brönner, G.; Flesch, H.; Dumont, Pascal; Eber, M.; Abecassis, Joseph

doi:10.1002/ijc.2910480412

Cited by 174 publications

(110 citation statements)

References 25 publications

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“…Our data also indicate that MMP-10 expression profiling may be of prognostic significance. Interestingly, MMP-10 overexpression has also been observed in squamous cell carcinomas of the head and neck (Muller et al, 1991;O-Charoenrat et al, 2001), oral cavity (Impola et al, 2004) and esophagus (Mathew et al, 2002). These tumor types harbor frequent chromosome 3q26 and PRKCI amplification (Pimkhaokham et al, 2000;Imoto et al, 2001;Snaddon et al, 2001;Osada and Takahashi, 2002).…”

Section: Discussionmentioning

confidence: 99%

Matrix metalloproteinase-10 is a critical effector of protein kinase Cι-Par6α-mediated lung cancer

et al. 2008

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Section: Discussionmentioning

confidence: 99%

Matrix metalloproteinase-10 is a critical effector of protein kinase Cι-Par6α-mediated lung cancer

et al. 2008

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“…Recent in vivo studies have indicated that cancer cells are able to induce production of proteases by neighbouring stromal cells (Hewitt et al, 1991;Muller et al, 1991;Polette et al, 1991;Borchers et al, 1994). The inability to identify a specific MMP gene or genes common to all cancers supports the probability that progression may be affected by quantitative changes in levels of expression of one or more MMPs, differential expression of TIMP inhibitors, or qualitative changes in the specific genes expressed.…”

Section: Northern Blot Analysis Of Gelatinase a And B Transcriptsmentioning

confidence: 99%

Differential expression of matrix metalloproteinases in activated c-rasHa-transfected immortalized human keratinocytes

Meade-Tollin

Boukamp²,

Fusenig³

et al. 1998

Br J Cancer

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Summary Elevated expression of matrix metalloproteinases (MMPs), a family of secreted proteinases that degrade matrix components of basement membranes and connective tissues, is strongly correlated with malignant expression in various human epithelial cancers and epithelial cancer cell lines. We have tested whether elevated levels of MMP expression are also associated with malignant progression in human cutaneous squamous cell carcinoma. Constitutive levels of expression of steady-state mRNA and of secreted protein encoded by three MMP genes (matrilysin, gelatinases A and B) were compared in a unique in vitro model of human skin carcinogenesis. This model is composed of the parental immortalized non-tumorigenic human keratinocyte line (HaCaT), and three activated c-Harvey-ras-oncogene transfected variants (A-4, 1-7 and 11-4). Although clone A-4 is non-tumorigenic, clones 1-7 and 11-4 exhibit benign and malignant tumorigenic phenotypes, respectively, after subcutaneous injection into athymic nude mice. Northern blot, Western blot, and zymogram analyses revealed three MMP-specific patterns of expression. Constitutive matrilysin mRNA expression was markedly increased in the 1-7 cells compared with HaCaT, A-4 or 11-4 cells. Secreted promatrilysin was distinctly increased in the tumorigenic 1-7 and 11-4 cells compared with the nontumorigenic HaCaT and A-4 cells. Gelatinase A mRNA and secreted gelatinase A protein levels were increased in each transfectant compared with HaCaT. Both active and inactive forms of gelatinase A were detected. Gelatinase B transcripts were not detected, but an EDTA-inhibitable gelatinase activity comigrating with gelatinase B was moderately enhanced in both tumorigenic variants compared with the non-tumorigenic cells. Because promatrilysin and 92-kDa gelatinase secretion were increased in both benign and malignant tumorigenic cells, and not related to invasiveness in this model, it is concluded that enhanced constitutive expression of these two MMPs is associated with acquisition of the tumorigenic phenotype, before acquisition of the malignant phenotype.Keywords: matrilysin; gelatinase; matrix metalloproteinase; human; keratinocyte; HaCaT-ras; malignant progressionThe predominant cause of cancer morbidity and mortality is metastasis of malignant cells from the primary tumour to secondary sites. Therefore, a critical goal in cancer treatment is prevention of metastasis, a process that is considered to involve repeated proteinasemediated degradation and cancer cell invasion of basement membranes and underlying connective tissues. Members of the matrix metalloproteinase (MMP) family of zinc-containing endopeptidases may play a pivotal role in in vivo invasion and metastasis because they can degrade matrix components of the basement membrane. At least 15 different MMPs from human sources have been characterized (Pendas et al, 1997). MMPs are secreted as proenzymes, and are subsequently activated. Furthermore, modulation of MMP activity by endogenous tissue inhibitors of metalloproteinases (TIM...

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“…Since ®brillar collagens are the most abundant structural components of human connective tissues, the ability to degrade them is crucial for invasion and metastasizing of neoplastic cells. Expression of MMP-1 has been observed in lung carcinomas (Urbanski et al, 1992;Wernert et al, 1994), squamous cell carcinomas of the head and neck (Polette et al, 1991;Muller et al, 1991;Gray et al, 1992), and in colorectal tumors, in which expression of MMP-1 correlates with poor prognosis (Hewitt et al, 1991;Murray et al, 1996). In these tumors, stromal cells appear to be responsible for MMP-1 production, indicating importance of crosstalk between tumor and stromal cells in tumor cell invasion (for review see Stetler-Stevenson et al, 1993;Wernert et al, 1994;Bolon et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Differential regulation of interstitial collagenase (MMP-1) gene expression by ETS transcription factors

1997

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Expression of interstitial collagenase (MMP-1) has been detected in stromal ®broblasts of various malignant tumors. Here, we have studied the e ect of three structurally di erent ETS transcription factors (ETS-1, ERGB/Fli-1, and PU.1) on MMP-1 promoter activity in NIH3T3 ®broblasts. ETS-1 increased the activity of 3.8 kb MMP-1 promoter construct up to tenfold, while ERGB/Fli-1 or PU.1 alone had no marked e ect on basal promoter activity. ETS-1 also markedly potentiated enhancement of MMP-1 promoter by both c-Jun and JunB, whereas ERGB/Fli-1 augmented only the e ect of c-Jun. Interestingly, PU.1 abolished induction of MMP-1 promoter by both c-Jun and JunB. Stimulation of MMP-1 promoter by 12-O-tetradecanoyl phorbol-13-acetate and okadaic acid was di erentially augmented by ETS-1 and ERGB/Fli-1, and abrogated by PU.1. Cotransfection studies with MMP-1 promoter 5'-deletion constructs revealed that AP-1 site was necessary for PU.1-elicited suppression. As compared to control cell lines, PU.1-positive stable cells exhibited clearly weaker binding of c-Jun and JunD containing AP-1 complexes to MMP-1 promoter AP-1 element, as well as marked reduction in basal level and induction of c-jun mRNA by 12-O-tetradecanoyl phorbol-13-acetate and okadaic acid, suggesting a novel mechanism for PU.1-mediated inhibition of AP-1 dependent gene expression. These results show that three structurally distinct ETS transcription factors di erently modulate AP-1 dependent upregulation of MMP-1 gene expression.

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Expression of collagenase‐related metalloproteinase genes in human lung or head and neck tumours

Cited by 174 publications

References 25 publications

Matrix metalloproteinase-10 is a critical effector of protein kinase Cι-Par6α-mediated lung cancer

Matrix metalloproteinase-10 is a critical effector of protein kinase Cι-Par6α-mediated lung cancer

Differential expression of matrix metalloproteinases in activated c-rasHa-transfected immortalized human keratinocytes

Differential regulation of interstitial collagenase (MMP-1) gene expression by ETS transcription factors

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