The collagenase gene family in humans consists of at least four members

Muller, Danièle; Quantin, Beatrice; Gesnel, Marie-Claude; Millon-Collard, R; Abecassis, Joseph; Breathnach, Richard

doi:10.1042/bj2530187

Cited by 345 publications

(221 citation statements)

References 19 publications

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“…The probes for metalloproteases 1, 3 and 7 were generous gifts from Dr H Satoh. The probes for bovine urokinase-type plasminogen activator (uPA) and (Whithan et al, 1986), the full coding sequence for MMP-7 cDNA (Muller et al, 1988) and the full coding sequence for uPA and uPA receptor cDNA (Kratzschmar et al, 1993).…”

Section: Western Northern and Southern Blot Analysesmentioning

confidence: 99%

Midkine induces the transformation of NIH3T3 cells

Kadomatsu

Hagihara²,

Akhter³

et al. 1997

Br J Cancer

138

111

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Summary Midkine (MK) is a heparin-binding growth factor and is frequently expressed at high levels in many human carcinomas. To investigate further the roles of MK in the regulation of cell growth, we introduced MK expression in NIH3T3 cells. A mixture of transfectants of an MK expression vector, but not a control vector, formed colonies in soft agar, showed an elevated cell number at confluence, and formed tumours in nude mice. An interesting characteristic of the transformed cells was that they became spontaneously detached from the culture dish substratum. In the transformed cells, MK was not only secreted, but also localized, in the perinuclear region as spots. The present data indicate that MK has the potential to transform NIH3T3 cells and suggest that overexpression of the MK gene may promote unregulated cell growth in vivo.

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Section: Western Northern and Southern Blot Analysesmentioning

confidence: 99%

Midkine induces the transformation of NIH3T3 cells

Kadomatsu

Hagihara²,

Akhter³

et al. 1997

Br J Cancer

138

111

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“…A 350-bp sequence of the matrilysin full-length cDNA probe (Muller et al, 1988) was radioactively labelled with [a-32P]dCTP (3000 Ci mmol-1) by random priming (US Biochemical, Cleveland, OH, USA). The gelatinase A probe was a synthetic 80-bp oligonucleotide whose sequence was complementary to a region of the 3' end of the respective cDNA sequence (nucleotides 1937-2015) (Midland Scientific, Midland, TX, USA) (Wilhelm et al, 1989;Basset et al, 1990).…”

Section: Northern Blot Analysesmentioning

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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“…Like several other MMPs, Str1 was ®rst cloned and later recloned as a cancer-speci®c gene (Matrisian et al, 1985;Muller et al, 1988;Ostrowski et al, 1988). In addition to degrading numerous ECM components, Str1 can activate gelatinase B and the collagenases, and can activate several serpin-type serine proteinase inhibitors (Sternlicht and Werb, 1999, for review).…”

Section: Introductionmentioning

confidence: 99%

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

2000

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Extracellular matrix-degrading matrix metalloproteinases (MMPs) are invariably upregulated in epithelial cancers and are key agonists in angiogenesis, invasion and metastasis. Yet most MMPs are secreted not by the cancer cells themselves, but by stromal cells within and around the tumor mass. Because the stromal environment can in¯uence tumor formation, and because MMPs can alter this environment, MMPs may also contribute to the initial stages of cancer development. Several recent studies in MMP-overexpressing and MMP-de®cient mice support this possibility, but have required carcinogens or pre-existing oncogenic mutations to initiate tumorigenesis. Here we review the spontaneous development of premalignant and malignant lesions in the mammary glands of transgenic mice that express an autoactivating form of MMP-3/stromelysin-1 under the control of the whey acidic protein gene promoter. These changes were absent in nontransgenic littermates and were quenched by co-expression of a human tissue inhibitor of metalloproteinases-1 (TIMP-1) transgene. Thus by altering the cellular microenvironment, stromelysin-1 can act as a natural tumor promoter and enhance cancer susceptibility.

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The collagenase gene family in humans consists of at least four members

Cited by 345 publications

References 19 publications

Midkine induces the transformation of NIH3T3 cells

Midkine induces the transformation of NIH3T3 cells

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

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

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