Genes of the Membrane-Type Matrix Metalloproteinase (MT-MMP) Gene Family, MMP14, MMP15, and MMP16, Localize to Human Chromosomes 14, 16, and 8, Respectively

Mattei, Marie-Genevı̀eve; Roëckel, Nathalie; Olsen, Bjørn R.; Apte, Suneel S.

doi:10.1006/geno.1996.4559

Cited by 28 publications

(13 citation statements)

References 7 publications

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“…According to our data, the genomic gene of MMP-26 is localized at the 11p15.3 loci, thereby being distant from the 11q21-q23 cluster of at least eight MMP genes (MMP-1, -3, -7, -8, -10, -12, -13, -20 and -27) [16]. The chromosomal gene of MMP-26 consists of six exons.…”

Section: Mapping Of the Transcription Start Sitementioning

confidence: 83%

Promoter characterization of the novel human matrix metalloproteinase-26 gene: regulation by the T-cell factor-4 implies specific expression of the gene in cancer cells of epithelial origin

Марченко

Marchenko

LENG³

et al. 2002

Biochemical Journal

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A novel matrix metalloproteinase-26 (MMP-26) is known to be specifically expressed in epithelial carcinomas. To facilitate studies of MMP-26 transcriptional regulation, we have cloned and characterized a 1 kb 5h-flanking region of the human MMP-26 gene. Altogether, our findings indicate that the MMP-26 promoter has distinctive structural and functional features among MMP genes. An unusual polyadenylation site proximal to the transcription-factor-binding sites protects transcription of the MMP-26 gene from the upstream promoters and represents a part of the stringent transcriptional regulation of the gene. The MMP-26 gene has a consensus TATA-box and one transcriptional start site located 60 and 35 nucleotides upstream of the translational start site, respectively. The MMP-26 promoter was able to drive luciferase expression in human A549 lung carcinoma, HT1080 fibrosarcoma and HEK293 embryonic kidney

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Section: Mapping Of the Transcription Start Sitementioning

confidence: 83%

Promoter characterization of the novel human matrix metalloproteinase-26 gene: regulation by the T-cell factor-4 implies specific expression of the gene in cancer cells of epithelial origin

Марченко

Marchenko

LENG³

et al. 2002

Biochemical Journal

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“…Soluble forms of MT1-MMP, ACE, DPPIV and APN are detectable in biological fluids (plasma, urine, synovial fluid) (Antczak et al, 2001b;Seiki, 2002;Kawai et al, 2003). TPs have been cloned and are localized at distinct chromosomal loci (Cambien and Soubrier, 1995;Alhenc-Gelas et al, 1997;Mattei et al, 1997;Cerretti, 1999;Antczak et al, 2001a). A polymorphism in the ACE gene exists, consisting of the insertion (I) or deletion (D) of a 287 bp DNA fragment in intron 16, which accounts for 20% of the variance in ACE expression or activity in blood and tissues among individuals (Cambien and Soubrier, 1995;Danilov et al, 1996).…”

Section: Normal Distribution and Correlation With Human Pathologymentioning

confidence: 99%

Transmembrane proteases in cell growth and invasion: new contributors to angiogenesis?

2004

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“…The results were compared with previously defined markers to obtain the linkage data. According to linkage mapping, the MMP-26 gene is located in the 11p15.3 loci, and is therefore distant from the 11q21-q23 cluster of at least eight MMP genes (MMP-1, MMP-3, MMP-7, MMP-8, MMP-10, MMP-12, MMP-13 and MMP-20) [46].…”

Section: Chromosomal Location and Genomic Structure Of The Mmp-26 Genementioning

confidence: 99%

Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin

Марченко

Ratnikov

Rozanov

et al. 2001

Biochemical Journal

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Identification of expanding roles for matrix metalloproteinases (MMPs) in complex regulatory processes of tissue remodelling has stimulated the search for genes encoding proteinases with unique functions, regulation and expression patterns. By using a novel cloning strategy, we identified three previously unknown human MMPs, i.e. MMP-21, MMP-26 and MMP-28, in comprehensive gene libraries. The present study is focused on the gene and the protein of a novel MMP, MMP-26. Our findings show that MMP-26 is specifically expressed in cancer cells of epithelial origin, including carcinomas of lung, prostate and breast. Several unique structural and regulatory features, including an unusual ' cysteine-switch ' motif, discriminate broadspectrum MMP-26 from most other MMPs. MMP-26 efficiently cleaves fibrinogen and extracellular matrix proteins, including fibronectin, vitronectin and denatured collagen. Protein sequence, minimal modular domain structure, exon-intron map-

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Genes of the Membrane-Type Matrix Metalloproteinase (MT-MMP) Gene Family, MMP14, MMP15, and MMP16, Localize to Human Chromosomes 14, 16, and 8, Respectively

Cited by 28 publications

References 7 publications

Promoter characterization of the novel human matrix metalloproteinase-26 gene: regulation by the T-cell factor-4 implies specific expression of the gene in cancer cells of epithelial origin

Promoter characterization of the novel human matrix metalloproteinase-26 gene: regulation by the T-cell factor-4 implies specific expression of the gene in cancer cells of epithelial origin

Transmembrane proteases in cell growth and invasion: new contributors to angiogenesis?

Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin

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