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  • 1
    Electronic Resource
    Electronic Resource
    A matrix metalloproteinase expressed on the surface of invasive tumour cells (1994)
    [s.l.] : Nature Publishing Group
    Nature 370 (1994), S. 61-65 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We screened cDNAs with homology to conserved regions in matrix metalloproteinase (MMP) genes (Fig. 1 legend) and iso-lated a unique 3.4-kilobase (kb) cDNA fragment (MMP-X1) from a human placenta cDNA library. This cDNA encodes a unique protein of 582 amino acids (Mr 66K) which can be closely ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/370061a0
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  • 2
    Electronic Resource
    Electronic Resource
    Heat shock-mediated transient increase in intracellular 3′, 5′-cyclic AMP results in tumor specific suppression of membrane type 1-matrix metalloproteinase production and progelatinase A activation (2000)
    Springer
    Clinical & experimental metastasis 18 (2000), S. 131-138 
    Details
    ISSN: 1573-7276
    Keywords: cAMP ; gelatinase A ; heat shock ; human fibroblasts ; human fibrosarcoma cells ; MT1-MMP ; tumor invasion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have previously reported that heat shock suppresses the production and gene expression of membrane type 1-matrix metalloproteinase (MT1-MMP) and thereby inhibits the activation of progelatinase A/proMMP-2 in human fibrosarcoma HT-1080 cells and human squamous carcinoma A431 cells and SAS cells (Sato et al. Biochem Biophys Res Commun 1999; 265: 189–93). In an effort to clarify the heat shock-mediated signal transduction pathways, an intracellular cAMP level was found to be transiently augmented in the heat shocked HT-1080 cells. When HT-1080 cells were pretreated with cAMP elevating reagents, forskolin and dibutyryl cAMP for 4 h instead of heat shock and then maintained in a fresh medium, the production and gene expression of MT1-MMP were similarly suppressed. The MT1-MMP-mediated activation of proMMP-2 was also inhibited in the forskolin- and dibutyryl cAMP-treated HT-1080 cells. Furthermore, the transiently augmented cAMP by forskolin as well as heat shock interfered with in vitro invasive activity of HT-1080 cells. In contrast, in normal human fibroblasts neither heat shock nor cAMP elevating reagents altered the concanavalin A-augmented MT1-MMP production and proMMP-2 activation. These results suggest that a transient increase in intracellular cAMP is a critical signal for heat shock to induce tumor specific-suppression of MT1-MMP production and proMMP-2 activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006760021997
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  • 3
    Electronic Resource
    Electronic Resource
    Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human oral squamous cell carcinomas: Implications for lymph node metastasis (2000)
    Springer
    Clinical & experimental metastasis 18 (2000), S. 179-188 
    Details
    ISSN: 1573-7276
    Keywords: activation of proMMP-2 ; lymph node metastasis ; matrix metalloproteinase ; membrane-type matrix metalloproteinase ; oral squamous cell carcinoma ; tissue inhibitor of metalloproteinases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We measured the production levels of seven different matrix metalloproteinases (MMP-1, 2, 3, 7, 8, 9 and 13) and two tissue inhibitors of metalloproteinases (TIMP-1 and 2) in the homogenates of human oral squamous cell carcinomas and control normal squamous epithelia by the corresponding sandwich enzyme immunoassay systems. The levels of MMP-1, 2, 3, 8, 9, 13 and TIMP-1 were significantly higher in the carcinoma samples than in the control. Among them, only the production level of MMP-2 was significantly higher in the carcinomas with cervical lymph node metastasis than in those without metastasis (P 〈 0.05). Gelatin zymography demonstrated that activation ratio of the zymogen of MMP-2 (proMMP-2) is significantly higher in the carcinomas with lymph node metastasis than in those without metastasis (P 〈 0.05) or normal control (P 〈 0.01). Quantitative RT-PCR for membrane-types 1, 2 and 3 MMPs (MT1, 2 and 3-MMPs), which activate proMMP-2 in vitro, demonstrated that MT1-MMP is predominantly expressed in the carcinoma tissues, and the expression level is significantly higher in the carcinomas with lymph node metastasis than in those without metastasis (P 〈 0.05) or the control samples (P 〈 0.05). Although MT2-MMP and MT3-MMP were detected in approximately 30% of the carcinoma cases, their expression levels were extremely lower compared with that of MT1-MMP. There was a direct correlation between the MT1-MMP expression level and proMMP-2 activation ratio (r = 0.62, P 〈 0.01). In situ hybridization and immunohistochemistry indicated that carcinoma cells and stromal cells adjacent to carcinoma cell nests express MT1-MMP transcripts and protein. MMP-2 and TIMP-2 were also immunolocalized to the carcinoma cells in the carcinoma samples. By in situ zymography, gelatinolytic activity was demonstrated in the carcinoma cell nests and abolished by the treatment with an MMP inhibitor, BB94. These results suggest that among seven different MMPs, the production of proMMP-2 and its activation mediated by MT1-MMP play an important role in the cervical lymph node metastasis of the human oral squamous cell carcinomas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006749501682
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  • 4
    Electronic Resource
    Electronic Resource
    Identification of cis-acting promoter elements that support expression of membrane-type 1 matrix metalloproteinase (MT1-MMP) in v-src transformed Madin–Darby canine kidney cells (2000)
    Springer
    Clinical & experimental metastasis 18 (2000), S. 675-681 
    Details
    ISSN: 1573-7276
    Keywords: invasion ; MT1-MMP ; promoter ; transformant ; v-src
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Membrane-type 1 matrix metalloproteinase (MT1-MMP) expressed in tumor cells is believed to be important for the pericellular degradation of extracellular matrices during invasion and metastasis. To analyze the mechanism by which MT1-MMP becomes expressed in cancer cells, we assessed the MT1-MMP promoter region for the presence of cis-acting promoter elements that support transcription in transformed cells. Our tumor model consisted of Madin–Darby canine kidney (MDCK) cells transformed by v-src (src4 cells). MT1-MMP mRNA was only faintly detected in parental cells but was strongly expressed in the src4 cells. In parallel, src4 cells invaded into collagen gels, whereas MDCK cells did not. When MDCK and src4 cells were transiently transfected with a plasmid containing of −3000 to −99 nt from the upstream region of the MT1-MMP gene, the promoter activity was 2.6-fold higher in src4 cells than in MDCK cells. Furthermore, the region between −399 and −356 nt was found to contain the src4-specific enhancer element(s). Tandem Sp1 binding sites were also found to be essential in promoting transcription. An Egr-1 site that partially overlaps with the Sp1 sites was found to cooperate with the src4-specific enhancer and to also contribute weakly to the basal promoter activity. The presence of transcription factors that bind to the src4-specific enhancer site was detected by mobility-shift assays in src4 cell nuclear extracts but only weakly in MDCK extracts. Thus, we have identified a novel enhancer element that acts specifically in the transformed cells to enhance MT1-MMP expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1013190118556
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