cDNA Sequence and mRNA Tissue Distribution of a Novel Human Matrix Metalloproteinase with a Potential Transmembrane Segment

Will, Horst; Hinzmann, Bernd

doi:10.1111/j.1432-1033.1995.tb20738.x

Cited by 290 publications

(102 citation statements)

References 21 publications

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“…They consist of collagenases, gelatinases, stromelysins (Birkedal-Hansen et al 1993), matrilysin (MMP-7) (Woessner and Taplin 1988;Quantin et al 1989) and matrix metalloelastases (MMP-12) (Shapiro et al 1993), and membrane-type matrix metalloproteinases (MT-MMPs) (Sato et al 1994;Will and Hinzmann 1995;Hernandez-Barrantes et al 2002). MMPs are known to be important in embryonic development, tissue morphogenesis and repair, inflammation and cancer (Nelson et al 2000;Sternlicht and Werb 2001).…”

Section: Introductionmentioning

confidence: 98%

Overexpression of TIMP-1 under the MMP-9 promoter interferes with wound healing in transgenic mice

Salonurmi

Parikka

Kontusaari

et al. 2004

Cell and Tissue Research

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We have generated transgenic mice harboring the murine matrix metalloproteinase 9 (MMP-9) promoter cloned in front of human TIMP-1 cDNA. The transgenic mice were viable and fertile and exhibited normal growth and general development. During wound healing the mice were shown to express human TIMP-1 in keratinocytes that normally express MMP-9. However, the healing of skin wounds was significantly retarded with slow migration of keratinocytes over the wound in transgenic mice. In situ zymography carried out on wound tissues revealed total blockage of gelatinolytic activity (i.e., MMP-9 and MMP-2). The results confirm studies with MMP-9 knockout mice showing that MMP-9 is not essential for general development, but they also demonstrate an important role of keratinocyte MMP-9, as well that of other keratinocyte MMPs that are inhibited by TIMP-1, in wound healing. The transgenic mice generated in this study provide a model for the role of MMPs in MMP-9-producing cells in other challenging situations such as bone fracture recovery and cancer invasion.

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Section: Introductionmentioning

confidence: 98%

Overexpression of TIMP-1 under the MMP-9 promoter interferes with wound healing in transgenic mice

Salonurmi

Parikka

Kontusaari

et al. 2004

Cell and Tissue Research

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“…4. Membrane-type matrix metalloproteinases (MTMMPs) make up a new subclass and include MT-MMP-1, -2, and -3 (Sato et al 1994;Will and Hinzmann 1995;Takino et al 1995). These MT-MMPs are localized at cell surfaces and their substrate specificities are not yet clear.…”

Section: Introductionmentioning

confidence: 99%

Immunohistochemistry of matrix metalloproteinases (MMP), their substrates, and their inhibitors (TIMP) during trophoblast invasion in the human placenta

Huppertz

Kertschanska

Demir

et al. 1997

Cell and Tissue Research

228

135

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The invasion of extravillous trophoblast cells into the maternal endometrium is one of the key events in human placentation. The ability of these cells to infiltrate the uterine wall and to anchor the placenta to it as well as their ability to infiltrate and to adjust utero-placental vessels to pregnancy depends, among other things, on their ability to secrete enzymes that degrade the extracellular matrix. Most of the latter enzymes belong to the family of matrix metalloproteinases. Their activity is regulated by the tissue inhibitors of matrix metalloproteinases. We have studied the distribution patterns of matrix metalloproteinases-1, -2, -3, and -9 and their inhibitors TIMP-1 and TIMP-2 as compared to the distribution of their substrates along the invasive pathway of extravillous trophoblast of 1st, 2nd, and 3rd trimester placentas by means of light microscopy on paraffin and cryostat sections as well as at the ultrastructural level (only 3rd trimester placenta). The comparison of different methods proved to be necessary, since the immunohistochemical distribution patterns of these soluble enzymes are considerably influenced by the pretreatment of tissues. All three methods revealed immunoreactivities of both, proteinases and their inhibitors, not only intracellularly in the extravillous trophoblast but also extracellularly in its surrounding matrix, the distribution patterns depending on the stage of pregnancy and on the degree of differentiation of trophoblast cells along their invasive pathway. Within the extracellular matrix, immunolocalization of matrix metalloproteinases as well as their inhibitors showed a specific relation to certain extracellular matrix molecules.

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“…The enhanced expression of proM-MP-2 has also been reported in the articular cartilage of human osteoarthritis (Martel-Pelletier et al 1994). In addition to soluble MMP, a family of membrane typematrix metalloproteinases (MT-MMP) has also been described (Will and Hinzmann 1995). Various studies have demonstrated the presence of MTl-MMP in a variety of human carcinoma cells and in their stromal cells (Okada et al 1995;Gilles et al 1996).…”

Section: Introductionmentioning

confidence: 99%

Expression of membrane type 1 matrix metalloproteinase, matrix metalloproteinase 2 and tissue inhibitor of metalloproteinase 2 in human cartilaginous tumors with special emphasis on mesenchymal and dedifferentiated chondrosarcoma

Sakamoto

Oda

Iwamoto

et al. 1999

Journal of Cancer Research and Clinical Oncology

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Membrane type 1 matrix metalloproteinase (MT1-MMP) has been identified as an activator of the proenzyme of matrix metalloproteinase 2 (MMP-2: gelatinase A), and has also been shown to play a crucial role in tumor invasion by activating proMMP2 in both lung and gastric carcinoma. The tissue inhibitor of metalloproteinase 2 (TIMP-2) plus the MT1-MMP complex also plays an important role in the activation of proMMP-2. In this study, the expressions of MT1-MMP, MMP-2 and TIMP-2 were evaluated in 10 enchondromas, 34 conventional chondrosarcomas, 5 clear-cell chondrosarcomas, 7 mesenchymal chondrosarcomas and 8 dedifferentiated chondrosarcomas. The expressions were immunohistochemically visualized on paraffin sections and the levels of expression were assessed semiquantitatively. The extent of staining was assessed by the extent score in order to determine the overall level of expression. The extent scores of MT1-MMP, MMP-2 and TIMP-2 in grade 2 chondrosarcoma were significantly higher than those in either enchondroma or grade 1 chondrosarcoma (P < 0.05). In conventional chondrosarcoma, significant correlations were found between the extent scores of MT1-MMP and MMP-2 (P < 0.001), MT1-MMP and TIMP-2 (P < 0.01), and MMP-2 and TIMP-2 (P < 0.01). The undifferentiated small round tumor cells of mesenchymal chondrosarcoma showed lower positive rates and extent scores for MT1-MMP (2/7, 0.7 +/- 0.5) and MMP-2 (3/7, 0.7 +/- 0.4) than for cartilaginous components of mesenchymal chondrosarcoma [MT1-MMP (4/7, 1.3 +/- 0.5) and MMP-2 (7/7, 1.9 +/- 0.3)] or conventional chondrosarcoma. In dedifferentiated chondrosarcoma, the extent scores of MT1-MMP, MMP-2 and TIMP-2 in low-grade cartilaginous components were not significantly different from those in conventional chondrosarcoma; however, the high-grade anaplastic components showed high extent scores for MT1-MMP, MMP-2 and TIMP-2, compared with the low-grade cartilaginous components of dedifferentiated chondrosarcoma or conventional chondrosarcoma. According to our results, the expression of MT1-MMP as well as that of MMP-2 or TIMP-2 demonstrated a significant correlation with the tumor grade in human cartilaginous tumors. Furthermore, the expressions of MT1-MMP, MMP-2 and TIMP-2 were also found to play a crucial role in invasion in the high-grade components of dedifferentiated chondrosarcoma.

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cDNA Sequence and mRNA Tissue Distribution of a Novel Human Matrix Metalloproteinase with a Potential Transmembrane Segment

Cited by 290 publications

References 21 publications

Overexpression of TIMP-1 under the MMP-9 promoter interferes with wound healing in transgenic mice

Overexpression of TIMP-1 under the MMP-9 promoter interferes with wound healing in transgenic mice

Immunohistochemistry of matrix metalloproteinases (MMP), their substrates, and their inhibitors (TIMP) during trophoblast invasion in the human placenta

Expression of membrane type 1 matrix metalloproteinase, matrix metalloproteinase 2 and tissue inhibitor of metalloproteinase 2 in human cartilaginous tumors with special emphasis on mesenchymal and dedifferentiated chondrosarcoma

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