PubMed:10408832 JSONTXT

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":32,"end":49},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":237,"end":254},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":420,"end":429},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":1121,"end":1124},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"0005140"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"0005140"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"0004993"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"0012833"}],"text":"MMP-2 release and activation in ovarian carcinoma: the role of fibroblasts.\nThe matrix metalloproteinase MMP-2 is up-regulated in epithelial cancers and its mRNA localizes to stromal fibroblasts. In this paper we show that co-culture of ovarian carcinoma cells with fibroblasts resulted in an enhanced release of proMMP-2 and TIMP-2 into the culture medium. Cell-cell interaction was a major factor in this response and carcinoma cells stimulated proMMP-2 release from fibroblasts but not vice versa. Collagen 1, in a dose-dependent fashion, induced activation of proMMP-2 by tumour-derived, but not normal, fibroblasts. Antibody to beta1 integrin also induced proMMP-2 activation by tumour-derived fibroblasts. The activation involved the processing of proMMP-2 by a membrane-bound metalloproteinase. We propose that, in the ovarian tumour microenvironment, interaction between tumour cells and fibroblasts may enhance fibroblast production of the proMMP-2 and TIMP-2. Collagen I, also present in the ovarian tumours, then induces these fibroblasts to activate proMMP-2 even in the presence of TIMP-2. This active MMP-2 can associate with the cell surface of tumour cells and fibroblasts and is used in the processes of tissue remodelling and invasion."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":141,"end":148},"obj":"HP_0002664"},{"id":"T2","span":{"begin":576,"end":582},"obj":"HP_0002664"},{"id":"T3","span":{"begin":684,"end":690},"obj":"HP_0002664"},{"id":"T4","span":{"begin":826,"end":840},"obj":"HP_0100615"},{"id":"T5","span":{"begin":834,"end":840},"obj":"HP_0002664"},{"id":"T6","span":{"begin":879,"end":885},"obj":"HP_0002664"},{"id":"T7","span":{"begin":1002,"end":1017},"obj":"HP_0100615"},{"id":"T8","span":{"begin":1010,"end":1017},"obj":"HP_0002664"},{"id":"T9","span":{"begin":1160,"end":1166},"obj":"HP_0002664"}],"text":"MMP-2 release and activation in ovarian carcinoma: the role of fibroblasts.\nThe matrix metalloproteinase MMP-2 is up-regulated in epithelial cancers and its mRNA localizes to stromal fibroblasts. In this paper we show that co-culture of ovarian carcinoma cells with fibroblasts resulted in an enhanced release of proMMP-2 and TIMP-2 into the culture medium. Cell-cell interaction was a major factor in this response and carcinoma cells stimulated proMMP-2 release from fibroblasts but not vice versa. Collagen 1, in a dose-dependent fashion, induced activation of proMMP-2 by tumour-derived, but not normal, fibroblasts. Antibody to beta1 integrin also induced proMMP-2 activation by tumour-derived fibroblasts. The activation involved the processing of proMMP-2 by a membrane-bound metalloproteinase. We propose that, in the ovarian tumour microenvironment, interaction between tumour cells and fibroblasts may enhance fibroblast production of the proMMP-2 and TIMP-2. Collagen I, also present in the ovarian tumours, then induces these fibroblasts to activate proMMP-2 even in the presence of TIMP-2. This active MMP-2 can associate with the cell surface of tumour cells and fibroblasts and is used in the processes of tissue remodelling and invasion."}

{"project":"CoMAGC","denotations":[{"id":"T1","span":{"begin":1062,"end":1070},"obj":"Gene"},{"id":"E2","span":{"begin":1053,"end":1061},"obj":"Positive_regulation"},{"id":"T2","span":{"begin":1002,"end":1017},"obj":"ovarian cancer"}],"relations":[{"id":"R1","pred":"themeOf","subj":"T1","obj":"E2"},{"id":"R3","pred":"CGE-increased","subj":"T1","obj":"T2"},{"id":"R4","pred":"CCS-unidentifiable","subj":"T1","obj":"T2"},{"id":"R5","pred":"PT-","subj":"T1","obj":"T2"},{"id":"R3","pred":"IGE-","subj":"T1","obj":"T2"}],"text":"MMP-2 release and activation in ovarian carcinoma: the role of fibroblasts.\nThe matrix metalloproteinase MMP-2 is up-regulated in epithelial cancers and its mRNA localizes to stromal fibroblasts. In this paper we show that co-culture of ovarian carcinoma cells with fibroblasts resulted in an enhanced release of proMMP-2 and TIMP-2 into the culture medium. Cell-cell interaction was a major factor in this response and carcinoma cells stimulated proMMP-2 release from fibroblasts but not vice versa. Collagen 1, in a dose-dependent fashion, induced activation of proMMP-2 by tumour-derived, but not normal, fibroblasts. Antibody to beta1 integrin also induced proMMP-2 activation by tumour-derived fibroblasts. The activation involved the processing of proMMP-2 by a membrane-bound metalloproteinase. We propose that, in the ovarian tumour microenvironment, interaction between tumour cells and fibroblasts may enhance fibroblast production of the proMMP-2 and TIMP-2. Collagen I, also present in the ovarian tumours, then induces these fibroblasts to activate proMMP-2 even in the presence of TIMP-2. This active MMP-2 can associate with the cell surface of tumour cells and fibroblasts and is used in the processes of tissue remodelling and invasion."}