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- W1648100608 abstract "Tumor invasion and metastasis formation are major obstacles for successful cancer therapy. Metastasis is a complex multistep process that requires sequential interactions between the invasive cell and the extracellular matrix. A model system for tumor invasion of extracellular matrix barriers has been developed, and application of this model has facilitated our understanding of the molecular mechanisms of metastasis formation. This model consists of three steps: tumor cell adhesion, extracellular matrix proteolysis, and cell migration. The role of the matrix metalloprotease enzymes in tumor cell-mediated extracellular matrix proteolysis is well established. We review the functional domain structure of the matrix metalloprotease enzymes in general and specifically the interaction of metastasis-associated gelatinase A (72-kDa type IV collagenase) with the tissue inhibitor of metalloproteases-2 (TIMP-2). We also discuss the physiologic activation of the matrix metalloprotease enzymes and the specific cellular mechanism of action of gelatinase A." @default.
- W1648100608 created "2016-06-24" @default.
- W1648100608 creator A5012764896 @default.
- W1648100608 creator A5019378601 @default.
- W1648100608 creator A5086886026 @default.
- W1648100608 date "1993-12-01" @default.
- W1648100608 modified "2023-10-17" @default.
- W1648100608 title "Extracellular matrix 6: Role of matrix metalloproteinases in tumor invasion and metastasis" @default.
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- W1648100608 doi "https://doi.org/10.1096/fasebj.7.15.8262328" @default.
- W1648100608 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8262328" @default.
- W1648100608 hasPublicationYear "1993" @default.
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