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Literature summary for 3.4.24.7 extracted from

  • Rowe, R.G.; Keena, D.; Sabeh, F.; Willis, A.L.; Weiss, S.J.
    Pulmonary fibroblasts mobilize the membrane-tethered matrix metalloprotease, MT1-MMP, to destructively remodel and invade interstitial type I collagen barriers (2011), Am. J. Physiol. Lung Cell Mol. Physiol., 301, L683-L692.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
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Mus musculus
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fibroblast
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Homo sapiens
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Synonyms

Synonyms Comment Organism
MT1-MMP
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Mus musculus
MT1-MMP
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Homo sapiens

General Information

General Information Comment Organism
physiological function MT1-MMP is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment Mus musculus
physiological function MT1-MMP is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment Homo sapiens