FEBS Letters · 2004 · 196 citations · 33 references
Life SciencesBiochemistryMolecular BiologyCell SignalingEnzymologyGene ExpressionExtracellular MatrixExtracellular Matrix BiochemistryMatrix Metalloproteinase GeneticsPlacental DevelopmentExtracellular Matrix ProteinsGrowth FactorsMatrix Metalloproteinase Gene ExpressionMatrix Metalloproteinase Gene RegulationMatrix Metalloproteinase InhibitorsMatrix Metalloproteinase ProcessingMatrix MetalloproteinasesMembrane Type Matrix Metalloproteinases
Matrix metalloproteinases (MMPs) and adamalysins (ADAMs) cleave many extracellular proteins, including matrix, growth factors, and receptors. We profiled the RNA levels of every MMP, several ADAMs, and inhibitors of metalloproteinases (TIMPs and RECK) in numerous mouse tissues during development and in the uterus during pregnancy. Observations include: most secreted MMPs are expressed at low to undetectable levels in tissues, whereas membrane-bound MMPs, ADAMs and inhibitors are abundant; almost every proteinase and inhibitor is present in the uterus or placenta at some time during gestation; the mouse collagenases mColA and mColB are found exclusively in the uterus and testis; and each tissue has its unique signature of proteinase and inhibitor expression.
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A metalloprotease-disintegrin participating in myoblast fusion
Takako Yagami-Hiromasa, Tomomi Sato, Tomohiro Kurisaki et al. · Nature · 1995 · 485 citations
Caroline M. Alexander, Elizabeth Hansell, Ole Behrendtsen et al. · Development · 1996 · 346 citations