Fibronectin degradation by MMP14, TMPRSS6

Stable Identifier
R-HSA-2533950
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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MMP14 (MT1-MMP) can degrade fibronectin (Shi & Sottile 2011). Studies have shown that fibronectin turnover is not prevented by protease inhibitors (Sottile & Hocking 2002) and suggest that caveolin-1-mediated endocytosis and intracellular degradation are involved (Salicioni et al. 2002, Sottile & Chandler 2004). Transmembrane protease serine 6 (Matriptase-2, TMPRSS6) is a transmembrane serine proteinase able to hydrolyze endogenous proteins such as type I collagen, fibronectin, and fibrinogen (Velasco et al. 2002).

Literature References
PubMed ID Title Journal Year
12149247 Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins

Velasco, G, Cal, S, Quesada, V, Sánchez, LM, López-Otín, C

J. Biol. Chem. 2002
22159414 MT1-MMP regulates the turnover and endocytosis of extracellular matrix fibronectin

Shi, F, Sottile, J

J. Cell. Sci. 2011
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
metalloendopeptidase activity of MMP14,TMPRSS6 [plasma membrane]
Physical Entity
Activity
Orthologous Events
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