[HTML][HTML] Neutrophil elastase cleaves laminin-332 (laminin-5) generating peptides that are chemotactic for neutrophils
P Mydel, JM Shipley, TL Adair-Kirk, DG Kelley… - Journal of biological …, 2008 - ASBMB
Proteolytic processing of laminin-332 by matrix metalloproteinase (MMP)-2 and MMP-14 has
been shown to yield fragments that are promigratory for epithelial cells. During acute and
chronic inflammation, proteases are elaborated by neutrophils and macrophages that can
degrade basement membranes. We investigated the susceptibility of laminin-332 to
degradation by the following neutrophil and macrophage proteases: neutrophil elastase
(NE), cathepsin G, proteinase-3, and MMPs-2,-8,-9, and-12. Protease-specific differences …
been shown to yield fragments that are promigratory for epithelial cells. During acute and
chronic inflammation, proteases are elaborated by neutrophils and macrophages that can
degrade basement membranes. We investigated the susceptibility of laminin-332 to
degradation by the following neutrophil and macrophage proteases: neutrophil elastase
(NE), cathepsin G, proteinase-3, and MMPs-2,-8,-9, and-12. Protease-specific differences …