[HTML][HTML] Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
WH Yu, JF Woessner - Journal of Biological Chemistry, 2000 - ASBMB
Many matrix metalloproteinases (MMPs) are tightly bound to tissues; matrilysin (MMP-7),
although the smallest of the MMPs, is one of the most tightly bound. The most likely docking
molecules for MMP-7 are heparan sulfate proteoglycans on or around epithelial cells and in
the underlying basement membrane. This is established by extraction experiments and
confocal microscopy. The enzyme is extracted from homogenates of postpartum rat uterus
by heparin/heparan sulfate and by heparinase III treatment. The enzyme is colocalized with …
although the smallest of the MMPs, is one of the most tightly bound. The most likely docking
molecules for MMP-7 are heparan sulfate proteoglycans on or around epithelial cells and in
the underlying basement membrane. This is established by extraction experiments and
confocal microscopy. The enzyme is extracted from homogenates of postpartum rat uterus
by heparin/heparan sulfate and by heparinase III treatment. The enzyme is colocalized with …