Matrix metalloproteinases (MMPs) are a family of enzymes capable of degrading extracellular matrix proteins [1].
As their name implies, MMPs were originally described as proteinases capable of degrading extracellular matrix proteins such as collagens, elastin, proteoglycans, and laminins.
As mFBs were capable of producing massive extracellular matrix proteins, most of which was composed of collagen, the total collagen content was quantified for both co-culture and control group.
The results suggest that human pancreatic ductal adenocarcinomas cells are capable of synthesising and producing extracellular matrix proteins in vitro and in vivo, but that the extent and pattern of ECM expression differs between the various tumours and conditions tested.
MMP-3 is a broad spectrum protease capable of cleaving several non-fibrillar extracellular matrix proteins as well as proteolytically activating other MMPs (e.g. MMP-2 and -9).
Our lung tissue model displays a stratified epithelium supported by a fibroblast layer and is capable of mucus secretion and active formation of extracellular matrix proteins (supplementary material Fig. S3) (Nguyen Hoang et al., 2012).
Thus, S. aureus is also capable of directly interacting with osteoblasts in the absence of extracellular matrix proteins such as fibronectin.
