Journal of Cell Science 115, e1901-e1901 (2002)
Copyright © 2002 The Company of Biologists Limited
doi:
Metalloproteinase inhibitors
Metalloproteinases are secreted or cell surface proteases that degrade or
proteolytically activate other cell surface molecules and components of the
extracellular matrix (ECM). These enzymes are important for control of
cell-cell and cell-ECM interactions during cell migration, differentiation and
proliferation and are regulated by a number of inhibitors. In a Commentary on
p. 3719, Gillian Murphy and
co-workers review our understanding of these inhibitors, which include the
tissue inhibitors of metalloproteinases (TIMPs), TIMP-like molecules such as
netrins, 
2 macroglobulin, and novel proteins such as RECK. TIMPs are
21-kDa proteins that inhibit all known matrix metalloproteinases (MMPs).
Not all of their effects appear to be due to inhibition of MMPs, however.
TIMP2, for example, has mitogenic effects on erythroid precursor cells, acting
through receptors linked to G proteins and cyclic AMP signalling. Similarly,
the biological activities of RECK during angiogenesis probably extend beyond
its ability to inhibit MMP-2, MMP-9 and MT1-MMP, and 2 macroglobulin
might well do more than just inhibit endoproteinases. Murphy and co-workers
suggest that only when these additional activities are fully understood will
we be able to exploit the therapeutic potential of metalloproteinase
inhibitors.
Related articles in JCS:
- Metalloproteinase inhibitors: biological actions and therapeutic opportunities
- Andrew H. Baker, Dylan R. Edwards, and Gillian Murphy
JCS 2002 115: 3719-3727.
[Abstract]
[Full Text]
