Identification of a novel 82 kDa proMMP-9 species associated with the surface of leukaemic cells: (auto-)catalytic activation and resistance to inhibition by TIMP-1.
MMP-9 (matrix metalloproteinase 9) plays a critical role in tumour progression. Although the biochemical properties of the secreted form of proMMP-9 are well characterized, little is known about the function and activity of cell surface-associated proMMP-9. We purified a novel 82 kDa species of proM...
Main Authors: | Ries, C, Pitsch, T, Mentele, R, Zahler, S, Egea, V, Nagase, H, Jochum, M |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2007
|
Similar Items
-
Fluorescence quenching studies of matrix metalloproteinases (MMPs): evidence for structural rearrangement of the proMMP-2/TIMP-2 complex upon mercurial activation.
by: Stack, MS, et al.
Published: (1996) -
The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface.
by: Itoh, Y, et al.
Published: (2008) -
X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding.
by: Jozic, D, et al.
Published: (2005) -
Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion.
by: Itoh, Y, et al.
Published: (2001) -
ProMMP-1 PRODUCTION BY CULTIVATED CELLS OF VASCULAR ENDОTHELIUM IN VITRO AND IN A HUMAN BODY
by: N. N. Scliankina, et al.
Published: (2014-06-01)