Purification of active matrix metalloproteinase catalytic domains and its use for screening of specific stromelysin-3 inhibitors

被引:28
|
作者
Kannan, R
Ruff, M
Kochins, JG
Manly, SP
Stoll, I
El Fahime, M
Noël, A
Foidart, JM
Rio, MC
Dive, V
Basset, P
机构
[1] Univ Strasbourg 1, IGBMC, CNRS, INSERM, F-67404 Illkirch Graffenstaden, France
[2] Bristol Myers Squibb Co, Pharmaceut Res Inst, Wallingford, CT 06492 USA
[3] Univ Liege, Lab Biol Tumeurs & Dev, B-4000 Liege, Belgium
[4] CEA, Dept Ingn & Etud Prot, F-91191 Gif Sur Yvette, France
关键词
alpha-1 proteinase inhibitor; cephalosporin; matrix metalloproteinase inhibitors; stromelysin-3;
D O I
10.1006/prep.1999.1068
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The matrix metalloproteinase (MMP) stromelysin-3 (ST3) has been shown to be involved in malignant tumor progression and therefore represents an attractive therapeutical target. In order to screen for ST3 synthetic inhibitors, we have produced and purified the catalytic domain of ST3, matrilysin, stromelysin-a, and membrane type-1 MMP from inclusion bodies in a bacterial system. Our strategy allowed the purification of MMPs directly in the active form, thereby avoiding in vitro activation. A total of 140,000 synthetic compounds from the Bristol-Myers Pharmaceutical Research Institute chemical deck were tested, using a substrate-based colorimetric enzymatic assay, in which ST3 activity was evaluated through its ability to cleave and inactivate alpha-1 proteinase inhibitor. One ST3 inhibitor belonging to the cephalosporin family of antibiotics was thereby identified. (C) 1999 Academic Press.
引用
收藏
页码:76 / 83
页数:8
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