Reference : Purification of active matrix metalloproteinase catalytic domains and its use for scr...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Purification of active matrix metalloproteinase catalytic domains and its use for screening of specific stromelysin-3 inhibitors.
Kannan, R. [ > > ]
Ruff, M. [ > > ]
Kochins, J. G. [ > > ]
Manly, S. P. [ > > ]
Stoll, I. [ > > ]
El Fahime, E. M. [ > > ]
Noël, Agnès mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biologie cellulaire et moléculaire appliquée à l'homme >]
Foidart, Jean-Michel mailto [Université de Liège - ULg > Département des sciences cliniques > Gynécologie - Obstétrique - Labo de biologie des tumeurs et du développement >]
Dive, v [ > > ]
Basset, P. [ > > ]
Protein Expression & Purification
Academic Press
Yes (verified by ORBi)
[en] α-1 proteinase inhibitor ; cephalosporin ; matrix metalloproteinase inhibitors ; stromelysin-3
[en] 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-2, 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 avoidingin vitroactivation. 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 α-1 proteinase inhibitor. One ST3 inhibitor belonging to the cephalosporin family of antibiotics was thereby identified.

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