Sieber_2006_Nat.Chem.Biol_2_274

Reference

Title : Proteomic profiling of metalloprotease activities with cocktails of active-site probes - Sieber_2006_Nat.Chem.Biol_2_274
Author(s) : Sieber SA , Niessen S , Hoover HS , Cravatt BF
Ref : Nat Chemical Biology , 2 :274 , 2006
Abstract :

Metalloproteases are a large, diverse class of enzymes involved in many physiological and disease processes. Metalloproteases are regulated by post-translational mechanisms that diminish the effectiveness of conventional genomic and proteomic methods for their functional characterization. Chemical probes directed at active sites offer a potential way to measure metalloprotease activities in biological systems; however, large variations in structure limit the scope of any single small-molecule probe aimed at profiling this enzyme class. Here, we address this problem by creating a library of metalloprotease-directed probes that show complementary target selectivity. These probes were applied as a 'cocktail' to proteomes and their labeling profiles were analyzed collectively using an advanced liquid chromatography-mass spectrometry platform. More than 20 metalloproteases were identified, including members from nearly all of the major branches of this enzyme class. These findings suggest that chemical proteomic methods can serve as a universal strategy to profile the activity of the metalloprotease superfamily in complex biological systems.

PubMedSearch : Sieber_2006_Nat.Chem.Biol_2_274
PubMedID: 16565715

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Citations formats

Sieber SA, Niessen S, Hoover HS, Cravatt BF (2006)
Proteomic profiling of metalloprotease activities with cocktails of active-site probes
Nat Chemical Biology 2 :274

Sieber SA, Niessen S, Hoover HS, Cravatt BF (2006)
Nat Chemical Biology 2 :274