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        Assays for Proteasome Inhibition

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        The ubiquitin-proteasome pathway has an essential role in the regulation of numerous cellular proteins, including those mediating inflammatory conditions and cancer (1 6 ). Intracellular proteins destined for proteolysis are first tagged with polyubiquitin chains through a cascade of enzyme-catalyzed events. These ‘marked’ proteins are then degraded via the 26S proteasome in an ATP-dependent manner (7 ). The 26S proteasome (EC 3.4.99.46) is a large, multisubunit enzyme (MW=2000 kDa) found in high concentration in all mammalian cells. The ATP hydrolytic activity and the specific subunits that bind ubiquitin in the 26S are located within a protein complex known as the 19S subunit which caps either end of the 20S core. The ATP-independent proteolytic activity of the proteasome is contained within this central 20S core (MW=730 kDa), a multicatalytic protease that has three well characterized peptidase activities. The three peptidases: chymotryptic, tryptic, and postglutamyl peptide hydrolytic activities, are associated with three distinct subunits: β5 , β2 , and β1 , respectively (8 ). Each site is defined by its ability to hydrolyze peptide substrates in vitro, with hydrophobic, basic or acidic amino acids in the P1 position.
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