Journal
CHEMISTRY & BIOLOGY
Volume 14, Issue 4, Pages 419-430Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2007.03.008
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Funding
- NCI NIH HHS [R01 CA131059-01A1, R01 CA131059-03, R01 CA131059-02, R01 CA131059] Funding Source: Medline
- NEI NIH HHS [R01 EY016782] Funding Source: Medline
- NINDS NIH HHS [R21 NS053593-01S2, R21 NS053593-01, R21 NS053593-01S1, R21 NS053593] Funding Source: Medline
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The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class 1 antigen presentation. However, its other pathophysiological functions are still not very well understood. This can be attributed mainly to a lack of appropriate molecular probes that can selectively modulate the immunoproteasome catalytic subunits. Herein, we report the development of molecular probes that selectively inhibit the major catalytic subunit, LIVIP2, of the immunoproteasome. We show that these compounds irreversibly modify the LMP2 subunit with high specificity. Importantly, LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LIVIP2 in regulating cell growth of malignant tumors that highly express LMP2.
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