b-AP15 - CAS 1009817-63-3
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Not Intended for Therapeutic Use. For research use only.
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b-AP15 is a deubiquitinases inhibitor for 19S proteasomes activity of Ub-AMC cleavage with IC50 of 2.1 μM.Not a general deubiquitinase inhibitor. Has minimal inhibition on recombinant and cytosolic nonproteasomal cysteine deubiquitinases.
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1.Induction of tumor cell apoptosis by a proteasome deubiquitinase inhibitor is associated with oxidative stress.
Brnjic S1, Mazurkiewicz M, Fryknäs M, Sun C, Zhang X, Larsson R, D'Arcy P, Linder S. Antioxid Redox Signal. 2014 Dec 10;21(17):2271-85. doi: 10.1089/ars.2013.5322. Epub 2013 Oct 17.
AIMS: b-AP15 is a recently described inhibitor of the USP14/UCHL5 deubiquitinases (DUBs) of the 19S proteasome. Exposure to b-AP15 results in blocking of proteasome function and accumulation of polyubiquitinated protein substrates in cells. This novel mechanism of proteasome inhibition may potentially be exploited for cancer therapy, in particular for treatment of malignancies resistant to currently used proteasome inhibitors. The aim of the present study was to characterize the cellular response to b-AP15-mediated proteasome DUB inhibition.
2.Regulation of TRAIL-receptor expression by the ubiquitin-proteasome system.
Sarhan D1, D'Arcy P2, Lundqvist A3. Int J Mol Sci. 2014 Oct 14;15(10):18557-73. doi: 10.3390/ijms151018557.
The tumor necrosis factor (TNF)-related apoptosis-inducing ligand- receptor (TRAIL-R) family has emerged as a key mediator of cell fate and survival. Ligation of TRAIL ligand to TRAIL-R1 or TRAIL-R2 initiates the extrinsic apoptotic pathway characterized by the recruitment of death domains, assembly of the death-inducing signaling complex (DISC), caspase activation and ultimately apoptosis. Conversely the decoy receptors TRAIL-R3 and TRAIL-R4, which lack the pro-apoptotic death domain, function to dampen the apoptotic response by competing for TRAIL ligand. The tissue restricted expression of the decoy receptors on normal but not cancer cells provides a therapeutic rational for the development of selective TRAIL-mediated anti-tumor therapies. Recent clinical trials using agonistic antibodies against the apoptosis-inducing TRAIL receptors or recombinant TRAIL have been promising; however the number of patients in complete remission remains stubbornly low.
3.Deubiquitinases Modulate Platelet Proteome Ubiquitination, Aggregation, and Thrombosis.
Gupta N1, Li W1, McIntyre TM2. Arterioscler Thromb Vasc Biol. 2015 Dec;35(12):2657-66. doi: 10.1161/ATVBAHA.115.306054. Epub 2015 Oct 15.
OBJECTIVE: Platelets express a functional ubiquitin-proteasome system. Mass spectrometry shows that platelets contain several deubiquitinases, but whether these are functional, modulate the proteome, or affect platelet reactivity are unknown.
4.Simultaneous inhibition of deubiquitinating enzymes (DUBs) and autophagy synergistically kills breast cancer cells.
Vogel RI1, Coughlin K2, Scotti A3, Iizuka Y2, Anchoori R4,5, Roden RB4,5,6, Marastoni M3, Bazzaro M1,2. Oncotarget. 2015 Feb 28;6(6):4159-70.
Breast cancer is one of the leading causes of cancer death among women in the United States. Patients expressing the estrogen and progesterone receptor (ER and PR) and human epidermal growth factor 2 (HER-2) tumor markers have favorable prognosis and efficacious therapeutic options. In contrast, tumors that are negative for these markers (triple-negative) have a disproportionate share of morbidity and mortality due to lack of a validated molecular target. Deubiquitinating enzymes (DUBs) are a critical component of ubiquitin-proteasome-system degradation and have been shown to be differentially expressed and activated in a number of cancers, including breast, with their aberrant activity linked to cancer prognosis and clinical outcome. We evaluated the effect of the DUB inhibitors b-AP15 and RA-9 alone and in combination with early- and late-stage lysosomal inhibitors on cell viability in a panel of triple negative breast cancer (TNBC) cell lines.
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