panobinostat and benzyloxycarbonylleucyl-leucyl-leucine-aldehyde

panobinostat has been researched along with benzyloxycarbonylleucyl-leucyl-leucine-aldehyde* in 2 studies

Other Studies

2 other study(ies) available for panobinostat and benzyloxycarbonylleucyl-leucyl-leucine-aldehyde

ArticleYear
The effect of acetylation on the protein stability of BmApoLp-III in the silkworm, Bombyx mori.
    Insect molecular biology, 2020, Volume: 29, Issue:1

    Acetylation is an important, reversible posttranslational modification to a protein. In a previous study, we found that there were a large number of acetylated sites in various nutrient storage proteins of the silkworm haemolymph. In this study, we confirmed that acetylation can affect the stability of nutrient storage protein Bombyx mori apolipophorin-III (BmApoLp-III). First, the expression of BmApoLp-III could be upregulated when BmN cells were treated with the deacetylase inhibitor panobinostat (LBH589); similarly, the expression was downregulated when the cells were treated with the acetylase inhibitor C646. Furthermore, the increase in acetylation by LBH589 could inhibit the degradation and improve the accumulation of BmApoLp-III in BmN cells treated with cycloheximide and MG132 respectively. Moreover, we found that an increase in acetylation could decrease the ubiquitination of BmApoLp-III and vice versa; therefore, we predicted that acetylation could improve the stability of BmApoLp-III by competing for ubiquitination and inhibiting the protein degradation pathway mediated by ubiquitin. Additionally, BmApoLp-III had an antiapoptosis function that increased after LBH589 treatment, which might have been due to the improved protein stability after acetylation. These results have laid the foundation for further study on the mechanism of acetylation in regulating the storage and utilization of silkworm nutrition.

    Topics: Acetylation; Animals; Apolipoproteins; Benzoates; Bombyx; Cell Line; Cycloheximide; Insect Proteins; Leupeptins; Nitrobenzenes; Panobinostat; Protein Stability; Pyrazoles; Pyrazolones

2020
A histone deacetylase inhibitor LBH589 downregulates XIAP in mesothelioma cell lines which is likely responsible for increased apoptosis with TRAIL.
    Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer, 2009, Volume: 4, Issue:2

    Tumor necrosis factor-alpha-related apoptosis-inducing ligand (TRAIL) is a member of tumor necrosis factor family and it is important for ligand induced apoptosis in tumor cells. TRAIL has been shown to be synergistic with a variety of chemotherapies and targeted agents. In the study, a combination of TRAIL and a histone deacetylase inhibitor LBH589 was studied in mesothelioma cell lines.. Five mesothelioma cell lines and two normal cell lines were tested for cell growth inhibition and apoptosis using high-throughput assays in the presence of LBH589, TRAIL and a combination of the two. Caspase induction was studied and levels of X-linked inhibitor of apoptosis (XIAP) were tested using Western blotting. A combination of a direct inhibitor of XIAP was also tested in combination with TRAIL.. In mesothelioma cell lines, a combination of LBH589 and TRAIL markedly increased cell growth inhibition and apoptosis when compared with the effect on normal cell lines. LBH589 and TRAIL appeared to induce higher levels of caspase 3 and 7 and this appeared to be closely related to ability of LBH589 to degrade XIAP. In addition, a direct inhibitor of XIAP was also sensitized cells to TRAIL apoptosis, providing an indirect confirmation for XIAP degradation as a possible mechanism of synergy.. In mesothelioma cell lines, LBH589 increases the sensitivity to TRAIL. In addition, at least partly, the mechanism of this induction of TRAIL sensitivity is due to LBH589 related degradation of XIAP. These results provide initial evidence for testing this combination in clinical trials.

    Topics: Acetylation; Apoptosis; BH3 Interacting Domain Death Agonist Protein; Caspases; Cysteine Proteinase Inhibitors; Enzyme Activation; Enzyme Inhibitors; Enzyme-Linked Immunosorbent Assay; Histone Deacetylase Inhibitors; Histones; Humans; Hydroxamic Acids; Immunoblotting; Indoles; Leupeptins; Mesothelioma; Panobinostat; Poly(ADP-ribose) Polymerases; TNF-Related Apoptosis-Inducing Ligand; Tumor Cells, Cultured; X-Linked Inhibitor of Apoptosis Protein

2009
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