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Microsporidians (Encephalitozoon cuniculi)
Published in Eric S. Loker, Bruce V. Hofkin, Parasitology, 2015
Eric S. Loker, Bruce V. Hofkin
Treatment Various benzimidazole-type drugs are suggested as treatments, including the anthelmintics albendazole, oxibendazole, and fenbendazole. Some studies suggest that there is enhanced efficacy when one of these drugs is administered in combination with enrofloxacin (Baytril®), a bacteriocidal drug commonly used in veterinary medicine.
Spotlight on ocular Kaposi’s sarcoma: an update on the presentation, diagnosis, and management options
Published in Expert Review of Ophthalmology, 2021
Nandini Venkateswaran, Juan C. Ramos, Adam K. Cohen, Osmel P. Alvarez, Noah K. Cohen, Anat Galor, Carol L. Karp
New anti-viral therapies may be on the horizon and could be explored for the treatment of KS; however, their efficacies against latent HHV8 infection could be limited theoretically. As mentioned previously, multiple compounds have been recently identified through an FDA-approved drug library that effectively inhibit HHV8 virion production [17]. Three of the identified compounds exhibited inhibitory effects on histamine receptors and blockage of histamine receptors by antagonists can inhibit HHV8 virion lytic replication. Other agents identified in this database such as monobenzone (an agent used for vitiligo treatment), oxibendazole (an agent used for intestinal helminth infections), oxaliplatin (a chemotherapy drug for colon and rectal cancers), and hycanthone (topoisomerase II inhibitor) all inhibit HHV8 lytic reactivation. Identified compounds targeting neurotransmitters, such as dopamine, adrenergic, serotonin, and muscarinic receptors, also exhibit a potential role in the regulation of HHV8 reactivation [17]. These new therapies targeting HHV8 are summarized in Table 2.
In vitro inhibition of the hepatic S-oxygenation of the anthelmintic albendazole by the natural monoterpene thymol in sheep
Published in Xenobiotica, 2020
Victoria Miró, Adrian Lifschitz, Paula Viviani, Carolina Rocha, Carlos Lanusse, Livio Costa, Guillermo Virkel
Reference standards (99% pure) of ABZ, albendazole sulfoxide (ABZSO), albendazole sulfone (ABZSO2) and oxibendazole (OBZ) were provided by Sigma-Aldrich Argentina. Stock solutions (5, 0.5, and 0.25 mM) of each BZD molecule were prepared in methanol (Baker Inc., Phillipsburg, USA). Benzydamine, benzydamine N-oxide, ethoxyresorufin, and resorufin were from Sigma-Aldrich Argentina. Nicotinamide adenine dinucleotide phosphate (NADP+), glucose-6-phosphate and glucose-6-phosphate dehydrogenase were from Roche and provided by Merck Argentina. Thymol (98.5% pure) was from Sigma-Aldrich Argentina. Buffer salts (KCl, NaCl, NaHCO3, Na2HPO4, NaH2PO4, K2HPO4, KH2PO4 and CH3COONH4, MgCl2, KH2PO4) and HPLC solvents (methanol and acetonitrile) were obtained from J.T Baker-Avantor (USA).
Epigenetic anticancer agents cause HMGB1 release in vivo
Published in OncoImmunology, 2018
Peng Liu, Liwei Zhao, Friedemann Loos, Kristina Iribarren, Oliver Kepp, Guido Kroemer
Based on these considerations, we decided to design a screen that would allow to accurately determine the nuclear release of HMGB1 induced by anticancer agents.6 For this, we used the “retention using selective hooks” (RUSH) system, in which a streptavidin-binding peptide (SBP) fused with HMGB1 and green fluorescent protein (GFP) was sequestered by streptavidin-NLS3 fusion protein in the nucleus. In cells expressing both the HMGB1-SBP-GFP fusion protein and the streptavidin-NLS3 hook, the GFP-dependent fluorescent signal is strictly confined to the nucleus, in punctiform structures. Upon addition of biotin, which competitively disrupts the interaction between HMGB1-SBP-GFP and streptavidin-NLS3, HMGB1-SBP-GFP remains in the nucleus, yet changes from a punctiform to a diffuse distribution. However, it is only after addition of ICD inducers such as anthracyclines, digoxigen, doxorubicin and mitoxantrone that HMGB1-SBP-GFP redistributed from the nucleus to the cytoplasm. (Fig. 1)6 This system then was used to identify HGMB1 releasing agents among approximately 2000 drugs and drug candidates. In the top list of agents causing nuclear HMGB1 release, we found several epigenetic modifiers (azacitidine, decitabine and suberoylanilide hydroxamic acid, SAHA), microtubule inhibitors (docetaxel, paclitaxel and nocodazole) as well as several anthelmintic agents (albendazole, fenbendazole, flubendazole, mebendazole, oxibendazole) that all are known to inhibit microtubule formation.6 Importantly, we could subsequently validate that intraperitoneal injection of azacitidine, decitabine and SAHA as well as that of anthelmintics induced the appearance of circulating HMGB1 in the plasma from mice. Thus, pharmacologically meaningful concentrations of these drugs stimulate the cellular release of HMGB1.