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Pulmonary reactions to novel chemotherapeutic agents and biomolecules
Published in Philippe Camus, Edward C Rosenow, Drug-induced and Iatrogenic Respiratory Disease, 2010
The FDA recently approved the first proteasome inhibitor, bortezomib, for the treatment of multiple myeloma and mantle-cell lymphoma. Early studies did not suggest any lung toxicity, but a report in 2006 from Miyakoshi and colleagues described severe pulmonary complications in 4 of 13 Japanese patients treated for multiple myeloma.151 The clinical presentation was characterized by asthma-like symptoms and fever, followed by respiratory failure with pulmonary infiltrates. In three of the patients, respiratory failure developed after repeated administration of bortezomib, and corticosteroids resulted in improvement; one of those three still ultimately died of respiratory failure, and autopsy showed diffuse alveolar damage. The fourth patient developed pulmonary complications immediately after the first dose of bortezomib, showed no improvement after corticosteroids, and died of respiratory failure.
Enzyme Kinetics and Drugs as Enzyme Inhibitors
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Although the proteasome is thus an essential component of cellular metabolism, drugs targeting this pathway—e.g., to prevent its upregulation in case of the above mentioned skeletal muscle atrophy—have been developed. The proteasome is also an important therapeutic target in cancer therapy (for a review of computational approaches for the discovery of human proteasome inhibitors see Guedes et al., 2016) because cancer cells such as myeloma cells produce a large amount of paraprotein. An example is bortezomib (opposite scheme) a proteasome inhibitor employed to treat patients with multiple myeloma, lymphoma, chronic lymphocytic leukemia, head and neck cancer, and prostate cancer (Mitchell, 2003). Bortezomib is a dipeptidyl boronic acid derivative (contains pyrazinoic acid, phenylalanine and leucine with boronic acid in its structure), approved by the FDA in 2003. It acts by reversibly targeting an active-site N-terminal threonine residue in the β5 subunit of the proteasome, and proteasome activity returns about 72 h after administration. Bortezomib-mediated proteasome inhibition blocks cell division and induces apoptosis via caspases. Furthermore, the inhibition acts on cancer cells by changes in regulator proteins controlling the cell cycle regulation and the activation of nuclear factor κ-B (NF-κB). NF-κB must be activated for a variety of important steps in the tumorigenic process such as angiogenesis, cell proliferation, and metastasis; for more details see Chen et al., 2011.
The emergence of nanoporous materials in lung cancer therapy
Published in Science and Technology of Advanced Materials, 2022
Deepika Radhakrishnan, Shan Mohanan, Goeun Choi, Jin-Ho Choy, Steffi Tiburcius, Hoang Trung Trinh, Shankar Bolan, Nikki Verrills, Pradeep Tanwar, Ajay Karakoti, Ajayan Vinu
Bortezomib (BTZ) is a clinically approved proteasome inhibitor for different cancer treatments. The main drawback of this medication is the reduced solubility similar to cisplatin. BTZ loaded MSNs modified and hybridized with histone H2A peptide showed better drug delivery in lung cancer cells. Histone H2A is a chimeric peptide that can overcome targeting obstacles in drug delivery. On comparing these two studies, the MSN modified with targeting agent is more specific with better efficacy [197]. Similarly, van Rijt et al. reported the MSNs capped with avidin (a tetrameric biotin binding protein) and functionalised with matrix metalloproteinase inhibitor 9 (MMP9) linkers. The linkers are peptide sequences which can be cleaved by overexpressed MMP9 in the cancer cells. The drugs, BTZ and cisplatin were loaded separately, and the efficiency of MSN as a delivery agent was compared. It was found that in lung cancer cell line A549 and H1299, both the drugs were released only in MMP9 expressed cell lines [198].
Enhancing laccase production by white-rot fungus trametes hirsuta SSM-3 in co-culture with yeast sporidiobolus pararoseus SSM-8
Published in Preparative Biochemistry & Biotechnology, 2020
Jianfen Zhang, Wei Ke, Hong Chen
The starch of PCB medium could be hydrolyzed to reducing sugar by amylase in monoculture, and then the hydrolyzates were consumed by T. hirsuta SSM-3. When the yeast was seeded to the flasks, it would consume reducing sugar for the proliferation. However, when two strains were cultured, the relationships of competition were established and a decrease of amylase was observed. In this study, enhanced production of laccase was detected with quick decrease of amylase activity. We can deduced that in PCB medium, the addition of the yeast leads to quick demand of glucose due to the growth of the yeast and forms a competition environment to T. hirsuta, it inhibited T. hirsuta cell to produce amylase, and stimulates it to overproduce laccase. It was reported that competition for resources among co-cultured microbes was natural[12]. Crowe et al. reported that fungal laccases could be involved in physiological processes as a virulence factor in interactions with other organisms[31]. Staszczak et al.[32] has reported that addition of proteasome inhibitor can increase laccase activity of T. versicolor. Thus, it deduced that the fungal laccase was considered to be a virulence factor in interactions with yeast in this study. The interactions between different microorganism play a critical role in co-cultures because cell growth by one species could enhance or inhibit the enzyme activities of the other strain present in the medium[5,17].