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Anti-Arthritic Potential of Gold Nanoparticle
Published in Klaus D. Sattler, st Century Nanoscience – A Handbook, 2020
Jayeeta Sengupta, Sourav Ghosh, Antony Gomes
It is thought that the main risk factor for rheumatoid arthritis is the genetic factors. Antigen-presenting cells of the immune system possess major histocompatibility (MHC) antigens (class II) at the cell surface, encoded by a gene HLA-DR4. It is estimated that a conserved sequence in HLA-DR4 gene contributes around 30% of total genetic risks for rheumatoid arthritis. This conserved and specific sequence in HLA-DR4 gene causes a slight change in class II MHC antigens, leading to the activation of T lymphocytes. The other genetic risk factors contributing to the initiation of the pathogenesis of rheumatoid arthritis include peptidyl arginine deiminase-4, STAT4, PTNP22, and CTLA4. Peptidyl argi-nine deiminase-4 causes increased citrullination of peptides, which unfolds the peptide (change in 3D structure) due to the loss of positively charged arginine residues. It makes the self-protein an antigen, producing specific anti-citrullinated peptide antibodies (rheumatoid arthritis-specific autoantibody). A polymorphism in peptidyl argi-nine deiminase-4 gene causes increased citrullination of peptides. Anti-citrullinated peptide antibodies can be identified up to 12–15 years before the commencement of clinical symptoms of rheumatoid arthritis, indicating a preclinical period of the pathogenesis of the disease. STAT4, PTNP22, and CTLA4 are involved in the activation of tumor necrosis factor receptor and T-cell activation, leading to the initiation of rheumatoid arthritis pathogenesis.
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
PLGA immobilised with DOX and PTX has shown promising results in lung cancers with high intake efficiency [270,271]. Kim et al. designed highly porous micron-sized PLGA particles functionalised with a peptide TRAIL (tumour necrosis factor (TNF)-related apoptosis-inducing ligand) and labelled with fluorescein N-hydroxysuccinimide for the delivery of DOX. TRAIL is reported to have no toxicity because it specifically binds to the overexpressed receptors such as DR4/TRAIL-R1 and DR5/TRAIL-R2 in cancer cells, which are not present in normal cells. The mean loading efficiency of DOX and TRAIL in PLGA microparticles was 87 ± 7% and 92 ± 2%, respectively. The synergistic effects of TRAIL modified DOX loaded PLGA were analysed in both in vitro (H226-human lung squamous cells) and in vivo mouse models administered via the inhalation route. The DOX was gradually released and sustained in the cells up to 7 days. However, the TRAIL leached out within a day, and only a trace amount was retained by the seventh day. The toxicity of DOX and TRIAL were analysed in H226 lung squamous cell carcinoma and it was found that co-treating with DOX (~1 µg/ml) and TRIAL (~0.01 µg/ml) reduced the maximum inhibitory concentration (IC50) of DOX of 3 µg/ml with 0.01 µg/ml TRIAL concentration [68].
Carnosic acid exhibits antiproliferative and proapoptotic effects in tumoral NCI-H460 and nontumoral IMR-90 lung cells
Published in Journal of Toxicology and Environmental Health, Part A, 2020
Amanda Cristina Corveloni, Simone Cristine Semprebon, Adrivanio Baranoski, Bruna Isabela Biazi, Thalita Alves Zanetti, Mário Sérgio Mantovani
Both IMR-90 and NCI-H460 cells demonstrated cell death by apoptosis following exposure to CA. Su et al. (2016) noted that CA inhibited cervical cancer cell growth associated with apoptosis, concomitant with the release of cytochrome c, and upregulation of proapoptotic protein levels, such as Bcl-2, Bax, Bak, Bad, Apaf1, and cleaved caspase-9 and 3. Zhang et al. (2017) found that CA enhanced apoptosis and caspase-3, 8, and 9 activities in HepG2 SMMC-7721 cells. Taj et al. (2012) reported that incubation of human ovarian cancer A2780 cells with rosemary extract (RE) containing CA altered the expression of a number of genes regulating apoptosis. Shi et al. (2017) showed that CA induced apoptosis in HCC827 and H358 lung cancer cells with activation of mitochondrial pathway associated with the rise of cleaved caspase-9 and 3, upregulation of Bax and Bad, and downregulation of Bcl-2 and Bcl-xl. Further, cells also exhibited activation of the extrinsic pathway, with activation of caspase-8 and upregulation of TRAIL, DR4, DR5, and FADD mRNA levels.
Synthesis, characterization, and in vitro evaluation of TRAIL-modified, cabazitaxel -loaded polymeric micelles for achieving synergistic anticancer therapy
Published in Journal of Biomaterials Science, Polymer Edition, 2018
Caochuan Feng, Xiaoxiong Han, Lili Chi, Jing Sun, Feirong Gong, Yaling Shen
Because of the presence of DR4 and DR5 on the surface of MCF-7 cells [37], confocal microscopy was used to observe the uptake of TRAIL-modified micelles by MCF-7 cells. As shown in Figure 8, after 30 min of incubation at 37 °C with free DiO, almost no green fluorescence was observed (Figure 8 A), and most of the green fluorescence was distributed on the cell membrane, which is consistent with the results reported in the literature [38]. The green fluorescence of the other three formulations showed a granular appearance, and the fluorescence intensity of the TRAIL-modified DiO-loaded micelles was the strongest among all samples (Figure 8C), whereas the MCF-7 cells incubated with unmodified micelles had a weak intracellular fluorescence (Figure 8B). In addition, when cells were pretreated with the TRAIL protein, the green fluorescence was weaker than that in the non-pretreated cells after 30-min incubation with TRAIL-coupled micelles, which may be due to a decrease in the number of cell surface receptors after pretreatment with the TRAIL protein (Figure 8D). These results indicate that encapsulated DiO is internalized into the cytoplasm as a micellar solution. In addition, the TRAIL-modified micelles showed a significantly stronger fluorescence in the cytoplasm than the unmodified micelles did and stronger than that in the pretreated groups, indicating that the enhanced uptake and absorption of DiO by cells is due to the surface modification of micelles with the TRAIL protein.