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Recent Advances of Nanotechnologies for Cancer Immunotherapy Treatment
Published in Loutfy H. Madkour, Nanoparticle-Based Drug Delivery in Cancer Treatment, 2022
Besides the TDLN, nanoparticles are also designed to target different types of immune cells, among which the DC is the most targeted cell because of its prominent role in antigen processing and presentation. The DC target is implemented by integrating ligands that combine with the membrane receptors on DCs, including the mannose, CD40, CD11c, DEC205, and DC-SIGN receptors. Studies found that the DC-targeted nanosystem could reinforce the endocytosis of DCs compared with the free form without nanoparticles [255–259]. Wang et al. conjugated mannose on the lipid–calcium–phosphate nanoparticles and found improved DC engulfment in the targeting-delivered group [260]. As a result, the co-encapsulated PD-L1 siRNA resulted in downregulation of PD-L1 in DCs that presented tumor antigens, further significantly prompted T-cell activation and proliferation, and exhibited profound inhibitory effects on tumor growth and metastasis. Similar results were reported in another study by Liu et al. [261]. In addition, targeting different molecules on the DC seemed to have different DC stimulation efficacy.
Clinical Management of Pancreatic Cancer
Published in Vittorio Cristini, Eugene J. Koay, Zhihui Wang, An Introduction to Physical Oncology, 2017
Programmed death-1 (PD-1) and programmed death ligand-1 (PD-L1) serve as key regulators of the immune response, called checkpoints. Activated T-cells express PD-1, while cancer cells and the associated stroma express PD-L1 and PD-L2. Upon binding of PD-1 to one of these ligands, T cells inactivate and undergo apoptosis, allowing tumor immune escape [285,286]. Clinical trials with monoclonal antibodies targeting PD-L1 or PD-1 have shown promising results in several tumors, such as renal cell carcinoma, melanoma, and non-small-cell lung cancer [287]. Although PD-L1 expression has been associated with poor prognosis in PDAC, targeting PD-L1 in PDAC has not shown significant response [286].
Anti-Cancer and Anti-Angiogenic Properties of Nano-Diamino-Tetrac, A Thyroid Hormone Derivative
Published in Shaker A. Mousa, Raj Bawa, Gerald F. Audette, The Road from Nanomedicine to Precision Medicine, 2020
Paul J. Davis, Shaker A. Mousa
There is substantial current interest in the programmed death-1 (PD-1)/PD-ligand 1 (PD-L1) checkpoint that regulates T cell-cancer cell interactions [95, 96] and defends cancer cells against immune destruction. Produced by cancer cells, PD-L1 binds to PD-1 expressed by T lymphocytes, suppressing activated T cell engagement of tumor cells and also inducing T cell apoptosis. Antibodies to PD-L1 have been shown to have clinical anti-cancer activity in subpopulations of cancer patients [95, 97], but also have induced undesirable autoimmune responses in previously healthy organs.
Production of codon-optimized Human papillomavirus type 52 L1 virus-like particles in Pichia pastoris BG10 expression system
Published in Preparative Biochemistry & Biotechnology, 2023
Kartika Sari Dewi, Sheila Chairunnisa, Sri Swasthikawati, Dian Fitria Agustiyanti, Apon Zainal Mustopa, Wien Kusharyoto, Ratih Asmana Ningrum
Confirmation of L1 protein expression was done using western blot analysis. Rabbit anti-HPV52 L1 antibody was used to detect L1 expression. Our result exhibited that L1 protein was successfully expressed in the P. pastoris expression system (Figure 7a,b). This result was strengthened by TEM analysis that showed the VLP formation in the intracellular fraction of the Pichia transformant (Figure 8). However, the analysis revealed many L1 proteins are still in the pentameric form (looks like a white circle with a much smaller size in the background). It means that the expression condition should be optimized to improve the VLP formation, including incubation temperature, OD600 of induction, inducer concentration, time of incubation and medium additives. Nevertheless, we concluded that P. pastoris expression system is suitable for HPV52 L1 VLP protein production.