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Order Tubulavirales
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
Przystal et al. (2019) introduced an intravenous phage vector for dual targeting of therapeutic genes to glioblastoma, in the form of a hybrid with adeno-associated virus (AAV), described in Chapter 9, designed to deliver a recombinant AAV genome by the capsid of the phage M13. The dual tumor targeting by this vector was first achieved by phage capsid display of the RGD4C ligand that bound the αvβ3 integrin receptor. Second, the genes were expressed from a tumor-activated and temozolomide (TMZ)-induced promoter of the glucose-regulated protein. The combination of TMZ and RGD4C/AAV-Grp78 targeted gene therapy exerted as a result a synergistic effect to suppress growth of orthotopic glioblastoma (Przystal et al. 2019).
Exploration of Nanonutraceuticals in Neurodegenerative Diseases
Published in Raj K. Keservani, Anil K. Sharma, Rajesh K. Kesharwani, Nutraceuticals and Dietary Supplements, 2020
Swati Pund, Amita Joshi, Vandana Patravale
Gaballah et al. (2016) showed potential use of resveratrol as a neuroprotective therapeutic agent in in a rat model of rotenone-induced PD. Resveratrol improved endoplasmic reticulum stress by downregulating C/EBP homologous protein and glucose-regulated protein 78 genes expression and hampered caspase-3 activity in the brain. It also activated glutathione peroxidase and Nrf2 signaling pathway and suppressed xanthine oxidase activity and protein carbonyls formation; thus restoring redox balance. Resveratrol induces heme oxygenase-1-dependent autophagy and prevents dopaminergic cell death by regulating autophagic flux (Lin et al., 2014).
Alteration in Cell Cycle Control Factors and the Induction of Oxygen-Regulated Proteins by Hypoxic Stress
Published in John J. Lemasters, Constance Oliver, Cell Biology of Trauma, 2020
Harold C. Smith, Robert L. Howell, John W. Ludlow
In terms of gene induction during ischemia, the most extensively studied scenario is the induction of glucose- and oxygen-regulated stress proteins within cells of solid tumor hypoxic microenvironments.5 Ischemic stress results in downregulation of DNA, RNA, and protein synthesis.6–11 Despite this generalized inhibition of macromolecular synthesis, induction of two glucose-regulated proteins (GRP 97 and 78) and five oxygen-regulated proteins (ORP 260, 150, 100, 80, and 33) has been demonstrated in both proliferating and differentiated cells through metabolic protein radiolabeling during ischemic stress.7,10–14 Varying constitutive levels of all GRP/ORP can be detected in most cells. Induction of these proteins at the level of transcription and translation rates7,10,14 can be observed within 2 h following sublethal levels of hypoxia,5,7,10,11,14 and reaches maximum synthetic rates/abundance within 12 h of hypoxia.
GRP78-targeted and doxorubicin-loaded nanodroplets combined with ultrasound: a potential novel theranostics for castration-resistant prostate cancer
Published in Drug Delivery, 2022
Yading Zhao, Dandan Shi, Mengmeng Shang, Xiao Sun, Lu Guo, Dong Meng, Xinxin Liu, Xiaoying Zhou, Jie Li
Glucose-regulated protein 78 (GRP78) can regulate the unfolded protein response (UPR) process and is mainly in the endoplasmic reticulum (ER) (Lee, 2007). Under stress conditions, such as glucose deficiency or hypoxia, the accumulation of misfolded and underglycosylated proteins can induce the UPR, which allows GRP78 to translocate to the membrane of cancer cells (Lee, 2007; Zhang et al., 2010). GRP78 is, therefore, an effective target for cancer treatment (Lee, 2014). GRP78 is overexpressed on the PCa cell membrane, and the SP94 peptide can specifically bind to GRP78 (Pootrakul et al., 2006; Delie et al., 2013; Jiang et al., 2019). The SP94 peptide has outstanding advantages, such as small size, little immunogenicity, and economic synthesis (Schottelius & Wester, 2009); offers an ideal ligand for targeting CRPC; and binds to the target by connecting to ultrasonic NDs.
Effects of salubrinal on ER stress in an experimental model of polycystic ovary syndrome
Published in Ultrastructural Pathology, 2020
Asli Emincik, Zeynep Banu Gungor, Elif Guzel
The endoplasmic reticulum (ER) is a prominent perinuclear organelle for the synthesis and folding of secretory proteins and membrane proteins. Due to hypoxia, oxidative damage, variation in calcium homeostasis, viral infections, protein inclusion bodies, elevated synthesis of secretory proteins, failure in cellular energy and/or nutritional homeostasis, unfolded or misfolded proteins are accumulated in the ER, resulting in ER stress. As a result of ER stress, unfolded protein response (UPR) is induced to protect the cell.13,14 78-kDa glucose-regulated protein (GRP78) and the corresponding three transmembrane proteins participate in the regulation of UPR. These are protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK), inositol-requiring enzyme 1 (IRE1), and activating transcription factor 6 (ATF6).15 If ER stress cannot be reversed, cell goes through apoptosis.16
Research progress of nanocarriers for gene therapy targeting abnormal glucose and lipid metabolism in tumors
Published in Drug Delivery, 2021
Xianhu Zeng, Zhipeng Li, Chunrong Zhu, Lisa Xu, Yong Sun, Shangcong Han
GRP87 is a glucose-regulated protein that plays a key role in tumor cell survival, tumor progression, metastasis, and resistance to therapy. The upregulation of GRP87 expression is beneficial for the continuous adaptation of the endoplasmic reticulum (ER), which can improve glucose metabolism (Ni et al. 2011; Lu et al. 2020). The expression of GRP87 was silenced by siRNA technology, and the glucose metabolism of the body was decreased. The particles also effectively reversed multidrug resistance and inhibited tumor proliferation and metastasis (Gifford & Hill 2018). Of course, the inorganic material added will adsorb siRNA and produce drug-loading effects. Compared with the polymer, its toxicity is greatly reduced, and the biological compatibility is increased.