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Nanotechnology-Mediated Strategy for the Treatment of Neuropathic Pain
Published in Cherry Bhargava, Amit Sachdeva, Nanotechnology, 2020
Pankaj Prashar, Ankita Sood, Anamika Gautam, Pardeep Kumar Sharma, Bimlesh Kumar, Indu Melkani, Sakshi Panchal, Sachin Kumar Singh, Monica Gulati, Narendra Kumar Pandey, Linu Dash, Anupriya, Varimadugu Bhanukirankumar Reddy
In many pathological conditions, including glucose deficiency, calcium exhaustion, free radical exposure, and the buildup of unfolded proteins, the normal working of ER has been impaired, inducing ER stress, which severely inhibits the protein folding cycle. Cells respond to stress by molecular chaperone expression like immunoglobulin protein binding, which starts a defensive mechanism known as unfold protein response (UPR). Immunoglobulin protein binding activation is used as a UPR initiation marker (Kong et al. 2020; Khangura et al. 2017). Three ER stress receptors facilitate the UPR: ER kinase PKR-like (PERK), the enzyme inositol requirement (IRE1), and the active transcription-factor (ATF6). Studies indicate that ER stress response is also a significant reaction, involving neuroinflammation, in inflammatory diseases (Sunderhaus, Law, and Kretzschmar 2019). The signaling process among ER stress and neuroinflammatory reaction is related by various mechanisms, such as reactive oxygen species, mitogen-activated protein kinase (MAPK), nuclear factor-kB, and calcium. The pro-inflammatory agents cause ER stress reaction, which in turn leads to induction of NP (Khangura et al. 2019).
Using chemical chaperones to increase recombinant human erythropoietin secretion in CHO cell line
Published in Preparative Biochemistry and Biotechnology, 2019
Mehri Mortazavi, Mohammad Ali Shokrgozar, Soroush Sardari, Kayhan Azadmanesh, Reza Mahdian, Hooman Kaghazian, Seyed Nezamedin Hosseini, Mohammad Hossein Hedayati
Endoplasmic reticulum is the prominent site of membrane and secretory protein folding. Protein folding is caused by molecular chaperones in ER such as glucose regulated protein 78/immunoglobulin binding protein (GRP78/BiP), X-box binding protein 1 (XBP1), activating transcription factor 4 (ATF4), and activating transcription factor 6 (ATF6).[1] Throughout protein synthesis by ribosomal residues on ER, a quality control process and post-translational modifications take place.[2–4] Recombinant protein overexpression in transfected cell lines usually results in protein misfolding, ER stress, and protein aggregation,[5,6] leading to the unfolded protein response.[7] Molecular chaperones and protein folding enzymes in ER act to solve this problem and help the protein to find its folding.[8] ER stress is induced due to the overload of unfolded, misfolded, and mutate proteins that cannot pass the protein secretion pathway and are stopped in ER.[4] Unfolded protein response (UPR) occurs in case ER stress is sensed by molecular chaperones in ER such as IRE1, PERK, and ATF6. Then GRP is released to reduce protein misfolding, and, at that time, UPR is activated. XBP1 and ATF4 are two other molecular chaperones in ER which are involved in UPR pathway.[1,7]