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The Role of Nanoparticles in Cancer Therapy through Apoptosis Induction
Published in Hala Gali-Muhtasib, Racha Chouaib, Nanoparticle Drug Delivery Systems for Cancer Treatment, 2020
Marveh Rahmati, Saeid Amanpour, Hadiseh Mohammadpour
Upon interaction of FasL with Fas receptor (Apo-1 or CD95), the death-inducing signaling complex (DISC), which contains adaptor proteins such as FADD and procaspase-8, is formed. In some cell types, activated CASP-8 directly activates other members of the caspase family and subsequently leads to the execution of apoptosis. In other types of cells, the induction of Fas pathway is not sufficient to trigger an apoptotic response, rather this pathway cross-talk with mitochondrial pathway through proteolytic degradation of Bid producing a truncated form of Bid (tBid). Then, tBid acts through a heterodimer with BAX or BAK, leading to the activation of the mitochondrial pathway of apoptosis. In this situation, the extrinsic pathway functions as an amplifier to induce an apoptotic response [35].
Pulsed Electric Fields in Biological Cells and Membranes
Published in James C. Lin, Electromagnetic Fields in Biological Systems, 2016
The basic mechanism underlying a majority of these methods and field induced biophenomena is the induction of a potential difference across the membrane by the external electric field. The seat of the electric field–driven bioresponses tends to be membranes because these sheaths represent nonconducting barriers that can easily be charged by external voltage pulsing. Consequently, large electric fields can be created across membranes that can then drive a host of bioeffects. The membranes are crucial not only because high electric fields can be created in these regions but also because important biological processes (e.g., irreversible apoptosis) are launched from these sites. For example, the extrinsic apoptotic pathway (Green 2000; Peter and Krammer 2003) involves the clustering of molecules such as the tumor necrosis factor-related apoptosis-inducing ligand (TRAIL), Fas-associated protein with death domain (FADD), and procaspase-8 leading to the formation of the death-inducing production. This in turn sets into motion a series of biochemical reactions that eventually lead to apoptosis (Song, Joshi, and Beebe 2010; Bagci et al. 2006; Budihardjo et al. 1999; Li, P. et al. 1997). The other apoptosis route (known as the intrinsic pathway) involves cytochrome c release from another membrane—the mitochondria, which is an intracellular organelle (Zoratti and Szabo 1995; Marzo et al. 1998).
Cell Biology for Bioprocessing
Published in Wei-Shou Hu, Cell Culture Bioprocess Engineering, 2020
Cells subject to developmentally regulated apoptosis express death receptors, such as the Fas death receptor, on their surface. The binding of an external Fas ligand to the death receptor recruits an adaptor molecule, Fas-associated death domain (FADD), to the cytoplasmic end of the receptor. The presence of FADD causes pro-caspase 8 or 9 to associate with the death receptor, forming a death-inducing signaling complex (DISC). The caspase is then proteolytically activated, triggering the activation of a series of downstream effector caspases (3, 6, and 7). The activation of these effector caspases leads to the final stages of cell destruction.
Hesperetin upregulates Fas/FasL expression and potentiates the antitumor effect of 5-fluorouracil in rat model of hepatocellular carcinoma
Published in Egyptian Journal of Basic and Applied Sciences, 2020
Merna G. Aboismaiel, Mohamed El-Mesery, Amro El-Karef, Mamdouh M. El-Shishtawy
Fas (CD95/APO-1) is a type-I trans-membrane protein that belongs to tumor necrosis factor (TNF) receptor superfamily [9]. The extrinsic apoptotic pathway can be initiated through interaction of Fas ligand (FasL) with its corresponding death receptor, Fas. This results in recruitment of the adaptor molecule Fas-associated death domain (FADD) to form a death inducing signaling complex (DISC) with procaspase-8. Cleavage of procaspase-8 results in activation of caspase-8, which mediates activation of downstream caspases and subsequent induction of apoptosis [10]. On the contrary, apoptosis can be suppressed via increased expression of B cell lymphoma-2 (Bcl-2) antiapoptotic proteins causing cancer cells to develop insensitivity toward chemotherapy and thus progression of cancer [11].