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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].
Mechanisms of Nanotoxicity to Cells, Animals, and Humans
Published in Vineet Kumar, Nandita Dasgupta, Shivendu Ranjan, Nanotoxicology, 2018
Belinda Wong Shu Ee, Puja Khanna, Ng Cheng Teng, Baeg Gyeong Hun
The extrinsic pathway, also known as the death receptor pathway, involves transmembrane receptor-mediated interactions. The name is derived from the role of death receptors, which are a part of the TNF receptor gene superfamily in this pathway. The cytoplasmic death domain is made up of around 80 amino acid residues and plays a critical role in transmitting death signals from cellular surface to intracellular signaling pathways. A few of the ligands that are best characterized in this pathway along with their receptors are FasL/FasR and TNF-α/TNFR1 (Elmore 2007). Fas ligand (FasL) binds to Fas receptor (FasR) which leads to the interaction of adaptor protein Fas-associated death domain protein (FADD) with procaspase-8. Thus, the death-inducing signaling complex (DISC) composed of FasR, FADD, and procaspase-8 is formed (Wajant 2002). Similarly, TNF-α binds to TNF receptor 1 (TNFR1) which promotes the binding of adaptor protein TNFR1-associated death domain protein (TRADD) to the death domain of TNFR1 (Hsu et al. 1995). Procaspase-8 is cleaved into its active form caspase-8 and sets the execution pathway in motion (Elmore 2007).
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].
Chlorogenic acid potentiates antitumor effect of doxorubicin through upregulation of death receptors in solid Ehrlich carcinoma model in mice
Published in Egyptian Journal of Basic and Applied Sciences, 2019
Nesma A. Abd Elrazik, Mohamed El-Mesery, Amro El-Karef, Laila A. Eissa, Amal M El Gayar
Apoptosis is an essential programmed cell death pathway which is regulated by many factors including the death receptors and Bcl-2 family members. Death receptors are members of tumor necrosis factor (TNF) receptor superfamily including Fas and TNF-related apoptosis-inducing ligand receptor (TRAIL-R) 1 and TRAIL-2. Activation of these receptors by their corresponding ligands results in the formation of death-inducing signaling complex that induces caspase activation and induction of apoptosis cascade [15–17].