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Journal articles on the topic 'FADD'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 December 2024

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1

Peng, Zhenying, Jian Ruan, Haiying Tian та ін. "The Family of Peanut Fatty Acid Desaturase Genes and a Functional Analysis of Four ω-3 AhFAD3 Members". Plant Molecular Biology Reporter 38, № 2 (2020): 209–21. http://dx.doi.org/10.1007/s11105-019-01191-0.

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AbstractThe synthesis of α-linolenic acid (ALA) requires the activity of ω-3 fatty acid desaturases (ω-3 FADs). The quality of peanut oil would be much improved if the content of ALA could be increased. A scan of the peanut genome revealed that it harbored 36 FAD genes, mapping to 16 of the species’ 20 chromosomes. A phylogenetic analysis concluded that these genes belonged to six sub-families, namely stearoyl-acyl-acyl carrier protein desaturases (SAD), FAD2, FAD3, FAD4/5, FAD6 and FAD7/8. Of these, FAD3 and FAD7/8 encoded ω-3 FADs, while genes belonging to the other four sub-families encoded

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2

Nakayama, Manabu, Emiko Suzuki, and Tomoki Takashina. "Engineered FADD Induces Apoptosis via an Artificial Death-Inducing Signaling Complex (DISC)." International Journal of Biomedical Science 5, no. 3 (2009): 237–45. http://dx.doi.org/10.59566/ijbs.2009.5237.

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An engineered Fas-associated death domain protein (FADD), 2DEDplusE-made previously by fusing the tandem DEDs of FADD to the E protein of lambda phage-greatly enhances apoptosis-inducing activity in adherent cells in vitro. To investigate the mechanism of apoptosis-inducing activity of this engineered FADD, we compared the apoptosis-inducing activity of various other engineered FADDs. The tandem DED of 2DEDplusE contributed most to the enhancement of apoptosis, and the E protein contributed moderately. The engineered factor produced artificial death-inducing signaling complex (DISC)-like signa

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3

Lucas, Robin L., C. Phoebe Lostroh, Concetta C. DiRusso, Michael P. Spector, Barry L. Wanner, and Catherine A. Lee. "Multiple Factors Independently RegulatehilA and Invasion Gene Expression in Salmonella enterica Serovar Typhimurium." Journal of Bacteriology 182, no. 7 (2000): 1872–82. http://dx.doi.org/10.1128/jb.182.7.1872-1882.2000.

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HilA activates the expression of Salmonella entericaserovar Typhimurium invasion genes. To learn more about regulation ofhilA, we isolated Tn5 mutants exhibiting reduced hilA and/or invasion gene expression. In addition to expected mutations, we identified Tn5 insertions inpstS, fadD, flhD, flhC, and fliA. Analysis of the pstS mutant indicates that hilA and invasion genes are repressed by the response regulator PhoB in the absence of the Pst high-affinity inorganic phosphate uptake system. This system is required for negative control of the PhoR-PhoB two-component regulatory system, suggesting

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4

Zhande, Rachel, Shauna M. Dauphinee, James A. Thomas, Masahiro Yamamoto, Shizuo Akira, and Aly Karsan. "FADD Negatively Regulates Lipopolysaccharide Signaling by Impairing Interleukin-1 Receptor-Associated Kinase 1-MyD88 Interaction." Molecular and Cellular Biology 27, no. 21 (2007): 7394–404. http://dx.doi.org/10.1128/mcb.00600-07.

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ABSTRACT Lipopolysaccharide (LPS) engages Toll-like receptor 4 (TLR4) on various cells to initiate inflammatory and angiogenic pathways. FADD is an adaptor protein involved in death receptor-mediated apoptosis. Here we report a role for FADD in regulation of TLR4 signals in endothelial cells. FADD specifically attenuates LPS-induced activation of c-Jun NH2-terminal kinase and phosphatidylinositol 3′-kinase in a death domain-dependent manner. In contrast, FADD-null cells show hyperactivation of these kinases. Examining physical associations of endogenous proteins, we show that FADD interacts wi

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5

Perez, Denise, and Eileen White. "E1B 19K Inhibits Fas-mediated Apoptosis through FADD-dependent Sequestration of FLICE." Journal of Cell Biology 141, no. 5 (1998): 1255–66. http://dx.doi.org/10.1083/jcb.141.5.1255.

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E1B 19K, the adenovirus Bcl-2 homologue, is a potent inhibitor of apoptosis induced by various stimuli including Fas and tumor necrosis factor-α. Fas and TNFR-1 belong to a family of cytokine-activated receptors that share key components in their signaling pathways, Fas-associating protein with death domain (FADD) and FADD-like interleukin-1β–converting enzyme (FLICE), to induce an apoptotic response. We demonstrate here that E1B 19K and Bcl-xL are able to inhibit apoptosis induced by FADD, but not FLICE. Surprisingly, apoptosis was abrogated by E1B 19K and Bcl-xL when FADD and FLICE were coex

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6

Zhang, Jianke. "Complementary functions of FADD and RIP1 critical for embryogenesis and T cell proliferation (50.8)." Journal of Immunology 186, no. 1_Supplement (2011): 50.8. http://dx.doi.org/10.4049/jimmunol.186.supp.50.8.

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Abstract FADD is a common adaptor shared by several death-receptors (DRs) for signaling apoptosis through recruitment and activation of caspase 8. DRs are essential for immune homeostasis, but dispensable during embryogenesis. Surprisingly, FADD-/- mice die in utero and conditional deletion of FADD leads to impaired lymphocyte proliferation. How FADD regulates embryogenesis and lymphocyte responses has been a long standing enigma. FADD could directly bind to RIP1, a serine/threonine kinase which mediates both necrosis and NF-kB activation. Our data indicate that FADD plays a role in regulating

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7

YOO, Jae-Ho, Oscar H. CHENG, and Gerhard E. GERBER. "Determination of the native form of FadD, the Escherichia coli fatty acyl-CoA synthetase, and characterization of limited proteolysis by outer membrane protease OmpT." Biochemical Journal 360, no. 3 (2001): 699–706. http://dx.doi.org/10.1042/bj3600699.

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Several studies have described FadD, the Escherichia coli fatty acyl-CoA synthetase [also known as fatty acid:CoA ligase (AMP-forming); EC 6.2.1.3], as a 42–50kDa enzyme. Based on sequencing and expression data from the fadD gene, other reports have suggested that FadD is a 62kDa protein and represents the sole fatty acyl-CoA synthetase in E. coli. We report that the 62kDa FadD enzyme is a substrate for the outer membrane protease OmpT in vitro, producing a 43kDa C-terminal fragment and a 19kDa N-terminal fragment. Immunoblotting with a FadD antibody revealed that only the 62kDa form of the en

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8

Ranjan, Kishu, Bhargav N. Waghela, Foram U. Vaidya, and Chandramani Pathak. "Cell-Penetrable Peptide-Conjugated FADD Induces Apoptosis and Regulates Inflammatory Signaling in Cancer Cells." International Journal of Molecular Sciences 21, no. 18 (2020): 6890. http://dx.doi.org/10.3390/ijms21186890.

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Dysregulated expression of Fas-associated death domain (FADD) is associated with the impediment of various cellular pathways, including apoptosis and inflammation. The adequate cytosolic expression of FADD is critical to the regulation of cancer cell proliferation. Importantly, cancer cells devise mechanisms to suppress FADD expression and, in turn, escape from apoptosis signaling. Formulating strategies, for direct delivery of FADD proteins into cancer cells in a controlled manner, may represent a promising therapeutic approach in cancer therapy. We chemically conjugated purified FADD protein

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9

Serrano, Alicia, Judith García-Martín, Martín Moret, José Manuel Martínez-Rivas, and Francisco Luque. "Transcriptomic Analysis During Olive Fruit Development and Expression Profiling of Fatty Acid Desaturase Genes." International Journal of Molecular Sciences 25, no. 20 (2024): 11150. http://dx.doi.org/10.3390/ijms252011150.

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The olive fruit is a drupe whose development and ripening takes several months from flowering to full maturation. During this period, several biochemical and physiological changes occur that affect the skin color, texture, composition, and size of the mesocarp. The final result is a fruit rich in fatty acids, phenolic compounds, tocopherols, pigments, sterols, terpenoids, and other compounds of nutritional interest. In this work, a transcriptomic analysis was performed using flowers (T0) and mesocarp tissue at seven different stages during olive fruit development and ripening (T1–T7) of the ‘P

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10

Zhang, Jianke, and Stephen Rosenberg. "An essential function of FADD in hematopoietic stem cells and progenitors (36.10)." Journal of Immunology 184, no. 1_Supplement (2010): 36.10. http://dx.doi.org/10.4049/jimmunol.184.supp.36.10.

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Abstract Signal transduction mediated by FADD represents a paradigm of co-regulation of both apoptosis and proliferation. Death receptors signal through FADD to activate the downstream caspase 8, and are required for homeostasis in the immune system, yet dispensable during embryonic development. In contrast, a FADD deficiency results in embryonic lethality. In previous studies, a lack of FADD in embryonic stem cells led to severe defects in lymphocyte development. However, conditional deletion of FADD following lymphoid lineage commitment still allows for the generation of T and B cell compart

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11

Chao, Wei, Yan Shen, Ling Li та ін. "Fas-associated death-domain protein inhibits TNF-α mediated NF-κB activation in cardiomyocytes". American Journal of Physiology-Heart and Circulatory Physiology 289, № 5 (2005): H2073—H2080. http://dx.doi.org/10.1152/ajpheart.01216.2004.

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Fas-associated death-domain protein (FADD) is an adaptor molecule that links death receptors to caspase-8 in many cell types including cardiomyocytes (CMs). Although FADD has previously been reported to play an important role in CM apoptosis, the effect of FADD on CM NF-κB signaling, which is a proinflammatory pathway, has not been delineated. To investigate the role of FADD in CM NF-κB activation, we utilized adenoviral gene transfer of wild-type FADD and a truncation mutant that lacks the death-effector domain (FADD-DED) in rat CMs in vitro TNF-α activated NF-κB in CMs as demonstrated by pho

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12

Zhang, Jianke, Hongxia Imtiyaz, and Stephen Rosenberg. "Novel aspects of the FADD function in lymphocytes revealed using hypomorphic FADD mutant and conditinal FADD-deficient mice (84.4)." Journal of Immunology 178, no. 1_Supplement (2007): S116. http://dx.doi.org/10.4049/jimmunol.178.supp.84.4.

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Abstract FADD was initially isolated as a death domain-containing protein interacting with the death receptor Fas. In the context of apoptotic signal transduction, the death domain of FADD interacts directly with the death domain of Fas and the death effector domain of FADD interacts with the death effector domain of pro-caspase-8. This leads to activation of the apical caspase-8 and subsequently downstream caspases such as caspase-3, -6 and -7. Fas-induced apoptosis is essential for maintaining lymphoid homeostasis and suppressing autoimmunity. Mutations in the Fas gene result in massive accu

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13

Pech-Canul, Ángel de la Cruz, Geovanny Rivera-Hernández, Joaquina Nogales, Otto Geiger, María J. Soto, and Isabel M. López-Lara. "Role of Sinorhizobium meliloti and Escherichia coli Long-Chain Acyl-CoA Synthetase FadD in Long-Term Survival." Microorganisms 8, no. 4 (2020): 470. http://dx.doi.org/10.3390/microorganisms8040470.

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FadD is an acyl-coenzyme A (CoA) synthetase specific for long-chain fatty acids (LCFA). Strains mutated in fadD cannot produce acyl-CoA and thus cannot grow on exogenous LCFA as the sole carbon source. Mutants in the fadD (smc02162) of Sinorhizobium meliloti are unable to grow on oleate as the sole carbon source and present an increased surface motility and accumulation of free fatty acids at the entry of the stationary phase of growth. In this study, we found that constitutive expression of the closest FadD homologues of S. meliloti, encoded by sma0150 and smb20650, could not revert any of th

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14

Marín-Rubio, José L., Laura Vela-Martín, José Fernández-Piqueras, and María Villa-Morales. "FADD in Cancer: Mechanisms of Altered Expression and Function, and Clinical Implications." Cancers 11, no. 10 (2019): 1462. http://dx.doi.org/10.3390/cancers11101462.

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FADD was initially described as an adaptor molecule for death receptor-mediated apoptosis, but subsequently it has been implicated in nonapoptotic cellular processes such as proliferation and cell cycle control. During the last decade, FADD has been shown to play a pivotal role in most of the signalosome complexes, such as the necroptosome and the inflammasome. Interestingly, various mechanisms involved in regulating FADD functions have been identified, essentially posttranslational modifications and secretion. All these aspects have been thoroughly addressed in previous reviews. However, FADD

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15

Nuthalapati, Soniya, Ranjitha P.V.Sai, Radhika Rani Kalapala, Lourdu Sasi Rekha Lingisetty, Sirisha Mekala, and Parveen Mohammad Firdosia. "Design a Low Power and High Speed 130nm Fulladder using Exclusive-OR and Exclusive NOR Gates." International Journal of Innovative Technology and Exploring Engineering 10, no. 5 (2021): 81–86. http://dx.doi.org/10.35940/ijitee.e8659.0310521.

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This literature illustrates the high speed and low power Full Adder (FADD) designs. This study relates to the composited structure of FADD design composed in one unit. In this the EXCL-OR/EXCL-NOR designs are used to design the FADD. Mostly concentrates on high speed standard FADD structure by combining the EXCL-OR/EXCL-NOR design in single unit. We implemented two composite structures of FADD through the full swing EXCL-OR/EXCL-NOR designs. And the EXCL-OR/EXCL-NOR design is done through pass transistor logic (PTL) and the same design projected on the composited FADD design. Such that the del

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16

Tungteakkhun, Sandy S., Maria Filippova, Jonathan W. Neidigh, Nadja Fodor, and Penelope J. Duerksen-Hughes. "The Interaction between Human Papillomavirus Type 16 and FADD Is Mediated by a Novel E6 Binding Domain." Journal of Virology 82, no. 19 (2008): 9600–9614. http://dx.doi.org/10.1128/jvi.00538-08.

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ABSTRACT High-risk strains of human papillomavirus, such as types 16 and 18, have been etiologically linked to cervical cancer. Most cervical cancer tissues are positive for both the E6 and E7 oncoproteins, since it is their cooperation that results in successful transformation and immortalization of infected cells. We have reported that E6 binds to tumor necrosis factor receptor 1 and to Fas-associated death domain (FADD) and, in doing so, prevents E6-expressing cells from responding to apoptotic stimuli. The binding site of E6 to FADD localizes to the first 23 amino acids of FADD and has now

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17

Wang, Fang, Hongbo Weng, Michael J. Quon, et al. "Dominant negative FADD dissipates the proapoptotic signalosome of the unfolded protein response in diabetic embryopathy." American Journal of Physiology-Endocrinology and Metabolism 309, no. 10 (2015): E861—E873. http://dx.doi.org/10.1152/ajpendo.00215.2015.

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Endoplasmic reticulum (ER) stress and caspase 8-dependent apoptosis are two interlinked causal events in maternal diabetes-induced neural tube defects (NTDs). The inositol-requiring enzyme 1α (IRE1α) signalosome mediates the proapoptotic effect of ER stress. Diabetes increases tumor necrosis factor receptor type 1R-associated death domain (TRADD) expression. Here, we revealed two new unfolded protein response (UPR) regulators, TRADD and Fas-associated protein with death domain (FADD). TRADD interacted with both the IRE1α-TRAF2-ASK1 complex and FADD. In vivo overexpression of a FADD dominant ne

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18

Gurung, Prajwal, and Thirumala-Devi Kanneganti. "FADD and caspase-8 mediate priming and activation of the canonical and non-canonical Nlrp3 inflammasomes (INC5P.321)." Journal of Immunology 192, no. 1_Supplement (2014): 120.1. http://dx.doi.org/10.4049/jimmunol.192.supp.120.1.

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Abstract The Nlrp3 inflammasomes are essential for protection against several infections and autoimmune diseases. Despite the plethora of research focused on understanding the roles of NLRP3 in various disease settings, the mechanisms controlling its activation remain enigmatic. Herein, we show through genetic studies that FADD or caspase-8 is required for both transcriptional priming and posttranslational activation of the canonical and non-canonical Nlrp3 inflammasomes. FADD and caspase-8 were required for caspase-1 activation during canonical Nlrp3 inflammasome activation by both soluble (L

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Khan, Amjad P., Katrina A. Schinske, Shyam Nyati, Mahaveer S. Bhojani, Brian D. Ross, and Alnawaz Rehemtulla. "High-Throughput Molecular Imaging for the Identification of FADD Kinase Inhibitors." Journal of Biomolecular Screening 15, no. 9 (2010): 1063–70. http://dx.doi.org/10.1177/1087057110380570.

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Fas-associated protein with death domain (FADD) was originally reported as a proapoptotic adaptor molecule that mediates receptor-induced apoptosis. Recent studies have revealed a potential role of FADD in NF-κB activation, embryogenesis, and cell cycle regulation and proliferation. Overexpression of FADD and its phosphorylation have been associated with the transformed phenotype in many cancers and is therefore a potential target for therapeutic intervention. In an effort to delineate signaling events that lead to FADD phosphorylation and to identify novel compounds that impinge on this pathw

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Ramos-Miguel, Alfredo, Antonio Miralles та Jesús A. García-Sevilla. "Correlation of rat cortical Fas-associated death domain (FADD) protein phosphorylation with the severity of spontaneous morphine abstinence syndrome: role of α2-adrenoceptors and extracellular signal-regulated kinases". Journal of Psychopharmacology 25, № 12 (2010): 1691–702. http://dx.doi.org/10.1177/0269881110387842.

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Fas-associated death domain (FADD) phosphorylation was recently implicated in opiate-induced neuroplasticity. To further explore the role of FADD in the mechanisms of morphine-induced physical dependence, the regulation of cortical p-FADD (and their interactions with α2-adrenoceptors and other signalling pathways) was assessed during spontaneous opiate withdrawal (SW) in morphine-dependent rats (10–100 mg/kg for 6 days). The main results indicated that oligomeric p-FADD in the cerebral cortex mirrored the time course of morphine SW (12–96 h), which resulted in a striking correlation between p-

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Marín-Rubio, José Luis, Laura Vela-Martín, Jack Gudgeon, et al. "A Dual Role for FADD in Human Precursor T-Cell Neoplasms." International Journal of Molecular Sciences 23, no. 23 (2022): 15157. http://dx.doi.org/10.3390/ijms232315157.

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A reduction in FADD levels has been reported in precursor T-cell neoplasms and other tumor types. Such reduction would impact on the ability of tumor cells to undergo apoptosis and has been associated with poor clinical outcomes. However, FADD is also known to participate in non-apoptotic functions, but these mechanisms are not well-understood. Linking FADD expression to the severity of precursor T-cell neoplasms could indicate its use as a prognostic marker and may open new avenues for targeted therapeutic strategies. Using transcriptomic and clinical data from patients with precursor T-cell

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Kim, P. K., A. S. Dutra, S. C. Chandrasekharappa, and J. M. Puck. "Genomic structure and mapping of human FADD, an intracellular mediator of lymphocyte apoptosis." Journal of Immunology 157, no. 12 (1996): 5461–66. http://dx.doi.org/10.4049/jimmunol.157.12.5461.

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Abstract Fas-associated death domain protein (FADD)/MORT1 is a 23-kDa cytoplasmic protein containing a C-terminal death domain that interacts with the intracellular death domain of the Fas transmembrane receptor. Cross-linking of Fas mediates apoptosis in a variety of cells, primarily peripheral T lymphocytes, for which this pathway plays a major role in mature lymphocyte homeostasis. We report the characterization of the human FADD gene, which spans approximately 3.6 kb and contains two exons (286 and 341 bp) separated by a 2.0-kb intron. FADD was mapped to chromosome 11q13.3 by the independe

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Walsh, Craig Michael, Sabrina Leverrier, Bryan D. Bell, Adrian F. Arechiga, and Brian M. Weist. "A non-apoptotic FADD/caspase-8 dependent mechanism essential for T cell clonal expansion (87.48)." Journal of Immunology 178, no. 1_Supplement (2007): S137. http://dx.doi.org/10.4049/jimmunol.178.supp.87.48.

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Abstract FADD constitutes an essential component of TNF receptor-induced apoptotic signaling. Paradoxically, FADD has also been shown to be crucial for lymphocyte development and activation. Using mice expressing a T cell specific transgene encoding the death domain of FADD (FADDdd), we have found that FADD participates in T cell clonal expansion. Based on BrdU uptake assays, we have found that FADD signaling is required for transition between the late G1 and S-phase of cell cycle. The defective progression through cycle is marked by a defect in cyclin E expression and CDK2 activation. We have

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Yeh, Jung-Hua, Shu-Ching Hsu, Shou-Hwa Han, and Ming-Zong Lai. "Mitogen-activated Protein Kinase Kinase Antagonized Fas-associated Death Domain Protein–mediated Apoptosis by Induced FLICE-inhibitory Protein Expression." Journal of Experimental Medicine 188, no. 10 (1998): 1795–802. http://dx.doi.org/10.1084/jem.188.10.1795.

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Fas and Fas-associated death domain (FADD) play a critical role in the homeostasis of different cell types. The regulation of Fas and FADD-mediated cell death is pivotal to many physiological functions. The activation of T lymphocytes by concanavalin A (Con A) inhibited Fas-mediated cell death. We identified that among the several activation signals downstream of Con A stimulation, mitogen-activated protein (MAP) kinase kinase (MKK) was the major kinase pathway that antagonized Fas-triggered cell death. MKK1 suppressed FADD- but not caspase-3– induced apoptosis, indicating that antagonism occu

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Nandu, Suruchi, Neha Chandra, and Astar Winoto. "FAS-associated death domain and tripartite motif-containing protein 21 negatively regulate virus-induced interferon production (P6126)." Journal of Immunology 190, no. 1_Supplement (2013): 128.14. http://dx.doi.org/10.4049/jimmunol.190.supp.128.14.

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Abstract While induction of type I Interferon (IFN) during the host antiviral response is imperative for efficient viral clearance, regulation of this response is crucial for immune system homeostasis. We have reported that FADD, a well characterized apoptotic protein, is involved in negatively regulating RNA virus-induced IFN-α production through a novel interaction with the E3 ubiquitin ligase, Tripartite Motif-Containing Protein 21 (TRIM21). Interaction between FADD and TRIM21 cooperatively represses IFN-α activation in Sendai virus infected cells. This occurs through TRIM21 targeted ubiqui

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Dowling, John P., and Jianke Zhang. "Distinct functions of RIP1 in immune homeostasis revealed using novel animal models." Journal of Immunology 196, no. 1_Supplement (2016): 204.7. http://dx.doi.org/10.4049/jimmunol.196.supp.204.7.

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Abstract RIP1 was originally identified as a protein associated with Fas and TNFR1, which can trigger apoptosis. However, initial studies indicated that RIP1 is dispensable for apoptotic signaling. Instead, cells lacking RIP1 are defective in TNFR1-induced activation of NF-kB, a critical player involved in pro-survival signaling. Recent studies indicate that a certain form of necrosis-like death, necroptosis, requires RIP1. In contrast, the Fas-associated death domain (FADD) protein appears to play an obligatory role in apoptosis induced by Fas and TNFR1. However, the embryonic lethality pheno

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Pech-Canul, Ángel, Joaquina Nogales, Alfonso Miranda-Molina, et al. "FadD Is Required for Utilization of Endogenous Fatty Acids Released from Membrane Lipids." Journal of Bacteriology 193, no. 22 (2011): 6295–304. http://dx.doi.org/10.1128/jb.05450-11.

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FadD is an acyl coenzyme A (CoA) synthetase responsible for the activation of exogenous long-chain fatty acids (LCFA) into acyl-CoAs. Mutation offadDin the symbiotic nitrogen-fixing bacteriumSinorhizobium melilotipromotes swarming motility and leads to defects in nodulation of alfalfa plants. In this study, we found thatS. melilotifadDmutants accumulated a mixture of free fatty acids during the stationary phase of growth. The composition of the free fatty acid pool and the results obtained after specific labeling of esterified fatty acids with a Δ5-desaturase (Δ5-Des) were in agreement with me

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González-Moles, Miguel Ángel, Ángela Ayén, Isábel González-Ruiz, et al. "Prognostic and Clinicopathological Significance of FADD Upregulation in Head and Neck Squamous Cell Carcinoma: A Systematic Review and Meta-Analysis." Cancers 12, no. 9 (2020): 2393. http://dx.doi.org/10.3390/cancers12092393.

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Fas-associated death domain (FADD) upregulation, i.e., gene amplification, protein phosphorylation and/or overexpression, has shown promising prognostic implications in head and neck squamous cell carcinoma (HNSCC). This systematic review and meta-analysis aims to evaluate the clinicopathological and prognostic significance of FADD upregulation in HNSCC. We searched studies published before February 2020 through PubMed, Embase, Web of Science, Scopus and Google Scholar. We evaluated the quality of the studies included using the QUIPS tool. The impact of FADD upregulation on survival and clinic

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Rasamny, Jk J., Amir Allak, Kaelyn A. Krook, et al. "Cyclin D1 and FADD as Biomarkers in Head and Neck Squamous Cell Carcinoma." Otolaryngology–Head and Neck Surgery 146, no. 6 (2012): 923–31. http://dx.doi.org/10.1177/0194599811435052.

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Objective. Cyclin D1 and FADD (Fas-associated protein with death domain) regulate the cell cycle and apoptosis, respectively, and are located on chromosome 11q13, which is frequently amplified in head and neck squamous cell carcinoma (HNSCC). This study evaluates these proteins as predictors of clinical outcomes for HNSCC. Study Design. Historical cohort study. Setting. Academic tertiary care center. Subjects. Two hundred twenty-two patients with upper aerodigestive HNSCC. Results. Patients with tumors that were strongly positive for cyclin D1 and FADD had reduced overall (OS; P = .003 and P &

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Zhang, Jing, Dapeng Zhang, and Zichun Hua. "FADD and its Phosphorylation." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 56, no. 7 (2004): 395–401. http://dx.doi.org/10.1080/15216540400008929.

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García-Fuster, M. Julia, and Jesús A. García-Sevilla. "Effects of anti-depressant treatments on FADD and p-FADD protein in rat brain cortex: enhanced anti-apoptotic p-FADD/FADD ratio after chronic desipramine and fluoxetine administration." Psychopharmacology 233, no. 15-16 (2016): 2955–71. http://dx.doi.org/10.1007/s00213-016-4342-6.

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Leverrier, Sabrina, Brian M. Weist, and Craig M. Walsh. "NON-APOPTOTIC INDUCTION OF CASPASE-8 IN T-CELLS DEPENDS ON FADD AND CELL CYCLE PROGRESSION (87.1)." Journal of Immunology 178, no. 1_Supplement (2007): S127. http://dx.doi.org/10.4049/jimmunol.178.supp.87.1.

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Abstract Upon triggering of apoptosis by tumor necrosis factor (TNF) receptor family member engagement, FADD (Fas-Associated Death Domain-containing protein) acts as an adaptor protein by recruiting caspase-8 and promoting its autocatalytic activation. Surprisingly, it was found that FADD and caspase-8 are also critical for T lymphocytes proliferation. Indeed, T cell specific overexpression of a FADD dominant-negative mutant (FADDdd) or conditional deletion of caspase-8 or FADD in T cells leads to profound defects in proliferation. While it is known that FADD transmits an apoptotic signal by r

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Oh, Jiyoung, and James Malter. "Pin1 attenuates Fas-mediated apoptosis through binding to FADD in activated eosinophils. (57.1)." Journal of Immunology 188, no. 1_Supplement (2012): 57.1. http://dx.doi.org/10.4049/jimmunol.188.supp.57.1.

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Abstract Pin1 is widely expressed peptidyl-prolyl isomerase (PPIase) that plays a key role in a variety of events including cell cycle progression, response to viruses, expression of cytokines and cell death. Eosinophils (Eos) rely on Pin1 to mediate prosurvival signaling induced by IL-5 or GM-CSF by binding to and inhibiting pro-apoptotic Bax. Here we show Pin1 also participates in Fas-mediated apoptosis of Eos. Fas activation suppressed Pin1 activity despite co-treatment with IL-5. This was accompanied by phosphorylation of Pin1 at Ser16 and increased nuclear, rather than plasma membrane loc

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Lu, Jiahuan, Anthony Wing Hung Chan, Ka Fai To та Jingying Zhou. "Turning immunologically cold tumors into hot ones by activating hepatoma-intrinsic FADD/NF-κB/CCL5 pathway". Journal of Immunology 208, № 1_Supplement (2022): 178.09. http://dx.doi.org/10.4049/jimmunol.208.supp.178.09.

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Abstract Lymphoepithelioma-like hepatocellular carcinoma (LEL-HCC) is a distinct variant of HCC that displayed immunologically hot tumor features with prominent tumor-infiltrating CD8+ T lymphocytes (TILs). Our whole exosome sequencing data pointed out an increased prevalence of chromosome 11q13.3 amplification in LEL-HCC, in which 13/17 genes located in 11q13.3 were upregulated. Among these genes, fas-associated death domain (FADD) displayed a strongest correlation with differentially upregulated immune regulatory genes in HCC with 11q13.3 amplicon. In addition, CD8+ T cells preferred to migr

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Kabra, Nisha H., Dragana Cado, and Astar Winoto. "A Tailless Fas-FADD Death-Effector Domain Chimera Is Sufficient to Execute Fas Function in T Cells But Not B Cells of MRL-lpr/lpr Mice." Journal of Immunology 162, no. 5 (1999): 2766–74. http://dx.doi.org/10.4049/jimmunol.162.5.2766.

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Abstract The Fas receptor delivers signals crucial for lymphocyte apoptosis through its cytoplasmic death domain. Several Fas cytoplasmic-associated proteins have been reported and studied in cell lines. So far, only Fas-associated death domain protein (FADD), another death domain-containing molecule has been shown to be essential for Fas signals in vivo. FADD is thought to function by recruiting caspase-8 through its death-effector domain. To test whether FADD is sufficient to deliver Fas signals, we generated transgenic mice expressing a chimera comprised of the Fas extracellular domain and

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Ranjan, Kishu, and Chandramani Pathak. "Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation." International Journal of Molecular Sciences 25, no. 6 (2024): 3228. http://dx.doi.org/10.3390/ijms25063228.

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Fas-associated death domain (FADD) is an adaptor protein that predominantly transduces the apoptosis signal from the death receptor (DR) to activate caspases, leading to the initiation of apoptotic signaling and the coordinated removal of damaged, infected, or unwanted cells. In addition to its apoptotic functions, FADD is involved in signaling pathways related to autophagy, cell proliferation, necroptosis, and cellular senescence, indicating its versatile role in cell survival and proliferation. The subcellular localization and intracellular expression of FADD play a crucial role in determini

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Alqahtani, Abdullah, Shtwai Alsubai, Mohemmed Sha, Veselý Peter, Ahmad S. Almadhor, and Sidra Abbas. "Falling and Drowning Detection Framework Using Smartphone Sensors." Computational Intelligence and Neuroscience 2022 (August 12, 2022): 1–12. http://dx.doi.org/10.1155/2022/6468870.

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Advancements in health monitoring using smartphone sensor technologies have made it possible to quantify the functional performance and deviations in an individual’s routine. Falling and drowning are significant unnatural causes of silent accidental deaths, which require an ambient approach to be detected. This paper presents the novel ambient assistive framework Falling and Drowning Detection (FaDD) for falling and drowning detection. FaDD perceives input from smartphone sensors, such as accelerometer, gyroscope, magnetometer, and GPS, that provide accurate readings of the movement of an indi

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Patel, Suketu, Derek Murphy, Eugenia Haralambieva, et al. "Increased Expression of Phosphorylated FADD in Anaplastic Large Cell and Other T-Cell Lymphomas." Biomarker Insights 9 (January 2014): BMI.S16553. http://dx.doi.org/10.4137/bmi.s16553.

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FAS-associated protein with death domain (FADD) is a major adaptor protein involved in extrinsic apoptosis, embryogenesis, and lymphocyte homeostasis. Although abnormalities of the FADD/death receptor apoptotic pathways have been established in tumorigenesis, fewer studies have analyzed the expression and role of phosphorylated FADD (pFADD). Our identification of FADD as a lymphoma-associated autoantigen in T-cell lymphoma patients raises the possibility that pFADD, with its correlation with cell cycle, may possess role(s) in human T-cell lymphoma development. This immunohistochemical study in

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Pellegrini, Marc, Sue Bath, Vanessa S. Marsden, et al. "FADD and caspase-8 are required for cytokine-induced proliferation of hemopoietic progenitor cells." Blood 106, no. 5 (2005): 1581–89. http://dx.doi.org/10.1182/blood-2005-01-0284.

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Abstract The role of caspase-8 and its adaptor Fas-associated death domain (FADD) in lymphocyte apoptosis is well defined, but their functions in other hemopoietic lineages are not clear. We were unable to generate transgenic mice expressing dominant inhibitors of FADD or caspase-8 in hemopoietic cells, possibly because their expression may have precluded production of vital hemopoietic cells. When using a retroviral gene delivery system, fetal liver stem cells expressing a dominant-negative mutant of FADD (FADD-DN) were unable to generate myeloid or lymphoid cells upon transplantation into le

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Thorburn, Jacqueline, Laura M. Bender, Michael J. Morgan, and Andrew Thorburn. "Caspase- and Serine Protease-dependent Apoptosis by the Death Domain of FADD in Normal Epithelial Cells." Molecular Biology of the Cell 14, no. 1 (2003): 67–77. http://dx.doi.org/10.1091/mbc.e02-04-0207.

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The adapter protein FADD consists of two protein interaction domains: a death domain and a death effector domain. The death domain binds to activated death receptors such as Fas, whereas the death effector domain binds to procaspase 8. An FADD mutant, which consists of only the death domain (FADD-DD), inhibits death receptor–induced apoptosis. FADD-DD can also activate a mechanistically distinct, cell type–specific apoptotic pathway that kills normal but not cancerous prostate epithelial cells. Here, we show that this apoptosis occurs through activation of caspases 9, 3, 6, and 7 and a serine

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Marín-Rubio, José L., Eduardo Pérez-Gómez, José Fernández-Piqueras, and María Villa-Morales. "S194-P-FADD as a marker of aggressiveness and poor prognosis in human T-cell lymphoblastic lymphoma." Carcinogenesis 40, no. 10 (2019): 1260–68. http://dx.doi.org/10.1093/carcin/bgz041.

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AbstractT-cell lymphoblastic lymphoma is a haematological disease with an urgent need for reliable prognostic biomarkers that allow therapeutic stratification and dose adjustment. The scarcity of human samples is responsible for the delayed progress in the study and the clinical management of this disease, especially compared with T-cell acute lymphoblastic leukaemia, its leukemic counterpart. In the present work, we have determined by immunohistochemistry that S194-P-FADD protein is significantly reduced in a cohort of 22 samples from human T-cell lymphoblastic lymphoma. Notably, the extent o

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Zhang, Haibing, and Jianke Zhang. "Novel functions of cFLIP in lymphocyte death signaling (163.22)." Journal of Immunology 188, no. 1_Supplement (2012): 163.22. http://dx.doi.org/10.4049/jimmunol.188.supp.163.22.

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Abstract Fas/Apo-1 signals through the FADD (Fas-associated death domain) adaptor protein, which recruits and activates the apical caspase 8 and leads to apoptosis. cFLIP is a homologue of caspase 8 but lacks caspase activities, and presumably inhibits apoptosis induced by the death receptors by competing with caspase 8 for binding to FADD. FADD, Caspase 8, and cFLIP form a signaling complex during death receptor-induced apoptosis. In addition to the cell death function, deletion of FADD, Caspase 8, and cFLIP results in embryonic lethality and lymphocytes proliferation defects upon TCR-induced

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Matsuda, Naoyuki, Hiroki Teramae, Seiji Yamamoto, Ken-ichi Takano, Yasuo Takano, and Yuichi Hattori. "Increased death receptor pathway of apoptotic signaling in septic mouse aorta: effect of systemic delivery of FADD siRNA." American Journal of Physiology-Heart and Circulatory Physiology 298, no. 1 (2010): H92—H101. http://dx.doi.org/10.1152/ajpheart.00069.2009.

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Recent evidence suggests that apoptotic cell death plays an important role in the pathophysiology of sepsis. Because there is extensive apoptosis of vascular endothelial cells in sepsis, we examined whether the death receptor pathway of apoptotic signaling is altered in thoracic aortas from mice with polymicrobial sepsis, as produced by cecal ligation and puncture (CLP). In septic aorta, total and surface expression levels of the two death receptors tumor necrosis factor receptor 1 and Fas were highly upregulated. Furthermore, marked increases in the mRNA and protein levels of Fas-associated d

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Zhou, Jingying, and Jiahuan Lu. "Abstract 5545: FADD activation renders hepatocellular carcinoma sensitive to immune checkpoint blockade by turning cold tumors hot." Cancer Research 84, no. 6_Supplement (2024): 5545. http://dx.doi.org/10.1158/1538-7445.am2024-5545.

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Abstract The heterogenicity of hepatocellular carcinoma (HCC) remains a key obstacle in turning the majority of ‘immune-cold’ tumors ‘hot’ for effective immune checkpoint blockade (ICB) therapy. Through studying the naturally-existed ‘hot’ HCC variant lymphoepithelioma-like (LEL)-HCC by RNA and whole exome sequencing analysis, we identified fas-associated death domain (FADD) as one of the top differentially expressed genes that associated with high tumoral CD8+T cell abundance. Of note, FADD upregulation was also observed in HCC patients with better ICB responsiveness. As FADD was mainly expre

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Hume, Aisling R., Jasmina Nikodinovic-Runic, and Kevin E. O'Connor. "FadD from Pseudomonas putida CA-3 Is a True Long-Chain Fatty Acyl Coenzyme A Synthetase That Activates Phenylalkanoic and Alkanoic Acids." Journal of Bacteriology 191, no. 24 (2009): 7554–65. http://dx.doi.org/10.1128/jb.01016-09.

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ABSTRACT A fatty acyl coenzyme A synthetase (FadD) from Pseudomonas putida CA-3 is capable of activating a wide range of phenylalkanoic and alkanoic acids. It exhibits the highest rates of reaction and catalytic efficiency with long-chain aromatic and aliphatic substrates. FadD exhibits higher k cat and Km values for aromatic substrates than for the aliphatic equivalents (e.g., 15-phenylpentadecanoic acid versus pentadecanoic acid). FadD is inhibited noncompetitively by both acrylic acid and 2-bromooctanoic acid. The deletion of the fadD gene from P. putida CA-3 resulted in no detectable growt

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Frisch, S. "Nuclear localization of FADD protein." Cell Death & Differentiation 11, no. 12 (2004): 1361–62. http://dx.doi.org/10.1038/sj.cdd.4401512.

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O'Reilly, L., S. Crawford, D. C. S. Huang, and A. Strasser. "Nuclear localisation of FADD – rebuttal." Cell Death & Differentiation 11, no. 12 (2004): 1362–63. http://dx.doi.org/10.1038/sj.cdd.4401513.

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Sheikh, M. Saeed, and Ying Huang. "The FADD is Going Nuclear." Cell Cycle 2, no. 4 (2003): 343–44. http://dx.doi.org/10.4161/cc.2.4.421.

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Kabra, N. H., C. Kang, L. C. Hsing, J. Zhang, and A. Winoto. "T cell-specific FADD-deficient mice: FADD is required for early T cell development." Proceedings of the National Academy of Sciences 98, no. 11 (2001): 6307–12. http://dx.doi.org/10.1073/pnas.111158698.

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Salort, G., M. Álvaro-Bartolomé, and J. A. García-Sevilla. "Pentobarbital-induced sleep upregulates the survival p-FADD/FADD ratio in mouse brain cortex." European Neuropsychopharmacology 29 (2019): S541—S542. http://dx.doi.org/10.1016/j.euroneuro.2018.11.800.

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