نتایج جستجو برای: fadd

تعداد نتایج: 1166  

Journal: :Circulation research 2003
Friedemann J Schaub W Conrad Liles Nicola Ferri Kirsten Sayson Ronald A Seifert Daniel F Bowen-Pope

We previously reported that treatment of human vascular smooth muscle cells (SMCs) with proapoptotic stimuli, including Fas ligand plus cycloheximide (FasL/Chx), or overexpression of Fas-associated death domain protein (FADD) result in increased expression of monocyte chemoattractant protein-1 (MCP-1) and other proinflammatory genes. In this study, we demonstrate that Fas/FADD-induced MCP-1 upr...

Journal: :Journal of bacteriology 2009
Aisling R Hume Jasmina Nikodinovic-Runic Kevin E O'Connor

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 K(m) values for aromatic substrates than for the aliphatic equivalents (e.g., 15-phenylpentadecanoic...

Journal: :The Journal of Experimental Medicine 1998
Jung-Hua Yeh Shu-Ching Hsu Shou-Hwa Han Ming-Zong Lai

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-acti...

Journal: :Journal of immunology 2003
Daniel R Beisner Isaac H Chu Adrian F Arechiga Stephen M Hedrick Craig M Walsh

Fas-associated death domain (FADD) is a death domain containing cytoplasmic adapter molecule required for the induction of apoptosis by death receptors. Paradoxically, FADD also plays a crucial role in the development and proliferation of T cells. Using T cells from mice expressing a dominant negative form of FADD (FADDdd), activation with anti-TCR Ab and costimulation or exogenous cytokines is...

Journal: :Blood 2005
Marc Pellegrini Sue Bath Vanessa S Marsden David C S Huang Donald Metcalf Alan W Harris Andreas Strasser

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 usin...

2016
Huei-Tzu Chien Sou-De Cheng Wen-Yu Chuang Chun-Ta Liao Hung-Ming Wang Shiang-Fu Huang

Amplification of 11q13.3 is a frequent event in human cancers, including head and neck squamous cell carcinoma. This chromosome region contains several genes that are potentially cancer drivers, including FADD (Fas associated via death domain), an apoptotic effector that was previously identified as a novel oncogene in laryngeal/pharyngeal cancer. This study was designed to explore the role of ...

2016
Yingting Liu Hongen Cui Xianjie Huang Bo Zhu Shengwen Guan Wei Cheng Yueyang Lai Xiaoxin Zhang Zi-Chun Hua

Fas-associated protein with death domain (FADD), a classical adaptor protein mediating apoptotic stimuli-induced cell death, has been reported to engage in several non-apoptotic processes such as T cell and cardiac development and tumorigenesis. Recently, there are several reports about the FADD's involvement in cell migration, however the underlying mechanism remains elusive. Here, we present ...

Journal: :Molecular cancer therapeutics 2007
Tomoki Takashina Manabu Nakayama

The ability to enhance apoptosis-inducing activity in specific cells, despite the presence of cellular antiapoptotic proteins, would allow the removal of target cells from a cell population. Here, we show that modification of Fas-associated protein with death domain (FADD) by fusing the tandem death effector domains (DED) of FADD to the E protein of lambda phage, a head coat protein with self-a...

Journal: :Carcinogenesis 2004
Keiji Shimada Syuichi Matsuyoshi Mitsutoshi Nakamura Eiwa Ishida Munehiro Kishi Noboru Konishi

FADD has been shown to be phosphorylated at Ser194 at the G2/M transition of the cell cycle. Here we have investigated the contribution of this phosphorylation to apoptosis induced by anticancer drugs in two human prostate cancer cell lines, LNCaP and DU145. Both were arrested at G2/M and FADD was found to be phosphorylated at Ser194 on treatment with paclitaxel. Inhibition of paclitaxel-induce...

Journal: :The Journal of biological chemistry 2004
Jorge M Caviglia Lei O Li Shuli Wang Concetta C DiRusso Rosalind A Coleman Tal M Lewin

Long chain fatty acids are converted to acyl-CoAs by acyl-CoA synthetase (fatty acid CoA ligase: AMP forming, E.C. 6.2.1.3; ACS). Escherichia coli has a single ACS, FadD, that is essential for growth when fatty acids are the sole carbon and energy source. Rodents have five ACS isoforms that differ in substrate specificity, tissue expression, and subcellular localization and are believed to chan...

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