China
Africa
Explore chapters and articles related to this topic
Peripheral muscles
Published in Claudio F. Donner, Nicolino Ambrosino, Roger S. Goldstein, Pulmonary Rehabilitation, 2020
Luis Puente-Maestu, François Maltais, André Nyberg, Didier Saey
Severe COPD patients, even with normal weight, exhibit increased levels of apoptosis in their quadriceps compared with control subjects (2,22). Some evidence suggests the possibility that excessive calcium accumulation in the cytoplasm, together with low energetic status during exercise and a permeability transition pore that, while less prone to form/open, may induce large mitochondrial swelling when opened, is a possible mechanism for increased apoptosis; however, low caspase 3 levels have been observed in the quadriceps of COPD (7). This is a puzzling observation, since caspase 3 is thought of as fundamental to both apoptosis induced by the death receptor pathway and stress (mitochondrial permeability transitory pore)-induced apoptosis. Thus a caspase-independent mechanism such as the mitochondrial apoptosis-inducing factor (AIF) might play a role (2,22).
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
There also exists a caspase-independent apoptotic pathway that is mediated by AIF (Apoptosis-Inducing Factor) [24]. AIF is phylogenetically an old flavoprotein observed in the mitochondrial intermembrane. Upon lethal stimuli, AIF translocates from mitochondria to the nucleus. It binds to DNA and mediates caspase-independent chromatin condensation and large scale DNA fragmentation [25, 26].
Cognition Enhancers
Published in Sahab Uddin, Rashid Mamunur, Advances in Neuropharmacology, 2020
Ramneek Kaur, Rashi Rajput, Sachin Kumar, Harleen Kaur, R. Rachana, Manisha Singh
If a neuron is stressed or injured, it might undergo apoptosis. It may be either extrinsic (which can be started by activating the receptors of cell surface) or intrinsic (involving the ER and the mitochondria). Cell death can be triggered by either of the losses of factors responsible for cell survival. Further, damage of DNA, which may thereby, cause the pro-apoptotic proteins from the mitochondria to stimulate caspase proteases and eventually, caspase activated DNase. Apoptosis can also be induced in caspase independent manner by triggering apoptosis-inducing factor (AIF) which is protein present in the intermembrane of the mitochondria. Attenuation of cell death can be triggered by stimulation of PKCγ in the hippocampus. Therefore, it is suggested that the activators of PKCγ inhibits apoptosis (Sun et al., 2009), thereby, increasing the usefulness as CE that can act on the patients specifically suffering from stroke, brain injury, and acute radiation sickness.
Anti-tumoral potential of a human granulysin-based, CEA-targeted cytolytic immunotoxin
Published in OncoImmunology, 2019
Raquel Ibáñez-Pérez, Patricia Guerrero-Ochoa, Sameer Al-Wasaby, Rocío Navarro, Antonio Tapia-Galisteo, Diego De Miguel, Oscar Gonzalo, Blanca Conde, Luis Martínez-Lostao, Ramón Hurtado-Guerrero, Laura Sanz, Alberto Anel
Histological studies on tissue sections obtained from resected tumors were also performed. As shown in the hematoxilin/eosin images (Figure 7a), untreated tumors from the control group or from the GRNLY-treated group presented the typical compact tissue structure of a fast-growing tumor. On the contrary, systemic injection of MFE23GRNLY caused a dramatic loss of cellularity in HeLa-CEA derived tumors (right panel of Figure 7a). Active caspase-3 immunochemistry gave some limited labeling in GRNLY-treated tumors (middle panel of Figure 7b), but this staining was much more extensive in the case of MFE23GRNLY-treated mice (right panel of Figure 7b). Upon DAPI labeling, untreated tumors or tumors treated by systemic GRNLY injection displayed nuclei with non-condensed chromatin (Figure 7c, left and middle panels, respectively). On the contrary, MFE23GRNLY-treated tumors showed less cellularity, condensed chromatin and fragmented nuclei (indicated with arrows in the right panel of Figure 7c). In addition, they also showed numerous cells with condensed chromatin concentrated in the nuclear margins (indicated with circles in the same image). This nuclear morphology is characteristic of apoptosis-inducing factor (AIF)-mediated cell death.10
Suppressor of TCR signaling-2 (STS-2) suppresses arthritis development in mice
Published in Modern Rheumatology, 2018
Namiko Okabe, Koichiro Ohmura, Masaki Katayama, Shuji Akizuki, Nick Carpino, Kosaku Murakami, Ran Nakashima, Motomu Hashimoto, Yoshitaka Imura, Hajime Yoshifuji, Masao Tanaka, Tsuneyo Mimori
Although STS-1 and STS-2 share the functions of suppressing T cell activation through TCR, only STS-2 was reported to bind AIF and promote caspase-independent apoptosis in vitro [15]. AIF is a flavoprotein that acts as NADH oxidase and regulates caspase-independent apoptosis [24–26]. AIF is located in inner mitochondrial membrane at steady state. Once AIF receives an apoptosis signal, it is released from mitochondria and moves into nucleus, then binds to DNA and induces aggregation and degradation of chromatin, resulting in apoptosis [27]. STS-2 is thought to promote interaction between released AIF and other co-factors in cytoplasm, and to promote apoptosis [15]. Our results of apoptosis analysis are compatible with the previous results that STS-2 promoted growth factor withdrawal cell death by enhancing AIF function.
Porphyromonas gingivalis degrades integrin β1 and induces AIF-mediated apoptosis of epithelial cells
Published in Infectious Diseases, 2019
Qian Li, Jie Zhou, Li Lin, Haijiao Zhao, Lei Miao, Yaping Pan
AIF, a ubiquitously expressed flavoprotein, is normally positioned in the mitochondrial intermembrane space. AIF could be released to the cytosol and nucleus to interact with DNA and/or RNA to initiate caspase-independent chromatinolysis in response to apoptosis stimuli [28]. We examined AIF to investigate caspase-independent apoptosis. Incubation of KB cells with P. gingivalis made AIF transfer to nucleus, suggesting that P. gingivalis infection activated the AIF proapoptotic activity. Moreover, when AIF was down-regulated by NP (50 μM), P. gingivalis-induced apoptosis decreased by almost 60%. Those results confirm our hypothesis that AIF is a main regulator of KB cell apoptosis after infection with P. gingivalis.