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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.
Exploration of novel heterofused 1,2,4-triazine derivative in colorectal cancer
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2021
Justyna Magdalena Hermanowicz, Anna Szymanowska, Beata Sieklucka, Robert Czarnomysy, Krystyna Pawlak, Anna Bielawska, Krzysztof Bielawski, Joanna Kalafut, Alicja Przybyszewska, Arkadiusz Surazynski, Adolfo Rivero-Muller, Mariusz Mojzych, Dariusz Pawlak
A decrease in MMP is one of the earliest changes associated with PCD. During apoptosis, the permeability of the external and the internal mitochondrial membrane is increased. As a consequence, the mitochondrial proteins are released into the cytosol through the outer membrane, e.g. cytochrome c and apoptosis inducing factor (AIF). The exposure to RSC, 5-FU, and MM-129 for 24 h resulted in the loss of membrane integrity in both colon adenocarcinoma cell lines (Supplementary Figure 1Sc, 1Sd). The rate of MMP-disrupted cells was increased in a concentration dependent manner. This effect was particularly seen in the case of MM-129 at a concentration of 3 µM, where the percentage of cells with decreased levels of MMP reached 71.3% and 81% for DLD-1 (Figure 7(a)) and HT-29 (Figure 7(b)), respectively. Moreover, in the case of MM-129, a clear concentration dependent effect was observed. This suggests that pyrazolo[4,3-e]tetrazolo[1,5-b][1,2,4]triazine-induced MMP disruption involved in the intrinsic apoptosis pathway.
Targeted therapy in acute myeloid leukemia: current status and new insights from a proteomic perspective
Published in Expert Review of Proteomics, 2020
Anneke D. van Dijk, Eveline S. J. M. de Bont, Steven M. Kornblau
The clinical applications of MS in acute leukemia include the identification of diagnostic biomarkers. Xu et al. for example developed a proteomic-classification system by analyzing 151 de novo acute leukemia patients using SELDI-TOF MS. The proteomic-subtypes correlated with the type of leukemia (acute promyelocytic leukemia (APL), granulocytic AML, monocytic AML, and acute lymphocytic leukemia (ALL)). The authors suggest that this proteomic classification holds promise to identify potential protein biomarkers for each specific subgroup of acute leukemia [50]. Protein biomarkers are also identified to distinguish between malignant AML and the premalignant myelodysplastic syndrome (MDS). Clinically, measurement of the percentage of bone marrow blasts remains the method of monitoring disease progression. A patient is diagnosed with MDS if the bone marrow contains <20% blasts, but the diagnosis changes into AML if 21% or more blasts are found. It is however clear that this cutoff between premalignant to malignant disease does not precisely reflect the degree of malignancy. It would be of clinical interest if a reliable biomarker could predict which MDS patients have a higher chance to progress into AML. Using MS, serum protein CXC chemokine ligands 4 and 7 (CXCL4, CXCL7) have been identified as proteins with decreased expression in advanced MDS [51]. Another study using MALDI-TOF MS identified that MOES, EZRI, and AIFM1 could be considered as AML-specific expressing proteins and therefore may serve as diagnostic biomarkers to distinguish MDS and AML [52].
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
The integrity of oral epithelium is a critical protective barrier of the defense against bacterial infection. Cycles of cell proliferation serve to maintain the barrier function of oral epithelial cells [15,16]. Previously, cell death was largely considered to be the result of necrosis, an unregulated and accidental cell death. Apoptosis, an active cell death regulated by caspase cascade, was regarded as a mechanism to illustrate the extensive destruction of oral tissue [17–20]. Caspase-3 is one of the key executioners of apoptosis and highly expresses in the gingival crevicular fluid and serum in patients with chronic periodontitis[21]. Increased DNA fragmentation, caspase-3 activity and the expression of apoptosis-related proteins such as Fas and FasL were detected in the gingival tissues of patients with chronic periodontitis [22–24]. Nevertheless, there are caspase-independent apoptotic pathways besides the caspase-dependent pathway [25,26]. AIF, a mitochondrial proapoptotic protein, normally locates in the intermembrane space of mitochondria and transfers to the nucleus after receiving proapoptotic stimulation [27,28]. Aral et al. found that AIF was significantly upregulated in the gingival crevicular fluid of patients with generalized aggressive periodontitis and chronic periodontitis [29]. But it is still unclear whether P. gingivalis regulates apoptosis of epithelial cells by caspases or AIF.