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Anticancer Properties of Silver Nanoparticles from Root Extract of Trigonella Foenum-Graecum
Published in Megh R. Goyal, Preeti Birwal, Santosh K. Mishra, Phytochemicals and Medicinal Plants in Food Design, 2022
Ramasamy Harikrishnan, Lourthu Samy S. Mary, Gunapathy Devi, Chellam Balasundaram
A number of proapoptotic fragments of molecules are discharged from the mt through the apoptosis. The mt in the presence of ATP discharged cytochrome c that linked with Apaf-1 in the cytosol encouraging its oligomerization. The apoptosome is produced from oligomeric-Apaf-1 combination and pro-caspase-9, which enhances the stimulation of caspase-9, and in chance triggers the effector caspases-3 and -7 [8]. The exciting outcome from this study was that though ATP concentration declined post-TFAgNPs interaction, the caspase-9 activity was quiet prominent in this experiment.
In Silico approach of soursop leaf for prediction of anticancer molecular target therapy
Published in Ade Gafar Abdullah, Isma Widiaty, Cep Ubad Abdullah, Medical Technology and Environmental Health, 2020
M.K. Dewi, Y. Kharisma, L. Yuniarti
Intrinsic pathway (mitochondria) occurs due to mitochondrial permeability that releases proapoptotic molecules into the cytosol. Growth factors and other signals can stimulate the formation of Bcl2 and Bcl-XL antiapoptotic proteins, which are present in the mitochondrial membrane and cytoplasm to prevent apoptosis. When cells are stressed, antiapoptosis is replaced by Bak and Bax proapoptosis which forms the channel through which cytochrome c and other mitochondrial proteins exit into the cytosol. Cytochrome c binds to the Apaf-1 protein and activates the caspase 9. Caspase 9 activates the exclusionary caspases 3, 6, and 7. Caspase, Bax, and Bid are proapoptotic proteins (Green 2006).
Tissue injury and repair
Published in C. Simon Herrington, Muir's Textbook of Pathology, 2020
The intrinsic pathway involves mitochondria. In normal cells, there are anti-apoptotic molecules present in the membranes of mitochondria. These belong to the Bcl-2 family of proteins, most notably Bcl-2 itself and Bcl-x. Their presence is stimulated by growth factors and other normal survival signals. Under circumstances of cellular stress or where the cell is deprived of its normal survival signals, there is a loss of the anti-apoptotic proteins and these are replaced by pro-apoptotic members of the same family such as Bax. A shift in the balance between pro- and anti-apoptotic Bcl-2 family members to favour apoptosis causes the mitochondrial membranes to become leaky (so-called mitochondrial permeability transition). One of the proteins that then escapes from the mitochondria is cytochrome C, an enzyme involved in respiration. In the cytosol, this protein binds to another protein Apaf-1 (apoptosis-activating factor 1), which is capable of activating caspases. Other proteins leak out from the mitochondria, which further encourages apoptosis.
Overexpression of NDRG2 promotes the therapeutic effect of pazopanib on ovarian cancer
Published in Journal of Receptors and Signal Transduction, 2021
Ying Cui, Guihua Shen, Linlin Ma, Qiubo Lv
Caspase-9 is a key regulator in the intrinsic pathway involved under multiple stimuli, including chemotherapies, stress agents, and radiation. Dysfunction of caspase-9 activation leads to the development of degenerative disease and cancer. Activation of caspase-9 requires the binding with APAF-1 [44]. APAF-1 is known to bind with caspase-9 through CARD domains, which provides an indispensable complementary interface for activation of caspase-9 [45]. A previous study found that activation of caspase-9 and caspase-3 are present at the end stage of the disease, suggesting that activation of caspases might contribute to the apoptosis of cells [46], this result showed that caspase-9 is required for the maintaining of cellular homeostasis via regulation of apoptosis. Other studies showed that activated caspase-9 further induce the cleave of caspase-3, which binds with the apoptosome and performs as an executor of the apoptosis process [47].
Possible modifier genes in the variation of neurofibromatosis type 1 clinical phenotypes
Published in Journal of Neurogenetics, 2018
Apoptosis can be initiated in the intrinsic and extrinsic pathways. Both pathways induce cell death by activating caspases. One of the important proteins in the intrinsic pathway is apoptotic protease activating factor-1 (Apaf-1), and any loss of expression of this protein can result in tumor development (Igney & Krammer, 2002). Hepatocellular carcinoma antigen 66 (HCA66) is one of the proteins that interacts with Apaf-1 and can regulate apoptosis. The HCA66 gene, located on chromosome 17q11.2, is one of the genes that is deleted in NF1-microdeletion syndrome (De Raedt et al., 2004). Patients with NF1-microdeletion syndrome have a distinct phenotype with a poor prognosis characterized by a low IQ, dysmorphic features, and numerous neurofibromas (Leppig et al., 1997). Piddubnyak et al. (2007) examined the effect of the modulated expression of HCA66 on the apoptosis of cell lines derived from NF1-microdeleted patients. In this study, they showed that HCA66 seems to regulate apoptosis at the level of the Apaf-1-induced activation of caspase-9 in the apoptosome following cytochrome c/dATP stimulation. Likewise, they presumed that the binding of HCA66 can also induce a conformational change that would increase the recruitment of caspase-9. Therefore, the reduced expression of HCA66 could make cell lines derived from NF1-microdeleted patients less susceptible to apoptosis. Accordingly, not only the HCA66 gene but also all of the proteins involved in the apoptotic pathway should be considered as possible modifiers in NF1 tumors.
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
The Bcl-2 gene family which includes anti-apoptotic Bcl-2 is significant in the regulation of cell apoptosis [37]. Here, we found that Bcl-2 gene expression in tumor tissue was reduced by CGA. In addition, the combination of CGA and DOX significantly decreased the Bcl-2 gene expression level in comparison with each treatment alone. Thus, the reduction in gene expression of Bcl-2 leads to disruption of mitochondrial outer membrane permeability and the release of cytochrome-c into the cytoplasm. Cytochrome-c triggers the formation of apoptosome by binding to apoptosis protease activating factor-1 (Apaf-1) and pro-caspase-9, allowing the release of caspase-9. This process in turn activates downstream executor caspases-3, caspase-6 and caspase-7 [38,39].