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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
The superfamily of BCl-2 family proteins located in the mitochondrial membrane determines cell fate decisions (i.e., cell survival or death) by controlling MOMP. Members of this family are classified into two groups, including pro-apoptotic or anti-apoptotic proteins, and are in the forms of homodimers or heterodimers. The pro-apoptotic proteins are further classified as multi-domain members, such as BCL-2 homology (BH) domain proteins such as BAX, BCLXs, and BAK, or single domain members, including BH3-only proteins BID, BIM, BAD, PUMA (p53 upregulated controller of apoptosis), and NOXA. The anti-apoptotic members contain multi-BH domain and include BCL-2, BCL-XL and MCL-1. Owing to the crucial role of BCL-2 family proteins, especially BH3-only proteins, in regulating and promoting apoptosis, they could be a potential target for therapeutic options [30]. Under normal physiological conditions, there is a balance between pro-apoptotic (BAX, BID, BAK or BAD) and anti-apoptotic (BCL-XL and BCL-2) members of the BCL-2 family. This balance can be disrupted by an internal stimulus, leading to an increase in the pro-apoptotic BCL-2 family members or the decrease in the anti-apoptotic BCL-2 family proteins. In most conditions, pro-apoptotic homodimers in the outer membrane of the mitochondrion are formed to make the mitochondrial membrane permeable to release cytochrome c and SMAC which, in turn, trigger the activation of apoptosis cascade [31].
Assessment of Quercetin Isolated from Enicostemma Littorale Against Few Cancer Targets: An in Silico Approach
Published in A. K. Haghi, Ana Cristina Faria Ribeiro, Lionello Pogliani, Devrim Balköse, Francisco Torrens, Omari V. Mukbaniani, Applied Chemistry and Chemical Engineering, 2017
Bcl-2 (B-cell lymphoma 2) is the founding member of Bcl-2 family of apoptosis regulator proteins encoded by the BCL-2 gene. Bcl-2 derives its name from B-cell lymphoma 2 as it is the second member of a range of proteins initially described in chromosomal translocations involving chromosomes 14 and 18 in follicular lymphomas. BCL-2 protein located on outer membrane of mitochondria, consisting 239 amino acids which suppress apoptosis, regulates cell death by controlling the mitochondrial membrane permeability. It also inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis activating factor (APAF-1). Hypermethylation at the fifth carbon ofthe cytosine residues would lead to the origin of cancer.66
Codelivery in Nanoparticle-based siRNA for Cancer Therapy
Published in Loutfy H. Madkour, Nanoparticle-Based Drug Delivery in Cancer Treatment, 2022
Among nondrug pump–related mechanisms, the most important is the activation of antiapoptotic pathways; a defense mechanism that rescues cells from cell death [38]. Apoptosis is the most common type of programmed cell death and is an essential part of the cell cycle. Apoptosis is activated by a series of cascade signals in which many proteins are involved. Bcl-2 is a protein of the Bcl-2 family, encoded by the gene BCL-2, which has a major role in preventing apoptosis in healthy cells [11]. Bcl-2 overexpression prevents cells from entering apoptosis. It is correlated with cancer cell survival and cancer cell resistance. Other members of the Bcl-2 family, such as Mcl-1, a protein encoded by the gene MCL-1, have been identified as inhibitors of apoptosis [39].
Inhibitory potentials of phytocompounds from Ocimum gratissimum against anti-apoptotic BCL-2 proteins associated with cancer: an integrated computational study
Published in Egyptian Journal of Basic and Applied Sciences, 2022
Gideon A. Gyebi, Oludare M. Ogunyemi, Ibrahim M. Ibrahim, Saheed O. Afolabi, Rotimi J. Ojo, Uju D.I. Ejike, Joseph O. Adebayo
Over expression of anti-apoptotic Bcl-2 family proteins is associated with different types of cancer. The anti-cancer activities of Ocimum gratissimum have been reported but the anti-cancer constituent(s) have not been identified. Herein, we applied different computation techniques to screen 103 Ocimum gratissimum derived phytochemicals for potential inhibitors against BCL-2, MCL-1, BCL-B BCL-XL and BFL-1. The Results from this study showed that five lead phytochemicals (ursolic acid, β-sitosterol, luteolin, apigenin 7,4’,dimethyl ether, basilimoside) had high binding tendencies to the five APB2Ps. Ursolic acid, β-sitosterol and luteolin exhibited different levels of multiplicity binding to atleast two of the anti-apoptotic Bcl-2 proteins which may in turn exert inhibitory effect to these proteins. The five lead phytochemicals satisfied the requisite properties for the in silico drug likeness analysis with well favorable ADMET properties. Ursolic acid and luteolin, complexed with the Bcl-2 and BCL-XL respectively, demonstrated high flexibility and structural stability in the 100 ns MD simulation. Evidences from previous work has established the inhibitory potential of ursolic acid, β-sitosterol and luteolin against the APB2Ps. The results suggest that the anti-proliferative activity O. gratissimum may be as a result of the synergistic activities of, at least, the lead phytochemicals. There is therefore further need to investigate these phytochemicals as potential drug candidates.
Cadmium induces cytotoxicity in normal mouse renal MM55.K cells
Published in International Journal of Environmental Health Research, 2022
Ho Jeong Lee, Ju Hong Lee, Seon Min Lee, Na Hyun Kim, Yeon Gyu Moon, Tae Kil Tak, Moonjung Hyun, Jeong Doo Heo
Apoptotic processes can be initiated through one of two pathways which are intrinsic and extrinsic pathways. Caspases are key components of both the apoptotic pathways, i.e. the intrinsic mitochondria-mediated and extrinsic death receptor-mediated apoptotic pathways. The intrinsic pathway is regulated by two groups of mitochondrial molecules, Bcl-2 and Bax. The Bcl-2 family consists of both pro- and anti-apoptotic members, and the balance between these members determines the susceptibility of a cell to apoptosis (Wyllie et al. 1980). According to report, the survivin is a member of inhibitor of apoptosis (IAP) family. These protein inhibits caspase activation leading to negative regulation of apoptosis (Mita et al. 2008). The present results indicate that CdCl2 significantly decreased the levels of pro-caspase-3 and −9 and increased the expression of cleaved caspase-3 and cleaved PARP. In the mitochondrial apoptotic pathway, we demonstrated that ΔΨm loss was caused by CdCl2 in MM55.K cells via flow cytometry. In addition, the expression of the anti-apoptotic Bcl-xL was decreased, whereas the expression of the pro-apoptotic Bax protein was unchanged, and the ratio of Bax/Bcl-xL increased in a dose-dependent manner in CdCl2-treated MM55.K cells.
Neurotoxicity of β-HgS differs from environmental mercury pollutants (MeHgCl and HgCl2) in Neuro-2a cell
Published in International Journal of Environmental Health Research, 2021
Zhenghua Xia, Hongtao Bi, Cen Li, Lujing Geng, Muhammad Usman, Yuzhi Du, Lixin Wei
Bcl-2 family proteins are involved in the response to apoptosis (Ji et al. 2008). Due to Bcl-2 family proteins has been proved to regulate mitochondrial-dependent apoptosis meanwhile balance anti- and pro-apoptotic members to arbitrate life/death decisions, therefore the ratio of Bcl-2 to Bax can use as a pivotal factor to determines whether apoptosis will occur in the cells exposed to injurious chemicals (Cheng et al. 2007; Pradelli et al. 2010). With the increase of incubation time, compared with the control group, the ratios of Bcl-2 and Bak in MeHg group decreased gradually, while the ratio of β-HgS increased gradually. Furthermore, our previous study found that mercury could affect the release of inflammatory cytokines in neuroglial cells (Tan et al. 2018). In this study, compare with the control group, the expressions of TNF-α, IL-6 and IL-1β in MeHgCl group were up-regulated significantly in 6 h, 12 h and 24 h, and the expressions of IL-1β and IL-6 in HgCl2 group was increased significant in 6 h and 24 h respectively. While, there was only significantly up-regulated of IL-6 in Neuro-2a cells after β-HgS exposure for 24 h. These findings indicate that β-HgS is much less neurotoxicity than MeHgCl and HgCl2 in Neuro-2a cells. However, the critical roles of these differences were still required investigation in the future.