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Apoptotic Effect of Gentamicin in Cochlea Ototoxic Rat Model (Preliminary Study)
Published in Cut Adeya Adella, Stem Cell Oncology, 2018
In this study, the pro-apoptotic role of gentamicin as shown in the apoptotic index of the fibroblasts of ototoxic rat models was evaluated. Gentamicin at a dosage of 40 mg/ml was enough to increase the apoptotic index in lateral cochlear wall fibroblasts. Gentamicin toxicity enhances stress markers (caspase 12), pro-apoptotic BAX, released caspase 3 and blocked anti-apoptotic Bcl-2 (Jaikumkao et al., 2016). In chinchillas exposed to gentamicin it was found that cochlea cell death markers increased (Ding et al., 2010). In this present study the method of intratympanic gentamicin injection dose to a Wistar rat used in other research (Sagit et al., 2013) was followed. The chosen termination time of 18 hours after exposure was based on the results of a study of the round window membrane in guinea pigs, which gave the best TUNEL results (Suzuki et al., 2008).
Therapeutic Options to Enhance Poststroke Recovery in Aged Humans
Published in Shamim I. Ahmad, Aging: Exploring a Complex Phenomenon, 2017
Aurel Popa-Wagner, Dumbrava Danut, Roxana Surugiu, Eugen Petcu, Daniela-Gabriela Glavan, Denissa-Greta Olaru, Raluca Sandu Elena
At tissue level one, a clear effect of hypothermia was the preservation of the infarct core, suggesting that the phagocytic activity of microglia was diminished in the animals kept under hypothermic conditions in the first 2 days poststroke. At the transcription level, hypothermia caused a reduction in the mRNA coding for caspase 12, NF-kappa B, and grp78 in the peri-infarcted region, suggesting an overall decrease in the transcriptional activity related to inflammation and apoptosis [62].
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
Apoptosis is an energy-dependent process. Two main apoptotic signaling pathways, including the extrinsic death receptor pathway and the intrinsic mitochondrial pathway, have been well-characterized. However, there are additional pathways that involve the T-cell-mediated cytotoxicity and the perforin-granzyme pathway. The perforin/granzyme pathway induces apoptosis through either granzyme B or granzyme A. Another recent pathway of apoptosis is mediated by the endoplasmic reticulum (ER) which plays important roles in cell fate and will be discussed in details later [17]. Apoptosis is mediated by chronological activation of protein superfamily of caspases [16]. Caspases are expressed in an inactive form of proenzymes in most cells. When activated, they activate other procaspases, leading to the initiation of the cascade of caspase-dependent apoptosis pathway. Caspases are highly conserved cysteine-dependent aspartate-specific proteases. There are different types of caspases: initiator caspases, including CASP-2, 8, 9, and 10; effector caspases, such as CASP-3, 6, and 7; and inflammatory caspases which are CASP-1, 4, and 5). The other caspases that have been recently studied are (i) caspase-11, which is involved in the regulation of apoptosis and cytokine maturation during septic shock, (ii) caspase-12, which mediates apoptosis through the endoplasmic reticulum, (iii) caspase-13, which is believed to be a bovine gene, and (iv) caspase-14, which is highly expressed just in embryonic tissues [23]. Initiator caspases are inactive until specific oligomeric activator protein binds to them. Subsequently, they bind to effector caspases. Effector caspases are then activated through proteolytic cleavage. The activated caspases then proteolytically degrade the intracellular proteins necessary for programmed cell death.
Dexmedetomidine Ameliorates Post-CPB Lung Injury in Rats by Activating the PI3K/Akt Pathway
Published in Journal of Investigative Surgery, 2020
Jian Li, Xuejiao Dou, Dongdong Li, Miao He, Ming Han, Hong Zhang
Apoptosis plays an important role in balancing cell proliferation and death [14]. The regulation of apoptosis depends on the death receptor pathway, the mitochondrial pathway, and the endoplasmic reticulum pathway. In the endoplasmic reticulum stress state, caspase-12 zymogen is specifically activated by other endoplasmic reticulum stress molecules, which leads to apoptosis by way of the caspase-3 pathway [15]. The caspase family contains some of the most important downstream effectors of the PI3K/Akt signaling pathway, which are mainly present in living cells in the form of inactive zymogens, and which play an essential role in apoptosis with caspase-9 acting as a promoter, and caspase-3 acting as an effector. It has been shown that the PI3K/Akt signaling pathway regulates the apoptotic cycle by inhibiting the activity of the caspase family [16].
Investigation of the protective effect of heparin pre-treatment on cerebral ischaemia in gerbils
Published in Pharmaceutical Biology, 2019
QingShan Ye, KeRong Hai, WenXun Liu, Yun Wang, XiaoHong Zhou, ZhenHai Ye, Xin Liu
The current study indicates that heparin pre-treatment reduced the expression of caspase-8 under hypoxia. Caspase-9 is a member of the caspase family and is required for the changes in the morphology of mitochondrion as well as for the production of reactive oxygen species (ROS). Caspase-9 is also required for normal hematopoietic development and is activated by the cytochrome released from mitochondria. Caspase-9 is associated with the mitochondrion-dependent apoptotic pathway (Kawamoto et al. 2016). Intriguingly, caspase-3 can be activated by caspase-9 (Ferrer and Planas 2003). The expression of FasL was increased during early reperfusion after MCAO, and the activated Fas receptor initiated the cell-death receptor pathway by binding to FasL (Ferrer and Planas 2003). FasL may serve as a death receptor for neuronal cells and participate in the death-receptor pathway following ischaemia (Felderhoff-Mueser et al. 2000). Calpain/caspase-12 activation induced by endoplasmic reticulum (ER) stress may activate caspase-3.
Protein misfolding, ER stress and chaperones: an approach to develop chaperone-based therapeutics for Alzheimer’s disease
Published in International Journal of Neuroscience, 2023
Rimaljot Singh, Navpreet Kaur, Neelima Dhingra, Tanzeer Kaur
In response to the accumulation of toxic intracellular Aβ and induced ER stress, caspase-12 is believed to be responsible for initiating the apoptotic cascade. Caspase-12 is a protein located in the cytoplasmic portion of ER that is usually activated by ER stress stimuli [89]. Studies suggest that after the generation of ER stress, the interaction of IRE1–TRAF2 complex with procaspase-12 is responsible for the activation of the caspase-12 pathway [90]. A study of the cortical neurons from caspase-12 knockout mice further added to the evidence that activation of caspase-12 and ER stress are linked and result in neuronal cell death in AD [64].