Zeitschriften- und Bucherschau

W., None E. J.; D., None W.; T., None S.; Müller, A. R.; Z., W.; S., G.; Smith, C.; M., R. R.; S., J. A.; D., K. J.; Z., E. B.; Ziemer, B.; W., G.; M., A.; K., M.; H.C., S.; Becker, U.; Bultmann, Christoph; Ego, B.; Oorschot, J. van; Mathys, H.-P.; Ego, Beate; Fischer, A. A.; Witte, M.

doi:10.1515/zatw.2004.116.3.416

Cited by 2 publications

(2 citation statements)

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“…In regulating mitochondrial fusion, OPA1 depends on Mfn1 (Cipolat et al, 2004). The expression of OPA1 is downregulated by cellular prion protein, leading to depletion of mtDNA and neuronal apoptosis, while overexpression of OPA1 can partially reverse cellular apoptosis induced by prion protein (Wu et al, 2019). Moreover, overexpression of Mfn2 rather than Mfn1 significantly inhibits the AβO-mediated cell death pathway (Park et al, 2015).…”

Section: The Disruption Of the Balance Of Mitochondrial Dynamics Caus...mentioning

confidence: 99%

Neurotoxic β-amyloid oligomers cause mitochondrial dysfunction—the trigger for PANoptosis in neurons

Meng,

Song,

Liu

et al. 2024

Front. Aging Neurosci.

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As the global population ages, the incidence of elderly patients with dementia, represented by Alzheimer's disease (AD), will continue to increase. Previous studies have suggested that β-amyloid protein (Aβ) deposition is a key factor leading to AD. However, the clinical efficacy of treating AD with anti-Aβ protein antibodies is not satisfactory, suggesting that Aβ amyloidosis may be a pathological change rather than a key factor leading to AD. Identification of the causes of AD and development of corresponding prevention and treatment strategies is an important goal of current research. Following the discovery of soluble oligomeric forms of Aβ (AβO) in 1998, scientists began to focus on the neurotoxicity of AβOs. As an endogenous neurotoxin, the active growth of AβOs can lead to neuronal death, which is believed to occur before plaque formation, suggesting that AβOs are the key factors leading to AD. PANoptosis, a newly proposed concept of cell death that includes known modes of pyroptosis, apoptosis, and necroptosis, is a form of cell death regulated by the PANoptosome complex. Neuronal survival depends on proper mitochondrial function. Under conditions of AβO interference, mitochondrial dysfunction occurs, releasing lethal contents as potential upstream effectors of the PANoptosome. Considering the critical role of neurons in cognitive function and the development of AD as well as the regulatory role of mitochondrial function in neuronal survival, investigation of the potential mechanisms leading to neuronal PANoptosis is crucial. This review describes the disruption of neuronal mitochondrial function by AβOs and elucidates how AβOs may activate neuronal PANoptosis by causing mitochondrial dysfunction during the development of AD, providing guidance for the development of targeted neuronal treatment strategies.

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Section: The Disruption Of the Balance Of Mitochondrial Dynamics Caus...mentioning

confidence: 99%

Neurotoxic β-amyloid oligomers cause mitochondrial dysfunction—the trigger for PANoptosis in neurons

Meng,

Song,

Liu

et al. 2024

Front. Aging Neurosci.

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“…A plethora of studies into neurodegeneration have demonstrated that the persistent accumulation of damaged mitochondria in neurons is involved in aging and neurodegenerative disorders, including prion disease (Norat et al, 2020). Our previous study has demonstrated that PrP 106−126 peptide can cause mitochondrial damage and dysfunction, in turn exacerbating the course of damage induced by PrP 106−126 based on cellular and animal models (Yang et al, 2008a;Li et al, 2018Li et al, , 2022Wu et al, 2019;Zhang et al, 2020). Specifically, mitochondrial homeostasis is gradually disrupted in N2a cells stimulated by PrP 106−126 , causing aggressive fission, reduced fusion, and intensified apoptosis.…”

mentioning

confidence: 99%

Cardiolipin externalization mediates prion protein (PrP) peptide 106–126-associated mitophagy and mitochondrial dysfunction

Yang,

Li,

et al. 2023

Front. Mol. Neurosci.

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Proper mitochondrial performance is imperative for the maintenance of normal neuronal function to prevent the development of neurodegenerative diseases. Persistent accumulation of damaged mitochondria plays a role in prion disease pathogenesis, which involves a chain of events that culminate in the generation of reactive oxygen species and neuronal death. Our previous studies have demonstrated that PINK1/Parkin-mediated mitophagy induced by PrP106−126 is defective and leads to an accumulation of damaged mitochondria after PrP106−126 treatment. Externalized cardiolipin (CL), a mitochondria-specific phospholipid, has been reported to play a role in mitophagy by directly interacting with LC3II at the outer mitochondrial membrane. The involvement of CL externalization in PrP106−126-induced mitophagy and its significance in other physiological processes of N2a cells treated with PrP106−126 remain unknown. We demonstrate that the PrP106−126 peptide caused a temporal course of mitophagy in N2a cells, which gradually increased and subsequently decreased. A similar trend in CL externalization to the mitochondrial surface was seen, resulting in a gradual decrease in CL content at the cellular level. Inhibition of CL externalization by knockdown of CL synthase, responsible for de novo synthesis of CL, or phospholipid scramblase-3 and NDPK-D, responsible for CL translocation to the mitochondrial surface, significantly decreased PrP106−126-induced mitophagy in N2a cells. Meanwhile, the inhibition of CL redistribution significantly decreased PINK1 and DRP1 recruitment in PrP106−126 treatment but had no significant decrease in Parkin recruitment. Furthermore, the inhibition of CL externalization resulted in impaired oxidative phosphorylation and severe oxidative stress, which led to mitochondrial dysfunction. Our results indicate that CL externalization induced by PrP106−126 on N2a cells plays a positive role in the initiation of mitophagy, leading to the stabilization of mitochondrial function.

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Zeitschriften- und Bucherschau

Cited by 2 publications

References 0 publications

Neurotoxic β-amyloid oligomers cause mitochondrial dysfunction—the trigger for PANoptosis in neurons

Neurotoxic β-amyloid oligomers cause mitochondrial dysfunction—the trigger for PANoptosis in neurons

Cardiolipin externalization mediates prion protein (PrP) peptide 106–126-associated mitophagy and mitochondrial dysfunction

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