Browsing by Subject "Cell biology"

Now showing 1 - 3 of 3
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    Alzheimer ß-amyloid peptides normal and abnormal localization
    (Murcia : F. Hernández, 2002) Takahashi, R.H.; Nam, E.E.; Edgar, M.; Gouras, G.K.
    Alzheimer's disease (AD) neuropathology is characterized by accumulation of “senile” plaques (SPs) and neurofibrillary tangles (NFTs) in vulnerable brain regions. SPs are principally composed of aggregates of up to 42/43 amino acid ß-amyloid (Aß) peptides. The discovery of familial AD (FAD) mutations in the genes for the amyloid precursor protein (APP) and presenilins (PSs), all of which increase Aß42 production, support the view that Aß is centrally involved in the pathogenesis of AD. Aß42 aggregates readily, and is thought to seed the formation of fibrils, which then act as templates for plaque formation. Aß is generated by the sequential intracellular cleavage of APP by ßsecretase to generate the N-terminal end of Aß, and intramembranous cleavage by g-secretase to generate the C-terminal end. Cell biological studies have demonstrated that Aß is generated in the ER, Golgi, and endosomal/lysosomal system. A central question involving the role of Aß in AD concerns how Aß causes disease and whether it is extracellular Aß deposition and/or intracellular Aß accumulation that initiates the disease process. The most prevalent view is that SPs are composed of extracellular deposits of secreted Aß and that Aß causes toxicity to surrounding neurons as extracellular SP. The recent emphasis on the intracellular biology of APP and Aß has led some investigators to consider the possibility that intraneuronal Aß may directly cause toxicity. In this review we will outline current knowledge of the localization of both intracellular and extracellular Aß.
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    Mitochondrial metabolism characterization of four different fish cell lines
    Espinosa-Ruiz, Cristóbal; Mayor-Lafuente, Javier; Esteban Abad, María de los Ángeles; Biología Celular e Histología
    Different cell lines (SAF-1, DLB-1, PLHC-1 and FuB-1) mitro stress (OCR and ECAR) raw data.
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    Stress-activated MAPK signaling controls fission yeast actomyosin ring integrity by modulating formin For3 levels
    (ELIFE SCIENCES PUBLICATIONS LTD, 2020-09-11) Gómez-Gil, E.; Martín-García, R.; Vicente-Soler, J.; Franco, A.; Vázquez-Marín, B.; Prieto-Ruiz, F.; Soto, T.; Pérez, P.; Madrid, M.; Cansado Vizoso, José; Genética y Microbiología
    Cytokinesis, which enables the physical separation of daughter cells once mitosis has been completed, is executed in fungal and animal cells by a contractile actin- and myosin-based ring (CAR). In the fission yeast Schizosaccharomyces pombe, the formin For3 nucleates actin cables and also co-operates for CAR assembly during cytokinesis. Mitogen-activated protein kinases (MAPKs) regulate essential adaptive responses in eukaryotic organisms to environmental changes. We show that the stress-activated protein kinase pathway (SAPK) and its effector, MAPK Sty1, downregulates CAR assembly in S. pombe when its integrity becomes compromised during cytoskeletal damage and stress by reducing For3 levels. Accurate control of For3 levels by the SAPK pathway may thus represent a novel regulatory mechanism of cytokinesis outcome in response to environmental cues. Conversely, SAPK signaling favors CAR assembly and integrity in its close relative Schizosaccharomyces japonicus, revealing a remarkable evolutionary divergence of this response within the fission yeast clade.