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GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice (2019)
Journal Article
Puig, B., Altmeppen, H. C., Linsenmeier, L., Chakroun, K., Wegwitz, F., Piontek, U. K., Tatzelt, J., Bate, C., Magnus, T., & Glatzel, M. (2019). GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice. PLoS Pathogens, 15(1), e1007520. https://doi.org/10.1371/journal.ppat.1007520

The cellular prion protein (PrPC) is a cell surface glycoprotein attached to the membrane by a glycosylphosphatidylinositol (GPI)-anchor and plays a critical role in transmissible, neurodegenerative and fatal prion diseases. Alterations in membrane a... Read More about GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice.

The phospholipase A2 pathway controls a synaptic cholesterol ester cycle and synapse damage (2018)
Journal Article
Osborne, C., West, E., & Bate, C. (2018). The phospholipase A2 pathway controls a synaptic cholesterol ester cycle and synapse damage. Journal of Cell Science, 131(8), https://doi.org/10.1242/jcs.211789

The cellular prion protein (PrPC) acts as a scaffold protein that organises signalling complexes. In synaptosomes, the aggregation of PrPC by amyloid-β (Aβ) oligomers attracts and activates cytoplasmic phospholipase A2 (cPLA2), leading to synapse deg... Read More about The phospholipase A2 pathway controls a synaptic cholesterol ester cycle and synapse damage.

Monomeric amyloid-ß reduced amyloid-ß oligomer-induced synapse damage in neuronal cultures (2018)
Journal Article
Bate, C., & Williams, A. (2018). Monomeric amyloid-ß reduced amyloid-ß oligomer-induced synapse damage in neuronal cultures. Neurobiology of Disease, 111, 48-58. https://doi.org/10.1016/j.nbd.2017.12.007

Alzheimer's disease is a progressive neurodegenerative disease characterized by the accumulation of amyloid-β (Aβ) in the brain. Aβ oligomers are believed to cause synapse damage resulting in the memory deficits that are characteristic of this diseas... Read More about Monomeric amyloid-ß reduced amyloid-ß oligomer-induced synapse damage in neuronal cultures.

Cholesterol ester hydrolase inhibitors reduce the production of synaptotoxic amyloid-beta oligomers (2018)
Journal Article
McHale-Owen, H., & Bate, C. (2018). Cholesterol ester hydrolase inhibitors reduce the production of synaptotoxic amyloid-beta oligomers. https://doi.org/10.1016/j.bbadis.2017.12.017

The production of amyloid-β (Aβ) is the key factor driving pathogenesis in Alzheimer's disease (AD). Increasing concentrations of Aβ within the brain cause synapse degeneration and the dementia that is characteristic of AD. Here the factors that affe... Read More about Cholesterol ester hydrolase inhibitors reduce the production of synaptotoxic amyloid-beta oligomers.

Valproic acid and its congener propylisopropylacetic acid reduced the amount of soluble amyloid-ß oligomers released from 7PA2 cells (2018)
Journal Article
Williams, R. S. B., & Bate, C. (2018). Valproic acid and its congener propylisopropylacetic acid reduced the amount of soluble amyloid-ß oligomers released from 7PA2 cells. Neuropharmacology, 128, 54-62. https://doi.org/10.1016/j.neuropharm.2017.09.031

The amyloid hypothesis of Alzheimer's disease suggests that synaptic degeneration and pathology is caused by the accumulation of amyloid-β (Aβ) peptides derived from the amyloid precursor protein (APP). Subsequently, soluble Aβ oligomers cause the lo... Read More about Valproic acid and its congener propylisopropylacetic acid reduced the amount of soluble amyloid-ß oligomers released from 7PA2 cells.

Breaking the Cycle, Cholesterol Cycling, and Synapse Damage in Response to Amyloid-ß (2017)
Journal Article
Bate, C. (2017). Breaking the Cycle, Cholesterol Cycling, and Synapse Damage in Response to Amyloid-ß. Journal of Experimental Neuroscience, 11, https://doi.org/10.1177/1179069517733096

Soluble amyloid-β (Aβ) oligomers, a key driver of pathogenesis in Alzheimer disease, bind to cellular prion proteins (PrPC) expressed on synaptosomes resulting in increased cholesterol concentrations, movement of cytoplasmic phospholipase A2 (cPLA2)... Read More about Breaking the Cycle, Cholesterol Cycling, and Synapse Damage in Response to Amyloid-ß.

The cholesterol ester cycle regulates signalling complexes and synapse damage caused by amyloid-ß (2017)
Journal Article
West, E., Osborne, C., & Bate, C. (2017). The cholesterol ester cycle regulates signalling complexes and synapse damage caused by amyloid-ß. Journal of Cell Science, 130, 3050-3059. https://doi.org/10.1242/jcs.205484

Cholesterol is required for the formation and function of some signalling platforms. In synaptosomes, amyloid-β (Aβ) oligomers, the causative agent in Alzheimer's disease, bind to cellular prion proteins (PrPC) resulting in increased cholesterol conc... Read More about The cholesterol ester cycle regulates signalling complexes and synapse damage caused by amyloid-ß.

Sialylated glycosylphosphatidylinositols suppress the production of toxic amyloid-ß oligomers (2017)
Journal Article
Nolan, W., McHale-Owen, H., & Bate, C. (2017). Sialylated glycosylphosphatidylinositols suppress the production of toxic amyloid-ß oligomers. Biochemical Journal, 474(17), 3045-3058. https://doi.org/10.1042/BCJ20170239

The production of amyloid-β (Aβ) is a key factor driving pathogenesis in Alzheimer's disease (AD). Increasing concentrations of soluble Aβ oligomers within the brain lead to synapse degeneration and the progressive dementia characteristic of AD. Sinc... Read More about Sialylated glycosylphosphatidylinositols suppress the production of toxic amyloid-ß oligomers.

Sialic Acid within the Glycosylphosphatidylinositol Anchor Targets the Cellular Prion Protein to Synapses (2016)
Journal Article
Bate, C., Nolan, W., McHale-Owen, H., & Williams, A. (2016). Sialic Acid within the Glycosylphosphatidylinositol Anchor Targets the Cellular Prion Protein to Synapses. Journal of Biological Chemistry, 291(33), 17093-101. https://doi.org/10.1074/jbc.M116.731117

Although the cellular prion protein (PrPC) is concentrated at synapses, the factors that target PrPC to synapses are not understood. Here we demonstrate that exogenous PrPC was rapidly targeted to synapses in recipient neurons derived from Prnp knock... Read More about Sialic Acid within the Glycosylphosphatidylinositol Anchor Targets the Cellular Prion Protein to Synapses.

An in vitro model for synaptic loss in neurodegenerative diseases suggests a neuroprotective role for valproic acid via inhibition of cPLA(2) dependent signalling (2016)
Journal Article
Williams, R. S. B., & Bate, C. (2016). An in vitro model for synaptic loss in neurodegenerative diseases suggests a neuroprotective role for valproic acid via inhibition of cPLA(2) dependent signalling. Neuropharmacology, 101, 566-575. https://doi.org/10.1016/j.neuropharm.2015.06.013

Many neurodegenerative diseases present the loss of synapses as a common pathological feature. Here we have employed an in vitro model for synaptic loss to investigate the molecular mechanism of a therapeutic treatment, valproic acid (VPA). We show t... Read More about An in vitro model for synaptic loss in neurodegenerative diseases suggests a neuroprotective role for valproic acid via inhibition of cPLA(2) dependent signalling.

Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation (2016)
Journal Article
Bate, C., Nolan, W., McHale-Owen, H., & Williams, A. (2016). Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation. Journal of Biological Chemistry, 291(33), 17093-17101. https://doi.org/10.1074/jbc.M116.731117

The prion diseases occur following the conversion of the cellular prion protein (PrPC) into disease-related isoforms (PrPSc). In this study, the role of the glycosylphosphatidylinositol (GPI) anchor attached to PrPC in prion formation was examined us... Read More about Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation.

Docosahexaenoic and eicosapentaenoic acids increase neuronal death in response to HuPrP82-146 and A beta 1-42
Journal Article
Bate, C., Marshall, V., Colombo, L., Diomede, L., Salmona, M., & Williams, A. Docosahexaenoic and eicosapentaenoic acids increase neuronal death in response to HuPrP82-146 and A beta 1-42. Neuropharmacology, 54(6), 934-943. https://doi.org/10.1016/j.neuropharm.2008.02.003

Dietary supplements containing polyunsaturated fatty acids (PUFA) are frequently taken for their perceived health benefits including a possible reduction in cognitive decline in the elderly. Here we report that pre-treatment with docosahexaenoic acid... Read More about Docosahexaenoic and eicosapentaenoic acids increase neuronal death in response to HuPrP82-146 and A beta 1-42.