Prion protein and its role in signal transduction

Didonna, Alessandro

doi:10.2478/s11658-013-0085-0

Cited by 24 publications

(22 citation statements)

References 112 publications

(127 reference statements)

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“…30,31 Efforts to elucidate the physiological role of PrPC in the CNS have determined its involvement in various functions, including cellular adhesion, cell signaling, ion homeostasis, and neuroprotection. [32][33][34][35][36][37][38][39][40][41][42][43][44] Because of PrPC's extracellular nature, it is possible that during blast exposure, shearing forces from the primary blast wave traversing across the brain may cause the tenuously bound PrPC to dislodge and collect within the systemic circulation. We addressed this hypothesis by subjecting adult male Sprague-Dawley (S-D) rats to controlled single pulse shockwaves closely simulating free field blast and collecting blood plasma afterwards for quantification of PrPC.…”

Section: Introductionmentioning

confidence: 99%

Primary Blast-Induced Traumatic Brain Injury in Rats Leads to Increased Prion Protein in Plasma: A Potential Biomarker for Blast-Induced Traumatic Brain Injury

Pham

Sawyer²,

Wang³

et al. 2015

Journal of Neurotrauma

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Traumatic brain injury (TBI) is deemed the ''signature injury'' of recent military conflicts in Afghanistan and Iraq, largely because of increased blast exposure. Injuries to the brain can often be misdiagnosed, leading to further complications in the future. Therefore, the use of protein biomarkers for the screening and diagnosis of TBI is urgently needed. In the present study, we have investigated the plasma levels of soluble cellular prion protein (PrPC) as a novel biomarker for the diagnosis of primary blast-induced TBI (bTBI). We hypothesize that the primary blast wave can disrupt the brain and dislodge extracellular localized PrPC, leading to a rise in concentration within the systemic circulation. Adult male Sprague-Dawley rats were exposed to single pulse shockwave overpressures of varying intensities (15-30 psi or 103.4-206.8 kPa] using an advanced blast simulator. Blood plasma was collected 24 h after insult, and PrPC concentration was determined with a modified commercial enzyme-linked immunosorbent assay (ELISA) specific for PrPC. We provide the first report that mean PrPC concentration in primary blast exposed rats (3.97 ng/mL -0.13 SE) is significantly increased compared with controls (2.46 ng/mL -0.14 SE; two tailed test p < 0.0001). Furthermore, we report a mild positive rank correlation between PrPC concentration and increasing blast intensity (psi) reflecting a plateaued response at higher pressure magnitudes, which may have implications for all military service members exposed to blast events. In conclusion, it appears that plasma levels of PrPC may be a novel biomarker for the detection of primary bTBI.

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Section: Introductionmentioning

confidence: 99%

Primary Blast-Induced Traumatic Brain Injury in Rats Leads to Increased Prion Protein in Plasma: A Potential Biomarker for Blast-Induced Traumatic Brain Injury

Pham

Sawyer²,

Wang³

et al. 2015

Journal of Neurotrauma

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“…However, the exact mechanism is still the subject of considerable discussion [80]. Interestingly recent findings indicate that PrP(C) is involved in signal transduction [81]. The pathological role of advanced glycation end products and the receptor for AGE in CJD was recently studied in the occipital lobe of three patients using anti-AGE and anti-RAGE antibodies [82].…”

Section: Glycation In Prion Diseasesmentioning

confidence: 99%

The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach

Salahuddin

Rabbani

Khan

2014

Cellular and Molecular Biology Letters

148

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of advanced glycation end products; ROS -reactive oxygen species; SNCA -synuclein alpha; sRAGE -soluble receptor of advanced glycation end products; TTR -transthyretin; TKtransketolase; TNF -tumor necrosis factor-α; TPP -thiamine pyrophosphate Review THE ROLE OF ADVANCED GLYCATION END PRODUCTS IN VARIOUS TYPES OF NEURODEGENERATIVE DISEASE:A THERAPEUTIC APPROACH Abstract: Protein glycation is initiated by a nucleophilic addition reaction between the free amino group from a protein, lipid or nucleic acid and the carbonyl group of a reducing sugar. This reaction forms a reversible Schiff base, which rearranges over a period of days to produce ketoamine or Amadori products. The Amadori products undergo dehydration and rearrangements and develop a cross-link between adjacent proteins, giving rise to protein aggregation or advanced glycation end products (AGEs). A number of studies Unauthenticated Download Date | 5/11/18 1:17 PM

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“…It is linked to the cell membrane via a glycosylphospatidylinositol (GPI) anchor, and localized within cholesterolrich domains called rafts. The physiological role of PrP C is still enigmatic; PrP C -null mice failed to show any gross phenotypic feature (Raeber et al 1998) and no univocal role has been proposed yet (Didonna 2013).…”

Section: Introductionmentioning

confidence: 99%

Peer Review #2 of "Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc (v0.1)"

2015

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Prion diseases are a group of fatal neurodegenerative disorders that affect humans and animals. They are characterized by the accumulation in the central nervous system of a pathological form of the host-encoded prion protein (PrP C). The prion protein is a membrane glycoprotein that consists of two domains: a globular, structured C-terminus and an unstructured N-terminus. The N-terminal part of the protein is involved in different functions in both health and disease. In the present work we discuss the production and biochemical characterization of a panel of four monoclonal antibodies (mAbs) against the distal N-terminus of PrP C using a well-established methodology based on the immunization of Prnp 0/0 mice. Additionally, we show their ability to block prion (PrP Sc) replication at nanomolar concentrations in a cell culture model of prion infection. These mAbs represent a promising tool for prion diagnostics and for studying the physiological role of the Nterminal domain of PrP C .

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Prion protein and its role in signal transduction

Cited by 24 publications

References 112 publications

Primary Blast-Induced Traumatic Brain Injury in Rats Leads to Increased Prion Protein in Plasma: A Potential Biomarker for Blast-Induced Traumatic Brain Injury

Primary Blast-Induced Traumatic Brain Injury in Rats Leads to Increased Prion Protein in Plasma: A Potential Biomarker for Blast-Induced Traumatic Brain Injury

The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach

Peer Review #2 of "Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc (v0.1)"

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