Ultrastructural localization of prion proteins: Physiological and pathological implications

Fournier, Jean‐Guy; Escaig-Haye, F.; Grigoriev, V.

doi:10.1002/1097-0029(20000701)50:1<76::aid-jemt11>3.0.co;2-#

Cited by 85 publications

(68 citation statements)

References 77 publications

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“…In contrast, ultrastructural analyses using brains of prion-infected mice and hamsters identified PrP Sc frequently at the plasma membranes and less frequently at synapses and compartments of the endolysosomal system (Arnold et al, 1995;Fournier et al, 2000;Godsave et al, 2008). Recently, Godsave and colleagues reported that in RML strain-infected mouse brains, the majority of PrP Sc clusters were detected at the plasma membranes, including membrane invaginations and the site of cell-to-cell contact, whereas in the other subcellular regions such as synapses and intracellular vesicles, PrP Sc clusters were detected only occasionally by immuno-electron microscopic examination using an antibody that recognizes the N-terminal region of PrP (Godsave et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Tanaka

Fujiwara

Suzuki

et al. 2016

Journal of General Virology

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We established abnormal isoform of prion protein (PrP Sc )-specific double immunostaining using mAb 132, which recognizes aa 119-127 of the PrP molecule, and novel PrP Sc -specific mAb 8D5, which recognizes the N-terminal region of the PrP molecule. Using the PrP Sc -specific double immunostaining, we analysed PrP Sc in immortalized neuronal cell lines and primary cerebralneuronal cultures infected with prions. The PrP Sc -specific double immunostaining showed the existence of PrP Sc positive for both mAbs 132 and 8D5, as well as those positive only for either mAb 132 or mAb 8D5. This indicated that double immunostaining detects a greater number of PrP Sc species than single immunostaining. Double immunostaining revealed cell-type-dependent differences in PrP Sc staining patterns. In the 22 L prion strain-infected Neuro2a (N2a)-3 cells, a subclone of N2a neuroblastoma cell line, or GT1-7, a subclone of the GT1 hypothalamic neuronal cell line, granular PrP Sc stains were observed at the perinuclear regions and cytoplasm, whereas unique string-like PrP Sc stains were predominantly observed on the surface of the 22 L straininfected primary cerebral neurons. Only 14 % of PrP Sc in the 22 L strain-infected N2a-3 cells were positive for mAb 8D5, indicating that most of the PrP Sc in N2a-3 lack the N-terminal portion. In contrast, nearly half PrP Sc detected in the 22 L strain-infected primary cerebral neurons were positive for mAb 8D5, suggesting the abundance of full-length PrP Sc that possesses the Nterminal portion of PrP. Further analysis of prion-infected primary neurons using PrP Sc -specific immunostaining will reveal the neuron-specific mechanism for prion propagation.

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Section: Discussionmentioning

confidence: 99%

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Tanaka

Fujiwara

Suzuki

et al. 2016

Journal of General Virology

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“…Most of these deposits appear to be extracellular, a conclusion that is confirmed by electron microscopic studies that have identified both fibrillar and nonaggregated forms of PrP Sc in spaces surrounding neurons and their processes (DeArmond et al, 1985;Jeffrey et al, 1994aJeffrey et al, , 1997. Published images showing intracellular accumulation of PrP Sc in brain are rare (Piccardo et al, 1990;Laszlo et al, 1992;Arnold et al, 1995;Fournier et al, 2000;Kovacs et al, 2005). The difficulty in visualizing intracellular PrP Sc deposits may be a consequence of the antigen retrieval techniques that are used to enhance the immunoreactivity of PrP Sc .…”

Section: Discussionmentioning

confidence: 99%

Visualization of Prion Infection in Transgenic Mice Expressing Green Fluorescent Protein-Tagged Prion Protein

Barmada¹

2005

Journal of Neuroscience

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“…PrP C is subject to endocytic recycling (10) and is present in secretory cytoplasmic granules (11) that, at least in platelets, can facilitate increases in surface membrane PrP C levels (12). Thus, surface expression levels may be influenced by post-translational processing as well as by transcriptional up-regulation.…”

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confidence: 99%

A role of cellular prion protein in programming T‐cell cytokine responses in disease

et al. 2009

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The cellular prion protein (PrPC) is widely expressed in neural and non‐neural tissues, but its function is unknown. Elucidation of the part played by PrPC in adaptive immunity has been a particular conundrum: increased expression of cell surface PrPChas been documented during T‐cell activation, yet the functional significance of this activation remains unclear, with conflicting data on the effects of Prnp gene knockout on various parameters of T‐cell immunity. We show here that Prnp mRNA is highly inducible within 8‐24 h of T‐cell activation, with surface protein levels rising from 24 h. When measured in parallel with CD69 and CD25, PrPC is a late activation antigen. Consistent with its up‐regulation being a late activation event, PrP deletion did not alter T‐cell‐antigen presenting cell conjugate formation. Most important, activated PrP0/0T cells demonstrated much reduced induction of several T helper (Th) 1, Th2, and Th17 cytokines, whereas others, such as TNF‐α and IL‐9, were unaffected. These changes were investigated in the context of an autoimmune model and a bacterial challenge model. In experimental autoimmune encephalomyelitis, PrP‐knockout mice showed enhanced disease in the face of reduced IL‐17 responses. In a streptococcal sepsis model, this constrained cytokine program was associated with poorer local control of infection, although with reduced bacteremia. The findings indicate that PrPC is a potentially important molecule influencing T‐cell activation and effector function.—Ingram, R.J., Isaacs, J.D., Kaur, G., Lowther, D.E., Reynolds, C.J., Boyton,R. J., Collinge, J., Jackson, G.S., Altmann, D.M. A role of cellular prion protein in programming T‐cell cytokine responses in disease. FASEB J. 23, 1672–1684 (2009)

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Ultrastructural localization of prion proteins: Physiological and pathological implications

Cited by 85 publications

References 77 publications

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Visualization of Prion Infection in Transgenic Mice Expressing Green Fluorescent Protein-Tagged Prion Protein

A role of cellular prion protein in programming T‐cell cytokine responses in disease

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