scholarly journals A Molecular Mechanism for Abnormal Prion Protein Accumulation

2019 ◽  
Author(s):  
Keiji Uchiyama ◽  
Suehiro Sakaguchi
Keyword(s):  
Molecular Mechanism ◽  
Prion Protein ◽  
Protein Accumulation

The inhibitory effect of the ScFv of an anti-prion protein antibody secreted from N2a58 cells on abnormal prion protein accumulation in scrapie-infected cells, ScN2a

Prions ◽  
2006 ◽  
pp. 255-255
Author(s):  
Yoshihisa Shimizu ◽  
Yuko Kaku-Ushiki ◽  
Shigeo Fukuda ◽  
Morikazu Shinagawa ◽  
Takashi Yokoyama ◽  
...  
Keyword(s):  
Prion Protein ◽  
Inhibitory Effect ◽  
Protein Accumulation ◽  
Infected Cells

scholarly journals Filipin Prevents Pathological Prion Protein Accumulation by Reducing Endocytosis and Inducing Cellular PrP Release

2002 ◽  
Vol 277 (28) ◽  
pp. 25457-25464 ◽  
Author(s):  
Mathieu Marella ◽  
Sylvain Lehmann ◽  
Jacques Grassi ◽  
Joëlle Chabry
Keyword(s):  
Prion Protein ◽  
Protein Accumulation

Prevalence of lymphoreticular prion protein accumulation in UK tissue samples

2004 ◽  
Vol 203 (3) ◽  
pp. 733-739 ◽  
Author(s):  
David A Hilton ◽  
Azra C Ghani ◽  
Lisa Conyers ◽  
Philip Edwards ◽  
Linda McCardle ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Accumulation ◽  
Tissue Samples

scholarly journals Prion-induced photoreceptor degeneration begins with misfolded prion protein accumulation in cones at two distinct sites: cilia and ribbon synapses

2021 ◽  
Vol 9 (1) ◽  
Author(s):  
James F. Striebel ◽  
Brent Race ◽  
Jacqueline M. Leung ◽  
Cindi Schwartz ◽  
Bruce Chesebro
Keyword(s):  
Retinitis Pigmentosa ◽  
Prion Protein ◽  
Bipolar Cell ◽  
Brain Diseases ◽  
Protein Accumulation ◽  
Post Inoculation ◽  
Rods And Cones ◽  
Ribbon Synapses ◽  
Cell Processes ◽  
Prpsc Deposition

AbstractAccumulation of misfolded host proteins is central to neuropathogenesis of numerous human brain diseases including prion and prion-like diseases. Neurons of retina are also affected by these diseases. Previously, our group and others found that prion-induced retinal damage to photoreceptor cells in mice and humans resembled pathology of human retinitis pigmentosa caused by mutations in retinal proteins. Here, using confocal, epifluorescent and electron microscopy we followed deposition of disease-associated prion protein (PrPSc) and its association with damage to critical retinal structures following intracerebral prion inoculation. The earliest time and place of retinal PrPSc deposition was 67 days post-inoculation (dpi) on the inner segment (IS) of cone photoreceptors. At 104 and 118 dpi, PrPSc was associated with the base of cilia and swollen cone inner segments, suggesting ciliopathy as a pathogenic mechanism. By 118 dpi, PrPSc was deposited in both rods and cones which showed rootlet damage in the IS, and photoreceptor cell death was indicated by thinning of the outer nuclear layer. In the outer plexiform layer (OPL) in uninfected mice, normal host PrP (PrPC) was mainly associated with cone bipolar cell processes, but in infected mice, at 118 dpi, PrPSc was detected on cone and rod bipolar cell dendrites extending into ribbon synapses. Loss of ribbon synapses in cone pedicles and rod spherules in the OPL was observed to precede destruction of most rods and cones over the next 2–3 weeks. However, bipolar cells and horizontal cells were less damaged, indicating high selectivity among neurons for injury by prions. PrPSc deposition in cone and rod inner segments and on the bipolar cell processes participating in ribbon synapses appear to be critical early events leading to damage and death of photoreceptors after prion infection. These mechanisms may also occur in human retinitis pigmentosa and prion-like diseases, such as AD.

Sign in / Sign up

Export Citation Format

Share Document