Anti-PrP antibodies detected at terminal stage of prion-affected mouse

Sassa, Yukiko; Kataoka, Natsumi; Inoshima, Yasuo; Ishiguro, Naotaka

doi:10.1016/j.cellimm.2010.03.018

Cited by 18 publications

(10 citation statements)

References 31 publications

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“…As the APPs and immunoglobulins are part of the globulin fraction, this increase could be the result of increased synthesis of APPs, as seen for the three positive APPs tested in this work: Hp, SAA and Cp. Several studies have failed to describe a significant increase in immunoglobulins at clinical classical scrapie, especially scrapie-specific IgG [43-45]. …”

Section: Discussionmentioning

confidence: 99%

Presence of an acute phase response in sheep with clinical classical scrapie

2012

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BackgroundWork with experimental scrapie in sheep has been performed on-site for many years including studies on PrPSc dissemination and histopathology of organs and tissues both at preclinical and clinical stages. In this work serum was sampled at regular intervals from lambs which were infected immediately after birth and from parallel healthy controls, and examined for acute phase proteins. In contrast to earlier experiments, which extensively studied PrPSc dissemination and histopathology in peripheral tissues and brain, this experiment is focusing on examination of serum for non-PrPSc markers that discriminates the two groups, and give insight into other on-going processes detectable in serum samples.ResultsThere was clear evidence of an acute phase response in sheep with clinical scrapie, both experimental and natural. All the three proteins, ceruloplasmin, haptoglobin and serum amyloid A, were increased at the clinical stage of scrapie.ConclusionThere was evidence of a systemic measurable acute phase response at the clinical terminal end-stage of classical scrapie.

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Section: Discussionmentioning

confidence: 99%

Presence of an acute phase response in sheep with clinical classical scrapie

2012

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“…44 Many studies have mentioned the involvement of the lymphoreticular cells in PrP Sc accumulation, replication and transport from the peripheral lymphoid organs to the central nervous system, 48 and the detection of anti-PrP antibody at the terminal stage of mouse scrapie. 49 Investigating local immunity may be important to understand prion disease progression in the body. In addition, the contribution of inflammation to the progression of prion disease is poorly understood.…”

Section: Discussionmentioning

confidence: 99%

Gene expression alterations in Rocky Mountain elk infected with chronic wasting disease

Basu

Almeida

Dudas

et al. 2012

Prion

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Chronic wasting disease (CWD) is an invariably fatal neurologic disease that naturally infects mule deer, white tailed deer and elk. The understanding of CWD neurodegeneration at a molecular level is very limited. In this study, microarray analysis was performed to determine changes in the gene expression profiles in six different tissues including brain, midbrain, thalamus, spleen, RPLN and tonsil of CWD-infected elk in comparison to non-infected healthy elk, using 24,000 bovine specific oligo probes. In total, 329 genes were found to be differentially expressed (> 2.0-fold) between CWD negative and positive brain tissues, with 132 genes upregulated and 197 genes downregulated. There were 249 DE genes in the spleen (168 up- and 81 downregulated), 30 DE genes in the retropharyngeal lymph node (RPLN) (18 up- and 12 downregulated), and 55 DE genes in the tonsil (21 up- and 34 downregulated). Using Gene Ontology (GO), the DE genes were assigned to functional groups associated with cellular process, biological regulation, metabolic process, and regulation of biological process. For all brain tissues, the highest ranking networks for DE genes identified by Ingenuity Pathway Analysis (IPA) were associated with neurological disease, cell morphology, cellular assembly and organization. Quantitative real-time PCR (qRT-PCR) validated the expression of DE genes primarily involved in different regulatory pathways, including neuronal signaling and synapse function, calcium signaling, apoptosis and cell death and immune cell trafficking and inflammatory response. This is the first study to evaluate altered gene expression in multiple organs including brain from orally infected elk and the results will improve our understanding of CWD neurodegeneration at the molecular level.

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“…11 This conversion followed by an accumulation of PrP Sc within the central nervous system resulting in disease 12 ( Fig. 1).…”

Section: Development Of Prion Diseasementioning

confidence: 99%

Prion protein scrapie and the normal cellular prion protein

Atkinson

Zhang

Munn

et al. 2015

Prion

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ABSTRACT. Prions are infectious proteins and over the past few decades, some prions have become renowned for their causative role in several neurodegenerative diseases in animals and humans. Since their discovery, the mechanisms and mode of transmission and molecular structure of prions have begun to be established. There is, however, still much to be elucidated about prion diseases, including the development of potential therapeutic strategies for treatment. The significance of prion disease is discussed here, including the categories of human and animal prion diseases, disease transmission, disease progression and the development of symptoms and potential future strategies for treatment. Furthermore, the structure and function of the normal cellular prion protein (PrP C ) and its importance in not only in prion disease development, but also in diseases such as cancer and Alzheimer's disease will also be discussed.

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Anti-PrP antibodies detected at terminal stage of prion-affected mouse

Cited by 18 publications

References 31 publications

Presence of an acute phase response in sheep with clinical classical scrapie

Presence of an acute phase response in sheep with clinical classical scrapie

Gene expression alterations in Rocky Mountain elk infected with chronic wasting disease

Prion protein scrapie and the normal cellular prion protein

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