Transmissible spongiform encephalopathies: a family of etiologically complex diseases—a review

Bounias, M.; Purdey, Mark

doi:10.1016/s0048-9697(02)00140-7

Cited by 18 publications

(13 citation statements)

References 131 publications

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“…For this purpose, we have investigated the occurrence of PrP c -specific mRNAs by RT-PCR, the protein concentration by ELISA and the cell-type-specific localization by immunohistochemistry in bovine kidney cortex. Many immunohistochemical studies have addressed the question of PrP c expression in various animals and organs and, recently, PrP c has been found to be expressed not only by neurons but also by several non-neuronal tissues (Bounias and Purdey 2002;Brown et al 2000;Burthem et al 2001;Ford et al 2000;Fournier et al 1998;Horiuchi et al 1995). The physiological function of PrP c is largely unknown.…”

Section: Discussionmentioning

confidence: 99%

Prion protein expression in bovine podocytes and extraglomerular mesangial cells

et al. 2006

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The cellular form of the prion protein (PrP(c)) is thought to be a substrate for an abnormal isoform of the prion protein (PrP(sc)). One emerging hypothesis is that the proposed conversion phenomenon takes place at the site at which the infectious agent meets PrP(c). PrP(c) is abundant in the central nervous system, but little is known about the cell-type-specific distribution of PrP(c) in non-neuronal tissues of cattle. We have studied whether PrP(c), a protein found predominantly in neurons, also exists in bovine podocytes, since neurons and podocytes share a large number of similarities. We have therefore examined the expression of PrP(c) by immunohistochemistry, reverse transcription/polymerase chain reaction and enzyme-linked immunosorbent analysis. Immunostained serial sections and specific antibodies against PrP(c) have revealed that PrP(c) is selectively localized in podocytes and is particularly strongly expressed in extraglomerular mesangial cells but not in endothelial or intraglomerular mesangial cells. The selective expression of PrP(c) in podocytes is of special importance, as it suggests that these cells represent possible targets for peripheral infection with prions and demonstrates that PrP(c) can be added to the list of neuronal factors expressed in mammalian podocytes.

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Section: Discussionmentioning

confidence: 99%

Prion protein expression in bovine podocytes and extraglomerular mesangial cells

et al. 2006

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“…For this purpose we have investigated the expression of PrP c specific mRNAs by Many immunohistochemical studies have addressed the question of PrP c expression in different animals and different organs and in recent years, it has been found that PrP c is not only expressed by neurons but also by several nonneuronal tissues (Horiuchi et al 1995;Fournier et al 1998;Ford et al 2000;Brown et al 2000;Burthem et al 2001;Bounias and Purdey 2002).…”

Section: Discussionmentioning

confidence: 99%

The normal cellular prion protein (PrPc) is strongly expressed in bovine endocrine pancreas

Amselgruber

Büttner

Schlegel

et al. 2005

Histochem Cell Biol

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Expression of the cellular prion protein (PrP(c)) has been shown to be crucial for the development of transmissible spongiform encephalopathies and for the accumulation of the disease-associated conformer (PrP(sc)) in the brain and other tissues. One of the emerging hypotheses is that the conversion phenomenon could take place at the site where the infectious agent meets PrP(c). In this work we have studied whether PrP(c), a protein found predominantly in neurons, could also exist in pancreatic endocrine cells since neuroectoderm-derived cells and pancreatic islet cells share a large number of similarities. For this purpose we have examined the expression of PrP(c) in a series of fetal and postnatal bovine pancreatic tissue by immunohistochemistry and RT-PCR. Using immunostained serial sections and specific antibodies against bovine PrP(c), insulin, glucagon, somatostatin, chromogranin A and chromogranin B we found that PrP(c) is highly expressed in all endocrine cells of fetal and adult pancreatic islets with a particular strong expression in A-cells. Moreover it became evident that the PrP(c) gene-neighbour chromogranin B as well as chromogranin A are coexpressed together with PrP(c). The selective expression of PrP(c) in the bovine endocrine pancreas is of particular importance regarding possible iatrogenic transmission routes and demonstrates also that bovine pancreatic islet cells could represent an interesting model to study the control of PrP-gene expression.

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“…Public sensitivity to BSE has become intense due to the European outbreak of bovine spongiform encephalopathy (BSE) in the 1980s and 1990s [1]–[4]. Ensuing cases of a variant form of Creutzfeldt-Jakob disease (vCJD) in humans began appearing, and has been largely attributed to the consumption of tainted products from BSE infected cattle [1], [2], [5]. Concerns over BSE are also exacerbated due to the obscure nature of infection and transmissibility through food consumption [5], [6].…”

Section: Introductionmentioning

confidence: 99%

A Study on the Analytical Sensitivity of 6 BSE Tests Used by the Canadian BSE Reference Laboratory

2011

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Bovine spongiform encephalopathy (BSE) surveillance programs have been employed in numerous countries to monitor BSE prevalence and to protect animal and human health. Since 1999, the European Commission (EC) authorized the evaluation and approval of 20 molecular based tests for the rapid detection of the pathological prion protein (PrPsc) in BSE infection. The diagnostic sensitivity, convenience, and speed of these tests have made molecular diagnostics the preferred method for BSE surveillance. The aim of this study was to determine the analytical sensitivity of 4 commercially available BSE rapid-test kits, including the Prionics®-Check WESTERN, the Prionics® Check-PrioSTRIP™, the BioRad® TeSeE™ ELISA, and the IDEXX® HerdChek™ EIA. Performances of these tests were then compared to 2 confirmatory tests, including the BioRad® TeSeE™ Western Blot and the modified Scrapie Associated Fibrils (SAF)/OIE Immunoblot. One 50% w/v homogenate was made from experimentally generated C-type BSE brain tissues in ddH2O. Homogenates were diluted through a background of BSE-negative brainstem homogenate. Masses of both positive and negative tissues in each dilution were calculated to maintain the appropriate tissue amounts for each test platform. Specific concentrated homogenization buffer was added accordingly to maintain the correct buffer condition for each test. ELISA-based tests were evaluated using their respective software/detection platforms. Blot-protocols were evaluated by manual measurements of blot signal density. Detection limitations were determined by fitted curves intersecting the manufacturers' positive/negative criteria. The confirmatory SAF Immunoblot displayed the highest analytical sensitivity, followed by the IDEXX® HerdChek™ EIA, Bio-Rad® TeSeE™ Western Blot, the Bio-Rad® TeSeE™ ELISA, Prionics®-Check PrioSTRIP™, and Prionics®-Check WESTERN™, respectively. Although the tests performed at different levels of sensitivity, the most sensitive and least sensitive of the rapid tests were separated by 2 logs in analytical sensitivity, meeting European performance requirements. All rapid tests appear suitable for targeted BSE surveillance programs, as implemented in Canada.

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Transmissible spongiform encephalopathies: a family of etiologically complex diseases—a review

Cited by 18 publications

References 131 publications

Prion protein expression in bovine podocytes and extraglomerular mesangial cells

Prion protein expression in bovine podocytes and extraglomerular mesangial cells

The normal cellular prion protein (PrPc) is strongly expressed in bovine endocrine pancreas

A Study on the Analytical Sensitivity of 6 BSE Tests Used by the Canadian BSE Reference Laboratory

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