NR AXHO
AU Acin,C.; Monleon,E.; Monzon,M.; Bolea,R.; Vargas,A.; Badiola,J.J.
TI Studies on Pathogenesis of Spanish Goat Scrapie Analyzing PRPsc Distribution by Immunohistochemistry
QU International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Pathology and Pathogenesis P03.26
IA http://www.prion2007.com/pdf/Prion Book of Abstracts.pdf
PT Konferenz-Poster
AB Scrapie is a transmissible spongiform encephalopathy (TSE) that causes a neurodegenerative disorder in sheep and goats. Either in both species, an abnormal form of the prion protein (PrPsc) accumulates in nervous and lymphoid tissues during the pathogenesis of the disease. In addition, it has been described the accumulation of PrPsc in other barrier limiting tissues as kidney or endocrine functional organs as adrenal gland. In this study, histopathological and immunohistochemical analysis has been performed in different target tissues (central and peripheral nervous systems) and several organs well known as target for replication (lymphoreticular system) or not well determined their importance on goat scrapie pathogenesis (heart, skin, kidney, urinary bladder, lung, liver, alimentary tract, pancreas, mammary gland, muscle and endocrine tissues) of three natural scrapie affected goats. In most of the animals, PrPsc can be detected in the ileal Peyer path and mesenteric lymph nodes. Later on, it can be detected in gut-associated and peripheral lymphoid tissue. The results seem to show that PrPsc propagation and distribution pass through lymphoreticular system followed by axonal transport detecting PrPsc in peripheral and central nervous system. As a last stage, PrPsc can be detected as perivascular deposits in the central nervous system, suggesting a possible haematogenous dissemination of the disease. Other localizations were reticular and fascicular zones of the adrenal gland, suggesting either haematogenous or axonal propagation of PrPsc. We have also sequence the complete open reading frame of the PRNP gene, founding polymorphisms in 18, 138, 154 and 211 codons.
AD C. Acin, E. Monleon, M. Monzon, R. Bolea, A. Vargas, J.J. Badiola, University of Zaragoza, Centro de Investigación en Enfermedades Prionicas, Spain
SP englisch
PO Schottland