{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T02:37:33Z","timestamp":1767926253595,"version":"3.49.0"},"reference-count":44,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2014,3,13]],"date-time":"2014-03-13T00:00:00Z","timestamp":1394668800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Neuropathology Appl Neurobio"],"published-print":{"date-parts":[[2014,4]]},"abstract":"<jats:sec><jats:title>Aims<\/jats:title><jats:p>Naturally occurring transmissible spongiform encephalopathies (<jats:styled-content style=\"fixed-case\">TSEs<\/jats:styled-content>) accumulate disease\u2010specific forms of prion protein on cell membranes in association with pathognomonic lesions. We wished to determine whether synthetic prion protein disorders recapitulated these and other subcellular <jats:styled-content style=\"fixed-case\">TSE<\/jats:styled-content>\u2010specific changes.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p><jats:styled-content style=\"fixed-case\">SSLOW<\/jats:styled-content> is a <jats:styled-content style=\"fixed-case\">TSE<\/jats:styled-content> initiated with refolded synthetic prion protein. Five terminally sick hamsters previously intracerebrally inoculated with third passage <jats:styled-content style=\"fixed-case\">SSLOW<\/jats:styled-content> were examined using light and immunogold electron microscopy.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p><jats:styled-content style=\"fixed-case\">SSLOW<\/jats:styled-content>\u2010affected hamsters showed widespread abnormal prion protein (<jats:styled-content style=\"fixed-case\">PrP<jats:sup>SSLOW<\/jats:sup><\/jats:styled-content>) and amyloid plaques. <jats:styled-content style=\"fixed-case\">PrP<jats:sup>SSLOW<\/jats:sup><\/jats:styled-content> accumulated on plasma lemmas of neurites and glia without pathological changes. <jats:styled-content style=\"fixed-case\">PrP<jats:sup>SSLOW<\/jats:sup><\/jats:styled-content> also colocalized with increased coated vesicles and pits, coated spiral membrane invaginations and membrane microfolding. <jats:styled-content style=\"fixed-case\">PrP<jats:sup>SSLOW<\/jats:sup><\/jats:styled-content> was additionally observed in lysosomes of microglial cells but not of neurones or astrocytes.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusions<\/jats:title><jats:p><jats:styled-content style=\"fixed-case\">PrP<jats:sup>SSLOW<\/jats:sup><\/jats:styled-content> is propagated by cell membrane conversion of normal <jats:styled-content style=\"fixed-case\">PrP<\/jats:styled-content> and lethal disease may be linked to the progressive growth of amyloid plaques. Cell membrane changes present in <jats:styled-content style=\"fixed-case\">SSLOW<\/jats:styled-content> are indistinguishable from those of naturally occurring <jats:styled-content style=\"fixed-case\">TSEs<\/jats:styled-content>. However, some lesions found in <jats:styled-content style=\"fixed-case\">SSLOW<\/jats:styled-content> are absent in natural animal <jats:styled-content style=\"fixed-case\">TSEs<\/jats:styled-content> and vice versa. <jats:styled-content style=\"fixed-case\">SSLOW<\/jats:styled-content> may not entirely recapitulate neuropathological features previously described for natural disease. End\u2010stage neuropathology in <jats:styled-content style=\"fixed-case\">SSLOW<\/jats:styled-content>, particularly the nature and distribution of amyloid plaques may be significantly influenced by the early redistribution of seeds within the inoculum and its recirculation following interstitial, perivascular and other drainage pathways. The way in which seeds are distributed and aggregate into plaques in <jats:styled-content style=\"fixed-case\">SSLOW<\/jats:styled-content> has significant overlap with murine <jats:styled-content style=\"fixed-case\">APP<\/jats:styled-content> overexpressing mice challenged with <jats:styled-content style=\"fixed-case\">A<\/jats:styled-content>\u03b2.<\/jats:p><\/jats:sec>","DOI":"10.1111\/nan.12053","type":"journal-article","created":{"date-parts":[[2013,4,12]],"date-time":"2013-04-12T08:44:37Z","timestamp":1365756277000},"page":"296-310","source":"Crossref","is-referenced-by-count":26,"title":["Pathology of <scp>SSLOW<\/scp>, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongiform encephalopathies"],"prefix":"10.1111","volume":"40","author":[{"given":"M.","family":"Jeffrey","sequence":"first","affiliation":[{"name":"Animal Health and Veterinary Laboratories Agency Lasswade Laboratory  Bush Loan Penicuik Midlothian UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"McGovern","sequence":"additional","affiliation":[{"name":"Animal Health and Veterinary Laboratories Agency Lasswade Laboratory  Bush Loan Penicuik Midlothian UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"N.","family":"Makarava","sequence":"additional","affiliation":[{"name":"Centre for Biomedical Engineering and Technology University of Maryland School of Medicine  Baltimore MD USA"},{"name":"Department of Anatomy and Neurobiology University of Maryland School of Medicine  Baltimore MD USA"},{"name":"Department of Neurology University of Maryland School of Medicine  Baltimore MD USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L.","family":"Gonz\u00e1lez","sequence":"additional","affiliation":[{"name":"Animal Health and Veterinary Laboratories Agency Lasswade Laboratory  Bush Loan Penicuik Midlothian UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Y.\u2010S.","family":"Kim","sequence":"additional","affiliation":[{"name":"Hallym University  Anyang Gyeonggi\u2010do Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R. 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